TNA Peri

Indications

• Fluid and electrolyte imbalances
• Hypoglycemia
• Nutritional supplementation
• Diabetic emergencies

Dosage

Children: Refer to the BNF for Children for appropriate paediatric dosing guidelines.

Adults: The dosage varies based on the clinical condition and specific formulation used. For intravenous administration, consult product literature for precise dosing.

Mechanism of action

Glucose supplies energy to tissues by undergoing glycolysis, which begins with its phosphorylation by hexokinase to form glucose 6-phosphate. This activates glucose for breakdown, ultimately generating ATP and NADH. The aerobic metabolism of glucose can yield up to 36 ATP molecules. Glucose also serves as a precursor for other biomolecules and regulates various physiological processes including gene transcription and hormone secretion.

Pharmacodynamics

Glucose is an obligatory energy source for cellular activities and plays a significant role in metabolic signaling. It is oxidized to yield energy through glycolysis, the citric acid cycle, and oxidative phosphorylation. Glucose can be converted into fat for energy storage and is stored as glycogen in the liver and muscles. Its administration increases blood glucose levels and stimulates insulin secretion, particularly through oral routes that activate gut incretin hormones.

Pharmacokinetics

Glucose is rapidly absorbed from the gastrointestinal tract or directly into the bloodstream when administered intravenously. It is distributed widely throughout the body and metabolized primarily in tissues requiring energy. The body maintains glucose homeostasis through regulatory mechanisms involving insulin and glucagon. Excess glucose can be stored as glycogen or converted to triglycerides for long-term energy storage.

Adverse effects

• Hyperglycemia
• Increased osmolarity
• Fluid overload
• Electrolyte imbalances

Interactions

• Insulin - may require dose adjustments

Precautions

• Use with caution in patients with diabetes mellitus
• Monitor blood glucose levels in patients receiving parenteral glucose
• Adjust dosage in renal impairment

Pregnancy

Glucose is generally considered safe in pregnancy; however, monitoring is advised, especially in diabetic patients.

Breast-feeding

Glucose is considered safe during breastfeeding, as it is a natural sugar found in breast milk.

Storage

Store at room temperature, away from light. Avoid freezing.

Formulations

• Glucose 5% solution for infusion
• Glucose 10% solution for infusion
• Glucose 0.9% solution for injection
• Glucose sodium chloride combination solutions

Indications

• Bladder irrigation during urological surgery
• Irrigation for transurethral resection of the prostate gland
• Irrigation for bladder tumors

Dosage

Children: Refer to the BNF for Children for pediatric dosing guidelines.

Adults: Refer to the product literature for specific dosing information.

Mechanism of action

Glycine binds to strychnine-sensitive and strychnine-insensitive glycine receptors in the central nervous system. The strychnine-sensitive receptor is a chloride channel that enhances inhibitory neurotransmission. This action may contribute to glycine's potential antispastic effects. Additionally, glycine potentiates NMDA receptor-mediated neurotransmission, which may have implications in managing certain neurological conditions, such as neuroleptic-resistant negative symptoms in schizophrenia.

Pharmacodynamics

Glycine plays a crucial role in various biological functions, including energy metabolism and immune response. It is involved in hormone synthesis and helps in modulating neurotransmitter release, particularly in inhibitory pathways. Glycine's ability to enhance chloride conductance in neurons contributes to its antispastic properties and its potential to mitigate oxidative stress in immune responses.

Pharmacokinetics

Glycine is absorbed readily in the gastrointestinal tract and is utilized by the body for protein synthesis and other metabolic functions. The distribution of glycine in the body is widespread, as it is present in various tissues. Glycine is metabolized in the liver and other tissues, with excretion primarily occurring via the kidneys. The pharmacokinetics of glycine can be influenced by factors such as age, renal function, and overall health status.

Adverse effects

• Fluid overload
• Electrolyte imbalance
• Nausea
• Vomiting
• Headache
• Hypotension

Precautions

• Monitor for signs of fluid overload during irrigation
• Use caution in patients with pre-existing electrolyte imbalances
• Careful consideration in patients with renal impairment

Pregnancy

Glycine is generally considered safe for use during pregnancy when used as an irrigation solution, but risks should be discussed with a healthcare provider.

Breast-feeding

Glycine is likely safe during breastfeeding, but limited data is available. Consultation with a healthcare professional is advisable.

Storage

Store in a cool, dry place. Protect from light. Do not freeze.

Formulations

• Glycine 1.5% irrigation solution 3 litre Easyflow bags
• Glycine 1.5% irrigation solution 1 litre Flowfusor bottles
• Glycine 1.5% irrigation solution 1 litre Easyflow bags
• Glycine 1.5% irrigation solution 2 litre Flowfusor bottles

Indications

• Support for cognitive function
• Enhancement of mental performance
• Management of stress-related fatigue

Dosage

Children: Refer to BNF for Children for appropriate dosing guidelines.

Adults: Refer to BNF for specific dosing recommendations.

Mechanism of action

Acetyltyrosine is believed to enhance the synthesis of catecholamines by providing a more bioavailable form of tyrosine. This may lead to increased levels of dopamine and norepinephrine in the brain, which can improve mood, cognitive function, and stress response.

Pharmacodynamics

As a precursor to neurotransmitters, acetyltyrosine may enhance mental performance and cognitive function. It is particularly noted for its ability to mitigate the effects of stress and fatigue on mental alertness and clarity.

Pharmacokinetics

Acetyltyrosine is rapidly absorbed from the gastrointestinal tract. Its half-life, distribution, and metabolism details are not well characterized, but it is expected to undergo hydrolysis to release tyrosine, which then participates in neurotransmitter synthesis. The renal excretion pathway is presumed to be involved in eliminating metabolites.

Pregnancy

There is limited data available on the use of acetyltyrosine during pregnancy. Caution is advised.

Breast-feeding

There is insufficient information regarding the excretion of acetyltyrosine in human milk. Caution is recommended.

Storage

Store in a cool, dry place away from light. Keep out of reach of children.

Formulations

• {'formulation': 'Tablets', 'strength': '500 mg'}
• {'formulation': 'Capsules', 'strength': '250 mg'}

Dosage

Children: Refer to specific drug guidelines for paediatric dosing.

Adults: Refer to specific drug guidelines for adult dosing.

Pregnancy

The safety of chain during pregnancy has not been established. It should only be used if the potential benefit justifies the potential risk to the fetus.

Breast-feeding

It is unknown whether chain is excreted in human milk. Caution should be exercised when administering to breastfeeding women.

Storage

Store in a cool, dry place away from light. Keep out of reach of children.

Indications

• Energy production
• Support for muscle metabolism
• Immune system enhancement
• Regulation of blood sugar levels

Dosage

Children: Refer to the BNF for Children for specific dosing guidelines.

Adults: Refer to the BNF for specific dosing guidelines.

Mechanism of action

L-Alanine is produced from pyruvate through transamination. It serves as an important energy source, particularly during prolonged exercise, where branched-chain amino acids (BCAAs) are utilized by muscle cells. The nitrogen component of BCAAs forms alanine, which is then converted into glucose by the liver, aiding in energy production and blood sugar regulation.

Pharmacodynamics

L-Alanine is crucial for energy production in muscle, brain, and central nervous system tissues. It strengthens the immune system by facilitating antibody production and plays an essential role in the metabolism of sugars and organic acids.

Pharmacokinetics

L-Alanine is readily available in the plasma and is utilized by various tissues for metabolic processes. It is produced endogenously and can also be derived from dietary sources. The dynamics of its metabolism involve conversion to glucose and participation in several metabolic pathways, including biotin metabolism and tRNA charging.

Pregnancy

L-Alanine is generally regarded as safe, but consult a healthcare professional before use during pregnancy.

Breast-feeding

L-Alanine is considered safe during breastfeeding, but it is advisable to consult a healthcare professional.

Storage

Store in a cool, dry place away from direct sunlight. Keep out of reach of children.

Formulations

• L-Alanine powder
• L-Alanine capsules
• L-Alanine tablets

Indications

• Cardiovascular diseases
• Erectile dysfunction
• Peripheral arterial disease
• Wound healing
• Muscle growth and recovery
• Immune system support

Dosage

Children: For paediatric dosing, it is important to refer to the BNF for Children for appropriate guidelines based on the child's age, weight, and clinical condition.

Adults: The typical dosage for adults varies based on the condition being treated, but common oral doses range from 2 to 30 grams per day, divided into multiple doses. For specific dosing recommendations, please refer to the BNF.

Mechanism of action

L-arginine is converted to nitric oxide by nitric oxide synthase (NOS), which is crucial for vascular function and blood flow regulation. NO activates guanylate cyclase, leading to increased levels of cyclic GMP, a secondary messenger that mediates vasodilation and other cellular responses. This pathway is vital in both the cardiovascular and immune systems, with different isoforms of NOS (eNOS, nNOS, iNOS) contributing to various physiological effects.

Pharmacodynamics

L-arginine has been shown to enhance immune responses, improve wound healing, stimulate growth hormone release, and support muscle hypertrophy and tissue repair. Its role in nitric oxide production aids in vasodilation, improving blood circulation and oxygen delivery to tissues, which is essential for recovery and regeneration.

Pharmacokinetics

L-arginine is absorbed from the gastrointestinal tract, with peak plasma concentrations occurring within 1-2 hours after oral administration. It is metabolized primarily in the liver and kidneys, with a half-life of approximately 1-2 hours. The bioavailability of L-arginine can be influenced by dietary intake and metabolic conditions.

Adverse effects

• Gastrointestinal disturbances
• Nausea
• Diarrhea
• Abdominal pain
• Hypotension
• Allergic reactions

Interactions

• Antihypertensive agents may have additive effects leading to increased hypotension
• Sildenafil and other medications for erectile dysfunction may have enhanced effects when used with L-arginine

Precautions

• Caution in patients with a history of asthma or allergies
• Use with caution in patients with hypotension
• Monitor blood pressure in patients taking antihypertensive medications

Pregnancy

The safety of L-arginine in pregnancy has not been established. Consult a healthcare provider before use.

Breast-feeding

L-arginine is excreted in breast milk, and its safety during breastfeeding is not well established. Consult a healthcare provider.

Storage

Store in a cool, dry place away from direct sunlight. Keep out of reach of children.

Formulations

• Oral tablets
• Powder for oral solution
• Capsules

Indications

• Rheumatoid arthritis
• Allergic diseases
• Ulcers
• Anemia

Dosage

Children: Refer to the BNF for Children for specific dosing recommendations.

Adults: Refer to the BNF for specific dosing guidelines.

Mechanism of action

The exact actions of supplemental L-histidine are not fully understood, but it is postulated to have immunomodulatory and antioxidant properties. It serves as the precursor for histamine, which can enhance suppressor T cell activity and potentially down-regulate the production of reactive oxygen species in immune cells. This may confer benefits in conditions like rheumatoid arthritis, where oxidative stress is a concern.

Pharmacodynamics

L-histidine is abundant in hemoglobin and contributes to various bodily functions. It has been clinically associated with treating rheumatoid arthritis, allergic diseases, ulcers, and anemia. Deficiencies in L-histidine can lead to complications such as impaired hearing. Its metabolites, particularly histamine, exhibit immunomodulatory effects and antioxidant capabilities.

Pharmacokinetics

L-histidine is absorbed through the gastrointestinal tract, and its bioavailability can be influenced by dietary intake. Once ingested, it is incorporated into proteins and utilized in various metabolic pathways, including histidine biosynthesis and tRNA charging. The metabolism of L-histidine involves its conversion to histamine, which subsequently participates in numerous physiological processes.

Pregnancy

There is limited data on the use of L-histidine during pregnancy. Consult healthcare professionals.

Breast-feeding

Limited information is available on the excretion of L-histidine in human milk. Consult healthcare professionals before use.

Storage

Store in a cool, dry place, away from direct sunlight. Keep out of reach of children.

Formulations

• L-histidine powder
• L-histidine capsules
• L-histidine tablets

Indications

• Protein supplementation in athletes
• Muscle recovery post-injury
• Support in conditions causing muscle wasting
• Management of metabolic disorders such as phenylketonuria

Dosage

Children: Refer to the BNF for Children for specific paediatric dosing guidelines.

Adults: Refer to the BNF for specific adult dosing guidelines.

Mechanism of action

Leucine undergoes catabolism primarily in muscle tissue, where it is transaminated by branched-chain amino acid aminotransferase, resulting in the formation of various keto acids. These products are further oxidized by branched-chain alpha-keto acid dehydrogenase, leading to the production of acetyl-CoA and acetoacetyl-CoA, classifying leucine as a strictly ketogenic amino acid. The metabolic pathways diverge thereafter, producing multiple intermediates necessary for various physiological functions.

Pharmacodynamics

As an essential amino acid, leucine aids in the regulation of blood sugar levels, supports muscle tissue growth and repair, enhances growth hormone production, and promotes wound healing. It is also known to help prevent muscle protein breakdown that can occur after physical trauma or stress. Leucine may have therapeutic potential for individuals with metabolic disorders such as phenylketonuria, where amino acid metabolism is impaired.

Pharmacokinetics

Leucine is absorbed in the intestines after dietary intake and is transported to tissues where it is utilized. Its bioavailability is influenced by dietary composition and the presence of other amino acids. Once in the muscle tissue, leucine is readily catabolized to produce energy substrates, contributing to muscle metabolism and repair processes. The half-life and excretion routes of leucine are not extensively documented but are primarily through urine in the form of metabolites.

Pregnancy

Leucine is considered safe during pregnancy when consumed in normal dietary amounts. However, high doses should be avoided unless prescribed by a healthcare professional.

Breast-feeding

Leucine is also considered safe during breastfeeding when taken in dietary amounts. High doses should be approached with caution and discussed with a healthcare provider.

Storage

Store in a cool, dry place, away from direct sunlight. Keep out of reach of children.

Formulations

• Capsule
• Tablet
• Powder

Indications

• Supplementation for athletes to enhance performance
• Support for muscle recovery post-exercise
• Management of protein malnutrition
• Potential role in metabolic disorders

Dosage

Children: Refer to specific guidelines or consult a healthcare professional for appropriate dosing.

Adults: Refer to specific guidelines or consult a healthcare professional for appropriate dosing.

Mechanism of action

L-isoleucine functions primarily as a substrate for protein synthesis and is involved in various metabolic pathways. It is converted into acetyl-CoA and succinyl-CoA, which are crucial for energy production through the citric acid cycle. Additionally, isoleucine can stimulate insulin secretion and improve glucose uptake in muscle cells, thereby playing a role in regulating blood sugar levels.

Pharmacodynamics

As an essential amino acid, L-isoleucine contributes to protein synthesis and muscle repair. It also has a role in energy metabolism and can be utilized by skeletal muscle as an energy source during exercise. Its ability to promote muscle recovery and reduce muscle soreness is well-documented, making it popular among athletes. Furthermore, it may enhance immune function by modulating the activity of immune cells.

Pharmacokinetics

L-isoleucine is absorbed in the gastrointestinal tract and is transported to tissues via the bloodstream. It is metabolized primarily in the liver and muscle tissues, where it undergoes transamination and deamination. The elimination half-life of L-isoleucine is relatively short, necessitating regular intake to maintain adequate levels in the body. The time to peak plasma concentration is typically within a few hours after ingestion.

Adverse effects

• Gastrointestinal disturbances
• Allergic reactions
• Fatigue
• Headache

Precautions

• Use with caution in individuals with metabolic disorders
• Monitor for potential allergic reactions

Pregnancy

The safety of isoleucine during pregnancy has not been extensively studied. Consult a healthcare provider before use.

Breast-feeding

Isoleucine is considered safe during breastfeeding but should be used under medical supervision.

Storage

Store in a cool, dry place, away from direct sunlight. Keep out of reach of children.

Formulations

• Powder
• Capsules
• Tablets

Indications

• Herpes simplex virus infections
• Lysine deficiency
• Support in calcium absorption
• Collagen synthesis

Dosage

Children: Refer to the BNF for Children for specific paediatric dosing guidelines.

Adults: Refer to the BNF for specific adult dosing guidelines.

Mechanism of action

Lysine inhibits the replication of herpes simplex virus by altering the amino acid ratio in tissues, particularly decreasing the availability of L-arginine which the virus requires for replication. Additionally, lysine is involved in protein synthesis where it binds with transfer RNA (tRNA) to facilitate the translation process that produces specific proteins.

Pharmacodynamics

Lysine ensures the adequate absorption of calcium, supports collagen formation which is essential for bone, cartilage, and connective tissues, and aids in the production of antibodies, hormones, and enzymes. A deficiency in lysine can lead to various health issues including fatigue, concentration difficulties, irritability, and reproductive problems.

Pharmacokinetics

Lysine is rapidly absorbed from the gastrointestinal tract. It is distributed throughout the body and is primarily excreted via the kidneys. The half-life and detailed metabolic pathways of lysine can vary based on individual physiological conditions and dietary intake.

Adverse effects

• Gastrointestinal disturbances
• Abdominal pain
• Nausea
• Diarrhea

Precautions

• Use with caution in individuals with kidney disease
• Monitor for gastrointestinal effects

Pregnancy

L-lysine is generally considered safe during pregnancy, but clinical advice should be sought.

Breast-feeding

L-lysine is excreted in breast milk, but is typically deemed safe during breastfeeding.

Storage

Store in a cool, dry place away from direct sunlight.

Formulations

• Tablets
• Capsules
• Powder

Indications

• Hepatotoxicity prevention, particularly related to acetaminophen overdose
• Cholesterol management
• Support for hair, skin, and nail health
• Heavy metal chelation
• Kidney function support

Mechanism of action

The exact mechanism of action of L-methionine's anti-hepatotoxic activity is not fully understood. It is believed that L-methionine metabolism may counteract the depletion of hepatic glutathione caused by high doses of acetaminophen, thereby reducing oxidative stress. Additionally, L-methionine and its metabolites may exhibit free-radical scavenging activity due to the presence of sulfur, which contributes to its potential antioxidant effects. L-methionine also plays a role in protein synthesis by binding with transfer RNA (tRNA) in the cytoplasm to facilitate the translation of mRNA into proteins.

Pharmacodynamics

L-methionine serves as a primary source of sulfur, which is vital for preventing disorders affecting hair, skin, and nails. It helps lower cholesterol levels by promoting the liver's production of lecithin, reduces liver fat, and may protect the kidneys. As a natural chelating agent, it aids in the detoxification of heavy metals and influences the formation of ammonia, leading to ammonia-free urine that minimizes bladder irritation. Furthermore, it is thought to promote hair growth and exhibit antioxidant properties.

Pharmacokinetics

L-methionine is absorbed in the gastrointestinal tract and subsequently distributed throughout the body. It undergoes metabolic conversion primarily in the liver, where it is involved in various pathways, including the biosynthesis of S-adenosyl-L-methionine and the regulation of one-carbon metabolism. The elimination of L-methionine occurs through metabolic pathways and is dependent on the body's protein synthesis needs.

Adverse effects

• Gastrointestinal disturbances
• Allergic reactions
• Nausea
• Vomiting

Precautions

• Use with caution in patients with renal impairment
• Not recommended for use in patients with known hypersensitivity to methionine

Pregnancy

There is limited data on the use of L-methionine during pregnancy. Consult a healthcare provider before use.

Breast-feeding

Limited information is available. Consult a healthcare provider before use while breastfeeding.

Storage

Store in a cool, dry place away from direct sunlight. Keep out of reach of children.

Formulations

• Tablets
• Capsules
• Powder

Indications

• Nutritional supplementation
• Support for wound healing
• Enhancement of immune function
• Potential adjunct therapy in conditions of stress or injury

Dosage

Children: Refer to the BNF for Children for specific dosage guidelines.

Adults: Refer to the BNF for specific dosage guidelines.

Mechanism of action

L-Ornithine is metabolised to L-arginine, which stimulates the pituitary gland to release growth hormone. This metabolic conversion is crucial during states of injury or stress when L-arginine levels may be insufficient for normal immune function and protein synthesis. Through its action on L-arginine metabolism, Lornithine may exert immunomodulatory and wound-healing effects.

Pharmacodynamics

As a non-essential amino acid, Lornithine is vital for protein, enzyme, and muscle tissue production. It is integral to the urea cycle, aiding in nitrogen disposal. Furthermore, Lornithine is involved in the synthesis of polyamines like putrescine and spermine, which are important for cell growth and function. It is also associated with enhancing growth hormone release and may contribute to fat metabolism.

Pharmacokinetics

The pharmacokinetics of Lornithine are not extensively detailed in the literature, but as a metabolite, it is likely absorbed through the gastrointestinal tract and subsequently distributed throughout the body where it participates in metabolic pathways. The synthesis of L-arginine from L-ornithine occurs primarily in the liver, and its effects may vary based on individual metabolic states and dietary intake.

Pregnancy

There are no adequate studies on the use of lornithine in pregnant women. It should be used only if clearly needed.

Breast-feeding

It is unknown whether lornithine is excreted in human milk. Caution should be exercised when administering to a nursing mother.

Storage

Store in a cool, dry place, away from direct sunlight. Keep out of reach of children.

Indications

• Depression
• Phenylketonuria (PKU)
• Vitiligo

Dosage

Children: Refer to the BNF for Children for specific dosing guidelines.

Adults: Refer to the BNF for specific dosing guidelines.

Mechanism of action

The supposed antidepressant effects of L-phenylalanine may be due to its role as a precursor in the synthesis of the neurotransmitters norepinephrine and dopamine. Elevated levels of these neurotransmitters are associated with antidepressant effects. Furthermore, L-phenylalanine may stimulate melanin production in affected skin, which is believed to contribute to its potential antivitiligo activity.

Pharmacodynamics

L-phenylalanine is utilized by the brain to produce norepinephrine, a neurotransmitter that facilitates signal transmission between nerve cells, enhances alertness, reduces hunger, functions as an antidepressant, and may help improve memory.

Pharmacokinetics

L-phenylalanine is absorbed in the gastrointestinal tract and enters the bloodstream, where it is transported to various tissues. It is incorporated into proteins through the process of translation, which is regulated by the availability of transfer RNA (tRNA) and messenger RNA (mRNA). The half-life and metabolism of L-phenylalanine in humans can vary based on dietary intake and individual metabolic rates.

Pregnancy

L-phenylalanine should be used during pregnancy only if clearly needed. Consult healthcare provider before use.

Breast-feeding

L-phenylalanine is excreted in breast milk. Caution is advised when administering to nursing mothers.

Storage

Store at room temperature, away from moisture and heat.

Indications

• Supplementation for collagen synthesis
• Support for connective tissue repair
• Assistance in joint and tendon health
• Support for skin health and repair
• Potential benefits in heart muscle function

Dosage

Children: Refer to the BNF for Children for appropriate dosing guidelines for paediatric patients.

Adults: Refer to the BNF for specific dosing recommendations based on clinical context and individual patient needs.

Mechanism of action

L-Proline is oxidized in the kidney by L-Proline oxidase to form L-Glutamic acid. This process involves the ring-opening of L-Proline, leading to the production of L-Ornithine and L-Glutamic acid, which can be converted back to L-Proline via L-Glutamic acid-gamma-semialdehyde. Its presence in collagen underscores its importance in connective tissue health.

Pharmacodynamics

L-Proline is a major component of cartilage and is crucial for maintaining youthful skin. It assists in the repair of muscle and connective tissue damage and is essential for immune function. Furthermore, L-Proline is important for the structural integrity and functioning of joints and tendons, and plays a significant role in the maintenance and strengthening of heart muscles.

Pharmacokinetics

L-Proline is readily absorbed and utilized by the body, with its metabolism primarily occurring in the kidneys and liver. It participates in various metabolic pathways, including proline metabolism and tRNA charging, facilitating protein synthesis and amino acid balance. The bioavailability and turnover rates can vary based on dietary intake and physiological conditions.

Pregnancy

Consult with a healthcare professional before use, as safety during pregnancy is not well established.

Breast-feeding

Consult with a healthcare professional before use, as safety during breastfeeding is not well established.

Storage

Store in a cool, dry place away from direct sunlight. Keep out of reach of children.

Formulations

• L-Proline powder
• L-Proline capsules
• L-Proline tablets

Indications

• Support in protein synthesis
• Metabolic disorders involving amino acids
• Potential use in neurological conditions

Dosage

Children: Refer to the BNF for Children for appropriate dosing information.

Adults: Refer to the BNF for specific dosing information as it may vary based on clinical context.

Mechanism of action

L-Serine is converted to glycine by the enzyme serine hydroxymethyltransferase, which results in the formation of one-carbon units necessary for the synthesis of purine bases adenine and guanine. These nucleobases are vital for the formation of DNA and RNA, as well as ATP and GTP, which are crucial for energy production in metabolic pathways.

Pharmacodynamics

As a nutritionally non-essential amino acid, L-Serine is critical for protein, enzyme, and muscle tissue production. It supports the metabolism of fats, fatty acids, and the immune response through antibody production. Additionally, L-Serine is utilized in cosmetics and skin care products for its moisturizing properties.

Pharmacokinetics

L-Serine is absorbed from dietary sources and is also synthesized in the body. It participates in various metabolic pathways, including those related to glycine and cysteine biosynthesis. The dynamics of its absorption, distribution, metabolism, and excretion are influenced by dietary intake and physiological needs.

Pregnancy

There is limited information on the use of L-serine during pregnancy. Consult a healthcare provider for advice.

Breast-feeding

L-serine is generally considered safe during breastfeeding, but consultation with a healthcare provider is advisable.

Storage

Store in a cool, dry place away from light. Keep out of reach of children.

Indications

• Protein synthesis support
• Liver health and function
• Digestive health
• Preventing excessive fat accumulation in the liver
• Potential mental health support

Dosage

Children: Refer to BNF for Children for dosing recommendations.

Adults: Refer to BNF for appropriate dosing guidance.

Mechanism of action

L-Threonine acts as a precursor to glycine and serine, facilitating protein synthesis by binding with transfer RNA (tRNA) in the cytoplasm. This binding is essential for the translation process, where specific proteins are synthesized based on the sequence of nucleotides in messenger RNA (mRNA). L-Threonine also functions as a lipotropic agent, preventing excessive fat accumulation in the liver and enhancing nutrient absorption.

Pharmacodynamics

L-Threonine is vital for maintaining protein balance and is necessary for the formation of collagen, elastin, and tooth enamel. It supports liver function and has lipotropic properties when combined with other amino acids, notably aspartic acid and methionine, aiding in the management of fat metabolism. Its role in protein synthesis is continuous, occurring in most cells throughout the body.

Pharmacokinetics

After ingestion, L-Threonine is absorbed in the gastrointestinal tract and utilized in various metabolic pathways, including amino acid biosynthesis and protein synthesis. The amino acid is distributed in the body as it participates in the synthesis of proteins and other biomolecules, with its bioavailability influenced by dietary intake and the presence of other amino acids.

Pregnancy

L-Threonine is generally considered safe during pregnancy, as it is an essential amino acid necessary for normal physiological functions. However, it is advisable to consult a healthcare provider before use.

Breast-feeding

L-Threonine is likely safe during breastfeeding, as it is a naturally occurring amino acid. Nevertheless, mothers should seek guidance from healthcare professionals regarding its use.

Storage

Store in a cool, dry place away from light. Keep out of reach of children.

Indications

• Insomnia
• Anxiety
• Depression
• Migraine headaches
• Chronic pain
• Obsessive-compulsive disorder
• Seasonal affective disorder
• Nutritional supplementation in infant formulas

Dosage

Adults: Refer to the BNF for specific dosing guidelines.

Mechanism of action

During the catabolism of tryptophan, several important side reactions occur, starting with the action of an iron porphyrin oxygenase that opens the indole ring. Kynurenine, a key intermediate, can be converted into kynurenic acid, which exhibits antiexcitotoxic and anticonvulsant properties. Furthermore, tryptophan is involved in producing nicotinic acid, contributing to NAD+ and NADP+ synthesis, and influencing serotonin turnover, which affects thyroid-stimulating hormone and prolactin release.

Pharmacodynamics

Tryptophan is crucial for synthesizing proteins, enzymes, and neurotransmitters, particularly serotonin and melatonin. It can act as a natural relaxant, alleviating insomnia, reducing anxiety and depression, and potentially alleviating migraine headaches. Additionally, it may help in chronic pain management, decrease impulsivity, and treat obsessive-compulsive disorders. Deficiencies in tryptophan can lead to adverse cardiovascular effects, including coronary artery spasms.

Pharmacokinetics

L-Tryptophan is absorbed in the gastrointestinal tract, with its bioavailability influenced by factors such as dietary composition and the presence of competing amino acids. It is metabolized primarily in the liver, with metabolites entering various metabolic pathways, including kynurenine and serotonin synthesis. The pharmacokinetics of tryptophan are affected by transport mechanisms across cell membranes, particularly within the context of tRNA charging and metabolic pathways related to amino acid catabolism.

Adverse effects

• Nausea
• Dizziness
• Drowsiness
• Dry mouth
• Abdominal pain
• Diarrhea

Precautions

• Use with caution in patients with a history of liver disease
• May interact with other medications that affect serotonin levels

Pregnancy

Safety during pregnancy has not been established; use only if clearly needed.

Breast-feeding

It is unknown if tryptophan is excreted in human milk; caution is advised.

Storage

Store in a cool, dry place away from direct sunlight.

Formulations

• Capsules
• Tablets
• Powder for oral solution

Indications

• Depression
• Stress reduction
• Cognitive enhancement
• Chronic fatigue
• Narcolepsy

Dosage

Children: Refer to the BNF for Children for recommended dosages in paediatric patients.

Adults: Refer to the BNF for specific dosing information, as it varies based on condition and formulation.

Mechanism of action

Tyrosine is produced in cells by hydroxylating phenylalanine. Its antidepressant activity is attributed to its role as a precursor in the synthesis of norepinephrine and dopamine. Elevated levels of these neurotransmitters are believed to contribute to its antidepressant effects.

Pharmacodynamics

L-Tyrosine is critical for synthesizing neurotransmitters, proteins, and enzymes. It can elevate mood, improve cognitive functions, and reduce stress. Its involvement in thyroid hormone production links it to metabolic processes, while deficiencies can manifest in various physiological symptoms, including low blood pressure and body temperature.

Pharmacokinetics

L-Tyrosine is readily absorbed from the gastrointestinal tract. Its metabolism involves conversion to catecholamines via the enzyme tyrosine hydroxylase. It is distributed throughout the body and utilized in protein synthesis as well as neurotransmitter production. The half-life and specific elimination pathways are not well-defined in the provided data.

Adverse effects

• Gastrointestinal disturbances
• Nausea
• Headaches
• Fatigue
• Heartburn

Precautions

• Caution in patients with hyperthyroidism
• Use with caution in patients taking medications for depression

Pregnancy

Limited information is available regarding the safety of L-tyrosine during pregnancy. It is advisable to consult a healthcare professional before use.

Breast-feeding

Limited information is available regarding the safety of L-tyrosine during breastfeeding. Consultation with a healthcare professional is recommended.

Storage

Store in a cool, dry place away from direct sunlight. Keep out of reach of children.

Indications

• Nutritional supplementation for athletes
• Support in muscle recovery post-exercise
• Management of metabolic disorders associated with BCAA catabolism
• Treatment of conditions related to L-valine deficiency

Mechanism of action

L-valine's catabolism initiates in muscle and involves transamination with a single BCAA aminotransferase, producing different a-keto acids that are further oxidized using branched-chain a-keto acid dehydrogenase. Valine primarily yields propionyl-CoA, a glucogenic precursor of succinyl-CoA. This pathway is crucial for energy production and metabolic regulation. L-valine also contributes to the biosynthesis of proteins and hormones, enhancing muscle growth, energy levels, and recovery from exercise.

Pharmacodynamics

As a branched-chain amino acid, L-valine exhibits stimulant activity that promotes muscle growth and tissue repair. It enhances energy levels and endurance, aids in recovery from muscle exertion, and supports the production of growth hormone. Its presence in the diet is essential for maintaining optimal health and preventing deficiencies that may lead to growth impairment, anemia, or neuropathic issues. L-valine should ideally be ingested with isoleucine and leucine in a ratio of 2:1:2 to maximize its benefits.

Pharmacokinetics

L-valine is absorbed in the intestines and utilized by the liver and muscle tissues. It is metabolized primarily in muscle, where it undergoes transamination and subsequent oxidative processes. The metabolic pathways involve the conversion of L-valine to propionyl-CoA, which can enter the citric acid cycle, contributing to ATP generation. The half-life and specific pharmacokinetic parameters of L-valine are not well-documented, emphasizing its dietary role rather than pharmacological use.

Adverse effects

• Gastrointestinal disturbances
• Neurological effects such as drowsiness
• Allergic reactions

Precautions

• Monitor for potential allergic reactions
• Use with caution in patients with metabolic disorders related to amino acid metabolism

Pregnancy

Safety during pregnancy has not been established. Consult a healthcare provider.

Breast-feeding

It is not known whether L-valine is excreted in human milk. Use with caution.

Storage

Store in a cool, dry place away from direct sunlight. Keep out of reach of children.

Formulations

• Powder for oral solution
• Tablets
• Capsules

Dosage

Children: Refer to specific product guidelines as dosage will depend on the type of medium and its intended application.

Adults: Refer to specific product guidelines as dosage will depend on the type of medium and its intended application.

Mechanism of action

The mechanism of action for a medium can vary greatly depending on the specific medium being referenced. Generally, media serve to maintain the stability and viability of cells or organisms during culture, enabling metabolic processes to occur. For instance, nutrient media provide essential nutrients, while selective media may inhibit the growth of certain organisms while promoting others.

Pharmacodynamics

Pharmacodynamics is largely dependent on the type of medium used and its components. In tissue cultures, the medium can influence cell growth, differentiation, and physiological responses. The interactions of cells with their environment are critical for cellular signaling and function.

Pharmacokinetics

Pharmacokinetics is not typically applicable to media in the same way it is for active drugs. However, the absorption and distribution of substances within a medium can affect how well the active ingredients are delivered or how organisms interact with the medium. Factors such as pH, osmolarity, and nutrient concentration can all influence these processes.

Pregnancy

Consult a healthcare provider before use, as the safety of medium in pregnancy has not been established.

Breast-feeding

Consult a healthcare provider before use, as it is unknown whether medium passes into breast milk.

Storage

Store in a cool, dry place, away from direct sunlight and moisture.

Indications

• Cardiovascular health
• Menopausal symptom relief
• Bone health
• Cholesterol management
• Potential cancer risk reduction

Dosage

Children: Refer to specific product guidelines or consult a healthcare professional for appropriate dosage.

Adults: Refer to specific product guidelines or consult a healthcare professional for appropriate dosage.

Mechanism of action

Soybeans contain isoflavones, which are phytoestrogens that can mimic the effects of estrogen in the body. They exert their effects primarily through binding to estrogen receptors and modulating gene expression related to estrogen-responsive pathways. This interaction can influence various physiological processes, including bone density, lipid metabolism, and hormonal balance.

Pharmacodynamics

The pharmacodynamics of soybeans are attributed to their content of isoflavones, notably genistein and daidzein. These compounds may exhibit antioxidant properties, modulate lipid profiles by lowering LDL cholesterol, and influence bone metabolism. Additionally, the anti-inflammatory effects of soy isoflavones may contribute to cardiovascular benefits. The bioactive compounds in soybeans can also have protective effects against certain cancers, particularly hormone-sensitive types, by interfering with cancer cell growth and proliferation.

Pharmacokinetics

Isoflavones are absorbed in the gastrointestinal tract, with peak plasma concentrations typically occurring within 1 to 3 hours after ingestion. The bioavailability of isoflavones can be influenced by factors such as food matrix, gut microbiota, and individual metabolism. Soy isoflavones undergo extensive metabolism in the liver, resulting in various metabolites, some of which may exhibit different biological activities. The elimination half-life of isoflavones can vary widely, depending on individual factors and the form in which soy is consumed.

Adverse effects

• Allergic reactions
• Gastrointestinal disturbances
• Nausea
• Diarrhea
• Flatulence

Precautions

• Use with caution in individuals with a known allergy to soy products.
• Monitor for potential interactions with anticoagulants, as soybean contains vitamin K.

Pregnancy

Soybean is generally considered safe during pregnancy when consumed in food amounts. However, high doses or supplements should be avoided due to potential hormonal effects.

Breast-feeding

Soybean is likely safe in food amounts during breastfeeding, but high doses or supplements should be approached with caution.

Storage

Store in a cool, dry place, away from direct sunlight. Keep tightly closed to avoid moisture.

Formulations

• Whole soybeans
• Soy flour
• Soy protein isolate
• Soy milk
• Soy oil
• Soy lecithin

Indications

• Hypertriglyceridemia
• Cardiovascular disease risk management
• Metabolic syndrome

Dosage

Children: In paediatric patients, management of elevated triglycerides should involve a thorough evaluation by a healthcare provider. Specific dosing will depend on the chosen pharmacotherapy and should be referred to established guidelines.

Adults: For adults, management of high triglycerides typically begins with lifestyle changes. If medication is indicated, the specific dosing regimen will depend on the drug selected and should be guided by clinical guidelines.

Mechanism of action

Triglycerides are primarily absorbed from dietary sources and synthesized in the liver. Their levels are regulated by hormones such as insulin and involve the action of lipoprotein lipase, which hydrolyzes triglycerides into free fatty acids for energy use. In pharmacological terms, certain medications such as fibrates and omega-3 fatty acids work by enhancing the clearance of triglycerides from the bloodstream.

Pharmacodynamics

Triglyceride levels are influenced by various factors including diet, physical activity, and hormonal regulation. High levels of triglycerides can lead to atherosclerosis, where plaque builds up in the arteries, potentially resulting in heart disease. Drugs that are used to lower triglyceride levels typically work by either reducing the synthesis of triglycerides in the liver or enhancing their breakdown and clearance.

Pharmacokinetics

Triglycerides are transported in the bloodstream as part of lipoproteins, mainly chylomicrons and very-low-density lipoproteins (VLDL). They are metabolized in peripheral tissues by lipoprotein lipase. The half-life of triglycerides in circulation is variable and depends on several factors including the type of lipoprotein and the individual’s metabolic state. The clearance and metabolism of triglycerides can also be affected by medications, lifestyle factors, and underlying health conditions.

Adverse effects

• Pancreatitis
• Abdominal pain
• Nausea
• Vomiting
• Fatigue
• Eruptive xanthomas
• Liver dysfunction

Precautions

• Use with caution in patients with a history of pancreatitis.
• Monitor liver function tests in patients receiving treatment that can affect triglyceride levels.
• Consider lifestyle modifications prior to pharmacological intervention.

Pregnancy

Elevated triglyceride levels can be common during pregnancy; however, significant increases should be monitored as they may pose risks for gestational diabetes and pancreatitis.

Breast-feeding

Some studies suggest that triglyceride levels may increase during lactation; however, clinical significance is typically low. Monitoring is advised.

Storage

Store in a cool, dry place away from light. Ensure that any medications related to triglycerides are stored according to the manufacturer's instructions.

Mechanism of action

Glucose supplies most of the energy to all tissues by generating energy molecules ATP and NADH during a series of metabolism reactions called glycolysis. Glycolysis can be divided into two main phases where the preparatory phase is initiated by the phosphorylation of glucose by hexokinase to form glucose 6-phosphate. The addition of the high-energy phosphate group activates glucose for the subsequent breakdown in later steps of glycolysis and is the rate-limiting step. Products end up as substrates for following reactions, to ultimately convert C6 glucose molecule into two C3 sugar molecules. These products enter the energy-releasing phase where the total of 4ATP and 2NADH molecules are generated per one glucose molecule. The total aerobic metabolism of glucose can produce up to 36 ATP molecules. These energy-producing reactions of glucose are limited to D-glucose as L-glucose cannot be phosphorylated by hexokinase. Glucose can act as precursors to generate other biomolecules such as vitamin C. It plays a role as a signaling molecule to control glucose and energy homeostasis. Glucose can regulate gene transcription, enzyme activity, hormone secretion, and the activity of glucoregulatory neurons. The types, number, and kinetics of glucose transporters expressed depends on the tissues and fine-tunes glucose uptake, metabolism, and signal generation to preserve cellular and whole body metabolic integrity. Vascular calcification is a hallmark of type 2 diabetes. Glucose stimulates calcification in culture of vascular smooth muscle cells (VSMCs) but the underlying mechanisms remain obscure. We observed that high glucose levels stimulated mouse and human VSMC trans-differentiation into chondrocytes, with increased levels of Sox9, type II collagen, glycosaminoglycan and Runx2 expression, and increased alkaline phosphatase activity and mineralization. These effects were associated with increased expression of IL-1beta, which stimulated alkaline phosphatase and calcification, suggesting that glucose induces chondrocyte differentiation of VSMCs, possibly through IL-1beta activation.

Pharmacodynamics

Blood glucose is an obligatory energy source for humans involved in various cellular activities, and it also acts as a signaling molecule for diverse glucose-sensing molecules and proteins. Glucose undergoes oxidation into carbon dioxide, water, and yields energy molecules in the process of glycolysis and subsequent citric cycle and oxidative phosphorylation. Glucose is readily converted into fat in the body which can be used as a source of energy as required. Under a similar conversion into storage of energy, glucose is stored in the liver and muscles as glycogen. Glucose stores are mobilized in a regulated manner, depending on the tissues' metabolic demands. Oral glucose tablets or injections serve to increase the supply of glucose and oral glucose administration is more effective in stimulating insulin secretion because it stimulates the incretin hormones from the gut, which promotes insulin secretion.

Mechanism of action

In the CNS, there exist strychnine-sensitive glycine binding sites as well as strychnine-insensitive glycine binding sites. The strychnine-insensitive glycine-binding site is located on the NMDA receptor complex. The strychnine-sensitive glycine receptor complex is comprised of a chloride channel and is a member of the ligand-gated ion channel superfamily. The putative antispastic activity of supplemental glycine could be mediated by glycine's binding to strychnine-sensitive binding sites in the spinal cord. This would result in increased chloride conductance and consequent enhancement of inhibitory neurotransmission. The ability of glycine to potentiate NMDA receptor-mediated neurotransmission raised the possibility of its use in the management of neuroleptic-resistant negative symptoms in schizophrenia. Animal studies indicate that supplemental glycine protects against endotoxin-induced lethality, hypoxia-reperfusion injury after liver transplantation, and D-galactosamine-mediated liver injury. Neutrophils are thought to participate in these pathologic processes via invasion of tissue and releasing such reactive oxygen species as superoxide. In vitro studies have shown that neutrophils contain a glycine-gated chloride channel that can attenuate increases in intracellular calcium and diminsh neutrophil oxidant production. This research is ealy-stage, but suggests that supplementary glycine may turn out to be useful in processes where neutrophil infiltration contributes to toxicity, such as ARDS. HYPERPOLARIZATION OF MOTONEURONS PRODUCED BY IONTOPHORETIC APPLICATION OF GLYCINE IS RELATIVELY TRANSIENT BUT APPROACHES THE EQUILIBRIUM POTENTIAL FOR THE INDIRECTLY ACTIVATED INHIBITORY POSTSYNAPTIC POTENTIAL...TESTS WITH GABA... INDICATE SIMILAR ELECTROPHYSIOLOGICAL EFFECTS & SIMILAR INCR IN CL- CONDUCTANCE. MAJOR EVIDENCE THAT FAVORS GLYCINE AS MEDIATOR OF INTRASPINAL POSTSYNAPTIC INHIBITION IS THE SELECTIVE ANTAGONISM OF ITS EFFECTS BY STRYCHNINE. ... GLYCINE ALSO APPEARS TO BE MOST LIKELY TRANSMITTER FOR INHIBITORY INTERNEURONS IN RETICULAR FORMATION BUT NOT IN CUNEATE NUCLEUS.

Pharmacodynamics

Helps trigger the release of oxygen to the energy requiring cell-making process; Important in the manufacturing of hormones responsible for a strong immune system.

Mechanism of action

L-Alanine is a non-essential amino acid that occurs in high levels in its free state in plasma. It is produced from pyruvate by transamination. It is involved in sugar and acid metabolism, increases immunity, and provides energy for muscle tissue, brain, and the central nervous system. BCAAs are used as a source of energy for muscle cells. During prolonged exercise, BCAAs are released from skeletal muscles and their carbon backbones are used as fuel, while their nitrogen portion is used to form another amino acid, Alanine. Alanine is then converted to Glucose by the liver. This form of energy production is called the Alanine-Glucose cycle, and it plays a major role in maintaining the body's blood sugar balance.

Pharmacodynamics

Is an important source of energy for muscle tissue, the brain and central nervous system; strengthens the immune system by producing antibodies; helps in the metabolism of sugars and organic acids.

Mechanism of action

Many of supplemental L-arginine's activities, including its possible anti-atherogenic actions, may be accounted for by its role as the precursor to nitric oxide or NO. NO is produced by all tissues of the body and plays very important roles in the cardiovascular system, immune system and nervous system. NO is formed from L-arginine via the enzyme nitric oxide synthase or synthetase (NOS), and the effects of NO are mainly mediated by 3,'5' -cyclic guanylate or cyclic GMP. NO activates the enzyme guanylate cyclase, which catalyzes the synthesis of cyclic GMP from guanosine triphosphate or GTP. Cyclic GMP is converted to guanylic acid via the enzyme cyclic GMP phosphodiesterase. NOS is a heme-containing enzyme with some sequences similar to cytochrome P-450 reductase. Several isoforms of NOS exist, two of which are constitutive and one of which is inducible by immunological stimuli. The constitutive NOS found in the vascular endothelium is designated eNOS and that present in the brain, spinal cord and peripheral nervous system is designated nNOS. The form of NOS induced by immunological or inflammatory stimuli is known as iNOS. iNOS may be expressed constitutively in select tissues such as lung epithelium. All the nitric oxide synthases use NADPH (reduced nicotinamide adenine dinucleotide phosphate) and oxygen (O2) as cosubstrates, as well as the cofactors FAD (flavin adenine dinucleotide), FMN (flavin mononucleotide), tetrahydrobiopterin and heme. Interestingly, ascorbic acid appears to enhance NOS activity by increasing intracellular tetrahydrobiopterin. eNOS and nNOS synthesize NO in response to an increased concentration of calcium ions or in some cases in response to calcium-independent stimuli, such as shear stress. In vitro studies of NOS indicate that the Km of the enzyme for L-arginine is in the micromolar range. The concentration of L-arginine in endothelial cells, as well as in other cells, and in plasma is in the millimolar range. What this means is that, under physiological conditions, NOS is saturated with its L-arginine substrate. In other words, L-arginine would not be expected to be rate-limiting for the enzyme, and it would not appear that supraphysiological levels of L-arginine which could occur with oral supplementation of the amino acid^would make any difference with regard to NO production. The reaction would appear to have reached its maximum level. However, in vivo studies have demonstrated that, under certain conditions, e.g. hypercholesterolemia, supplemental L-arginine could enhance endothelial-dependent vasodilation and NO production.

Pharmacodynamics

Studies have shown that is has improved immune responses to bacteria, viruses and tumor cells; promotes wound healing and regeneration of the liver; causes the release of growth hormones; considered crucial for optimal muscle growth and tissue repair.

Mechanism of action

Since the actions of supplemental L-histidine are unclear, any postulated mechanism is entirely speculative. However, some facts are known about L-histidine and some of its metabolites, such as histamine and trans-urocanic acid, which suggest that supplemental L-histidine may one day be shown to have immunomodulatory and/or antioxidant activities. Low free histidine has been found in the serum of some rheumatoid arthritis patients. Serum concentrations of other amino acids have been found to be normal in these patients. L-histidine is an excellent chelating agent for such metals as copper, iron and zinc. Copper and iron participate in a reaction (Fenton reaction) that generates potent reactive oxygen species that could be destructive to tissues, including joints. L-histidine is the obligate precursor of histamine, which is produced via the decarboxylation of the amino acid. In experimental animals, tissue histamine levels increase as the amount of dietary L-histidine increases. It is likely that this would be the case in humans as well. Histamine is known to possess immunomodulatory and antioxidant activity. Suppressor T cells have H2 receptors, and histamine activates them. Promotion of suppressor T cell activity could be beneficial in rheumatoid arthritis. Further, histamine has been shown to down-regulate the production of reactive oxygen species in phagocytic cells, such as monocytes, by binding to the H2 receptors on these cells. Decreased reactive oxygen species production by phagocytes could play antioxidant, anti-inflammatory and immunomodulatory roles in such diseases as rheumatoid arthritis. This latter mechanism is the rationale for the use of histamine itself in several clinical trials studying histamine for the treatment of certain types of cancer and viral diseases. In these trials, down-regulation by histamine of reactive oxygen species formation appears to inhibit the suppression of natural killer (NK) cells and cytotoxic T lymphocytes, allowing these cells to be more effective in attacking cancer cells and virally infected cells.

Pharmacodynamics

Is found abundantly in hemoglobin; has been used in the treatment of rheumatoid arthritis, allergic diseases, ulcers and anemia. A deficiency can cause poor hearing.

Mechanism of action

This group of essential amino acids are identified as the branched-chain amino acids, BCAAs. Because this arrangement of carbon atoms cannot be made by humans, these amino acids are an essential element in the diet. The catabolism of all three compounds initiates in muscle and yields NADH and FADH2 which can be utilized for ATP generation. The catabolism of all three of these amino acids uses the same enzymes in the first two steps. The first step in each case is a transamination using a single BCAA aminotransferase, with a-ketoglutarate as amine acceptor. As a result, three different a-keto acids are produced and are oxidized using a common branched-chain a-keto acid dehydrogenase, yielding the three different CoA derivatives. Subsequently the metabolic pathways diverge, producing many intermediates. The principal product from valine is propionylCoA, the glucogenic precursor of succinyl-CoA. Isoleucine catabolism terminates with production of acetylCoA and propionylCoA; thus isoleucine is both glucogenic and ketogenic. Leucine gives rise to acetylCoA and acetoacetylCoA, and is thus classified as strictly ketogenic. There are a number of genetic diseases associated with faulty catabolism of the BCAAs. The most common defect is in the branched-chain a-keto acid dehydrogenase. Since there is only one dehydrogenase enzyme for all three amino acids, all three a-keto acids accumulate and are excreted in the urine. The disease is known as Maple syrup urine disease because of the characteristic odor of the urine in afflicted individuals. Mental retardation in these cases is extensive. Unfortunately, since these are essential amino acids, they cannot be heavily restricted in the diet; ultimately, the life of afflicted individuals is short and development is abnormal The main neurological problems are due to poor formation of myelin in the CNS. The mechanism of intracellular protein degradation, by which protein is hydrolyzed to free amino acids, is more complex and is not as well characterized at the mechanistic level as that of synthesis. A wide variety of different enzymes that are capable of splitting peptide bonds are present in cells. However, the bulk of cellular proteolysis seems to be shared between two multienzyme systems: the lysosomal and proteasomal systems. The lysosome is a membrane-enclosed vesicle inside the cell that contains a variety of proteolytic enzymes and operates mostly at acid pH. Volumes of the cytoplasm are engulfed (autophagy) and are then subjected to the action of the protease enzymes at high concentration. This system is thought to be relatively unselective in most cases, although it can also degrade specific intracellular proteins. The system is highly regulated by hormones such as insulin and glucocorticoids, and by amino acids. The second system is the ATP-dependent ubiquitin-proteasome system, which is present in the cytoplasm. The first step is to join molecules of ubiquitin, a basic 76-amino acid peptide, to lysine residues in the target protein. Several enzymes are involved in this process, which selectively targets proteins for degradation by a second component, the proteasome. Dietary leucine transported into the brain parenchyma serves several functions. Most prominent is the role of leucine as a metabolic precursor of fuel molecules, alpha-ketoisocaproate and ketone bodies. As alternatives to glucose, these compounds are forwarded by the producing astrocytes to the adjacent neural cells. Leucine furthermore participates in the maintenance of the nitrogen balance in the glutamate/glutamine cycle pertinent to the neurotransmitter glutamate. Leucine also serves as a regulator of the activity of some enzymes important for brain energy metabolism. Another role of leucine as an informational molecule is in mTOR signaling that participates in the regulation of food ingestion. The importance of leucine for brain function is stressed by the fact that inborn errors in its metabolism cause metabolic dis

Pharmacodynamics

An essential amino acid. (Claim) Leucine helps with the regulation of blood-sugar levels, the growth and repair of muscle tissue (such as bones, skin and muscles), growth hormone production, wound healing as well as energy regulation. It can assist to prevent the breakdown of muscle proteins that sometimes occur after trauma or severe stress. It may also be beneficial for individuals with phenylketonuria - a condition in which the body cannot metabolize the amino acid phenylalanine

Mechanism of action

Proteins of the herpes simplex virus are rich in L-arginine, and tissue culture studies indicate an enhancing effect on viral replication when the amino acid ratio of L-arginine to lysine is high in the tissue culture media. When the ratio of L-lysine to L-arginine is high, viral replication and the cytopathogenicity of herpes simplex virus have been found to be inhibited. L-lysine may facilitate the absorption of calcium from the small intestine. Amino acids are selected for protein synthesis by binding with transfer RNA (tRNA) in the cell cytoplasm. The information on the amino acid sequence of each individual protein is contained in the sequence of nucleotides in the messenger RNA (mRNA) molecules, which are synthesized in the nucleus from regions of DNA by the process of transcription. The mRNA molecules then interact with various tRNA molecules attached to specific amino acids in the cytoplasm to synthesize the specific protein by linking together individual amino acids; this process, known as translation, is regulated by amino acids (e.g., leucine), and hormones. Which specific proteins are expressed in any particular cell and the relative rates at which the different cellular proteins are synthesized, are determined by the relative abundances of the different mRNAs and the availability of specific tRNA-amino acid combinations, and hence by the rate of transcription and the stability of the messages. From a nutritional and metabolic point of view, it is important to recognize that protein synthesis is a continuing process that takes place in most cells of the body. In a steady state, when neither net growth nor protein loss is occurring, protein synthesis is balanced by an equal amount of protein degradation. The major consequence of inadequate protein intakes, or diets low or lacking in specific indispensable amino acids relative to other amino acids (often termed limiting amino acids), is a shift in this balance so that rates of synthesis of some body proteins decrease while protein degradation continues, thus providing an endogenous source of those amino acids most in need. /Amino acids/ The mechanism of intracellular protein degradation, by which protein is hydrolyzed to free amino acids, is more complex and is not as well characterized at the mechanistic level as that of synthesis. A wide variety of different enzymes that are capable of splitting peptide bonds are present in cells. However, the bulk of cellular proteolysis seems to be shared between two multienzyme systems: the lysosomal and proteasomal systems. The lysosome is a membrane-enclosed vesicle inside the cell that contains a variety of proteolytic enzymes and operates mostly at acid pH. Volumes of the cytoplasm are engulfed (autophagy) and are then subjected to the action of the protease enzymes at high concentration. This system is thought to be relatively unselective in most cases, although it can also degrade specific intracellular proteins. The system is highly regulated by hormones such as insulin and glucocorticoids, and by amino acids. The second system is the ATP-dependent ubiquitin-proteasome system, which is present in the cytoplasm. The first step is to join molecules of ubiquitin, a basic 76-amino acid peptide, to lysine residues in the target protein. Several enzymes are involved in this process, which selectively targets proteins for degradation by a second component, the proteasome. /Amino acids/

Pharmacodynamics

Insures the adequate absorption of calcium; helps form collagen ( which makes up bone cartilage & connective tissues); aids in the production of antibodies, hormones & enzymes. Recent studies have shown that Lysine may be effective against herpes by improving the balance of nutrients that reduce viral growth. A deficiency may result in tiredness, inability to concentrate, irritability, bloodshot eyes, retarded growth, hair loss, anemia & reproductive problems.

Mechanism of action

The mechanism of the possible anti-hepatotoxic activity of L-methionine is not entirely clear. It is thought that metabolism of high doses of acetaminophen in the liver lead to decreased levels of hepatic glutathione and increased oxidative stress. L-methionine is a precursor to L-cysteine. L-cysteine itself may have antioxidant activity. L-cysteine is also a precursor to the antioxidant glutathione. Antioxidant activity of L-methionine and metabolites of L-methionine appear to account for its possible anti-hepatotoxic activity. Recent research suggests that methionine itself has free-radical scavenging activity by virtue of its sulfur, as well as its chelating ability. Amino acids are selected for protein synthesis by binding with transfer RNA (tRNA) in the cell cytoplasm. The information on the amino acid sequence of each individual protein is contained in the sequence of nucleotides in the messenger RNA (mRNA) molecules, which are synthesized in the nucleus from regions of DNA by the process of transcription. The mRNA molecules then interact with various tRNA molecules attached to specific amino acids in the cytoplasm to synthesize the specific protein by linking together individual amino acids; this process, known as translation, is regulated by amino acids (e.g., leucine), and hormones. Which specific proteins are expressed in any particular cell and the relative rates at which the different cellular proteins are synthesized, are determined by the relative abundances of the different mRNAs and the availability of specific tRNA-amino acid combinations, and hence by the rate of transcription and the stability of the messages. From a nutritional and metabolic point of view, it is important to recognize that protein synthesis is a continuing process that takes place in most cells of the body. In a steady state, when neither net growth nor protein loss is occurring, protein synthesis is balanced by an equal amount of protein degradation. The major consequence of inadequate protein intakes, or diets low or lacking in specific indispensable amino acids relative to other amino acids (often termed limiting amino acids), is a shift in this balance so that rates of synthesis of some body proteins decrease while protein degradation continues, thus providing an endogenous source of those amino acids most in need. /Protein synthesis/ The mechanism of intracellular protein degradation, by which protein is hydrolyzed to free amino acids, is more complex and is not as well characterized at the mechanistic level as that of synthesis. A wide variety of different enzymes that are capable of splitting peptide bonds are present in cells. However, the bulk of cellular proteolysis seems to be shared between two multienzyme systems: the lysosomal and proteasomal systems. The lysosome is a membrane-enclosed vesicle inside the cell that contains a variety of proteolytic enzymes and operates mostly at acid pH. Volumes of the cytoplasm are engulfed (autophagy) and are then subjected to the action of the protease enzymes at high concentration. This system is thought to be relatively unselective in most cases, although it can also degrade specific intracellular proteins. The system is highly regulated by hormones such as insulin and glucocorticoids, and by amino acids. The second system is the ATP-dependent ubiquitin-proteasome system, which is present in the cytoplasm. The first step is to join molecules of ubiquitin, a basic 76-amino acid peptide, to lysine residues in the target protein. Several enzymes are involved in this process, which selectively targets proteins for degradation by a second component, the proteasome. /Protein degradation/ Methionine dependence, the inability of cells to grow when the amino acid methionine is replaced in culture medium by its metabolic precursor homocysteine, is characteristic of many cancer cell lines and some tumors in situ. Most cell lines proliferate normally under these conditions. The methionine dependent t

Pharmacodynamics

L-Methionine is a principle supplier of sulfur which prevents disorders of the hair, skin and nails; helps lower cholesterol levels by increasing the liver's production of lecithin; reduces liver fat and protects the kidneys; a natural chelating agent for heavy metals; regulates the formation of ammonia and creates ammonia-free urine which reduces bladder irritation; influences hair follicles and promotes hair growth. L-methionine may protect against the toxic effects of hepatotoxins, such as acetaminophen. Methionine may have antioxidant activity.

Mechanism of action

L-Ornithine is metabolised to L-arginine. L-arginine stimulates the pituitary release of growth hormone. Burns or other injuries affect the state of L-arginine in tissues throughout the body. As De novo synthesis of L-arginine during these conditions is usually not sufficient for normal immune function, nor for normal protein synthesis, L-ornithine may have immunomodulatory and wound-healing activities under these conditions (by virtue of its metabolism to L-arginine).

Pharmacodynamics

A non-essential and nonprotein amino acid, ornithine is critical for the production of the body's proteins, enzymes and muscle tissue. Ornithine plays a central role in the urea cycle and is important for the disposal of excess nitrogen (ammonia). Ornithine is the starting point for the synthesis of many polyamines such as putrescine and spermine. Ornithine supplements are claimed to enhance the release of growth hormone and to burn excess body fat. Ornithine is necessary for proper immune function and good liver function.

Mechanism of action

The supposed antidepressant effects of L-phenylalanine may be due to its role as a precursor in the synthesis of the neurotransmitters norepinephrine and dopamine. Elevated brain norepinephrine and dopamine levels are thought to be associated with antidepressant effects. The mechanism of L-phenylalanine's possible antivitiligo activity is not well understood. It is thought that L-phenylalanine may stimulate the production of melanin in the affected skin Amino acids are selected for protein synthesis by binding with transfer RNA (tRNA) in the cell cytoplasm. The information on the amino acid sequence of each individual protein is contained in the sequence of nucleotides in the messenger RNA (mRNA) molecules, which are synthesized in the nucleus from regions of DNA by the process of transcription. The mRNA molecules then interact with various tRNA molecules attached to specific amino acids in the cytoplasm to synthesize the specific protein by linking together individual amino acids; this process, known as translation, is regulated by amino acids (e.g., leucine), and hormones. Which specific proteins are expressed in any particular cell and the relative rates at which the different cellular proteins are synthesized, are determined by the relative abundances of the different mRNAs and the availability of specific tRNA-amino acid combinations, and hence by the rate of transcription and the stability of the messages. From a nutritional and metabolic point of view, it is important to recognize that protein synthesis is a continuing process that takes place in most cells of the body. In a steady state, when neither net growth nor protein loss is occurring, protein synthesis is balanced by an equal amount of protein degradation. The major consequence of inadequate protein intakes, or diets low or lacking in specific indispensable amino acids relative to other amino acids (often termed limiting amino acids), is a shift in this balance so that rates of synthesis of some body proteins decrease while protein degradation continues, thus providing an endogenous source of those amino acids most in need. /Amino acids/ The mechanism of intracellular protein degradation, by which protein is hydrolyzed to free amino acids, is more complex and is not as well characterized at the mechanistic level as that of synthesis. A wide variety of different enzymes that are capable of splitting peptide bonds are present in cells. However, the bulk of cellular proteolysis seems to be shared between two multienzyme systems: the lysosomal and proteasomal systems. The lysosome is a membrane-enclosed vesicle inside the cell that contains a variety of proteolytic enzymes and operates mostly at acid pH. Volumes of the cytoplasm are engulfed (autophagy) and are then subjected to the action of the protease enzymes at high concentration. This system is thought to be relatively unselective in most cases, although it can also degrade specific intracellular proteins. The system is highly regulated by hormones such as insulin and glucocorticoids, and by amino acids. The second system is the ATP-dependent ubiquitin-proteasome system, which is present in the cytoplasm. The first step is to join molecules of ubiquitin, a basic 76-amino acid peptide, to lysine residues in the target protein. Several enzymes are involved in this process, which selectively targets proteins for degradation by a second component, the proteasome. /Amino acids/

Pharmacodynamics

Used by the brain to produce Norepinephrine, a chemical that transmits signals between nerve cells and the brain; keeps you awake and alert; reduces hunger pains; functions as an antidepressant and helps improve memory.

Mechanism of action

Glycogenic, by L-Proline oxidase in the kidney, it is ring-opened and is oxidized to form L-Glutamic acid. L-Ornithine and L-Glutamic acid are converted to L-Proline via L-Glutamic acid-gamma-semialdehyde. It is contained abundantly in collagen, and is intimately involved in the function of arthrosis and chordae.

Pharmacodynamics

L-Proline is a major amino acid found in cartilage and is important for maintaining youthful skin as well as repair of muscle, connective tissue and skin damage. It is also essential for the immune system, and for necessary balance of this formula. It is an essential component of collagen and is important for proper functioning of joints and tendons. L-Proline is extremely important for the proper functioning of joints and tendons. Helps maintain and strengthen heart muscles.

Mechanism of action

L-Serine plays a role in cell growth and development (cellular proliferation). The conversion of L-serine to glycine by serine hydroxymethyltransferase results in the formation of the one-carbon units necessary for the synthesis of the purine bases, adenine and guanine. These bases when linked to the phosphate ester of pentose sugars are essential components of DNA and RNA and the end products of energy producing metabolic pathways, ATP and GTP. In addition, L-serine conversion to glycine via this same enzyme provides the one-carbon units necessary for production of the pyrimidine nucleotide, deoxythymidine monophosphate, also an essential component of DNA.

Pharmacodynamics

Serine is classified as a nutritionally non-essential amino acid. Serine is critical for the production of the body's proteins, enzymes and muscle tissue. Serine is needed for the proper metabolism of fats and fatty acids. It also helps in the production of antibodies. Serine is used as a natural moisturizing agent in some cosmetics and skin care products. The main source of essential amino acids is from the diet, non-essential amino acids are normally synthesize by humans and other mammals from common intermediates.

Mechanism of action

L-Threonine is a precursor to the amino acids glycine and serine. It acts as a lipotropic in controlling fat build-up in the liver. May help combat mental illness and may be very useful in indigestion and intestinal malfunctions. Also, threonine prevents excessive liver fat. Nutrients are more readily absorbed when threonine is present. Amino acids are selected for protein synthesis by binding with transfer RNA (tRNA) in the cell cytoplasm. The information on the amino acid sequence of each individual protein is contained in the sequence of nucleotides in the messenger RNA (mRNA) molecules, which are synthesized in the nucleus from regions of DNA by the process of transcription. The mRNA molecules then interact with various tRNA molecules attached to specific amino acids in the cytoplasm to synthesize the specific protein by linking together individual amino acids; this process, known as translation, is regulated by amino acids (e.g., leucine), and hormones. Which specific proteins are expressed in any particular cell and the relative rates at which the different cellular proteins are synthesized, are determined by the relative abundances of the different mRNAs and the availability of specific tRNA-amino acid combinations, and hence by the rate of transcription and the stability of the messages. From a nutritional and metabolic point of view, it is important to recognize that protein synthesis is a continuing process that takes place in most cells of the body. In a steady state, when neither net growth nor protein loss is occurring, protein synthesis is balanced by an equal amount of protein degradation. The major consequence of inadequate protein intakes, or diets low or lacking in specific indispensable amino acids relative to other amino acids (often termed limiting amino acids), is a shift in this balance so that rates of synthesis of some body proteins decrease while protein degradation continues, thus providing an endogenous source of those amino acids most in need. /Protein synthesis/ The mechanism of intracellular protein degradation, by which protein is hydrolyzed to free amino acids, is more complex and is not as well characterized at the mechanistic level as that of synthesis. A wide variety of different enzymes that are capable of splitting peptide bonds are present in cells. However, the bulk of cellular proteolysis seems to be shared between two multienzyme systems: the lysosomal and proteasomal systems. The lysosome is a membrane-enclosed vesicle inside the cell that contains a variety of proteolytic enzymes and operates mostly at acid pH. Volumes of the cytoplasm are engulfed (autophagy) and are then subjected to the action of the protease enzymes at high concentration. This system is thought to be relatively unselective in most cases, although it can also degrade specific intracellular proteins. The system is highly regulated by hormones such as insulin and glucocorticoids, and by amino acids. The second system is the ATP-dependent ubiquitin-proteasome system, which is present in the cytoplasm. The first step is to join molecules of ubiquitin, a basic 76-amino acid peptide, to lysine residues in the target protein. Several enzymes are involved in this process, which selectively targets proteins for degradation by a second component, the proteasome. /Protein degradation/

Pharmacodynamics

L-Threonine is an essential amino acid that helps to maintain the proper protein balance in the body. It is important for the formation of collagen, elastin, and tooth enamel, and aids liver and lipotropic function when combined with aspartic acid and methionine.

Mechanism of action

A number of important side reactions occur during the catabolism of tryptophan on the pathway to acetoacetate. The first enzyme of the catabolic pathway is an iron porphyrin oxygenase that opens the indole ring. The latter enzyme is highly inducible, its concentration rising almost 10-fold on a diet high in tryptophan. Kynurenine is the first key branch point intermediate in the pathway. Kynurenine undergoes deamniation in a standard transamination reaction yielding kynurenic acid. Kynurenic acid and metabolites have been shown to act as antiexcitotoxics and anticonvulsives. A second side branch reaction produces anthranilic acid plus alanine. Another equivalent of alanine is produced further along the main catabolic pathway, and it is the production of these alanine residues that allows tryptophan to be classified among the glucogenic and ketogenic amino acids. The second important branch point converts kynurenine into 2-amino-3-carboxymuconic semialdehyde, which has two fates. The main flow of carbon elements from this intermediate is to glutarate. An important side reaction in liver is a transamination and several rearrangements to produce limited amounts of nicotinic acid, which leads to production of a small amount of NAD⁺ and NADP⁺. Findings indicate that enhanced rates of serotonin turnover produced by (L)-tryptophan and physical restraint are associated with inhibition of thyroid-stimulating hormone (TSH) and stimulation of prolactin release from anterior pituitary in rats. L-Tryptophan, an indispensable amino acid, serves as a precursor for several small molecules of functional significance including the vitamin niacin, the neurotransmitter serotonin, the metabolite tryptamine, and the pineal hormone melatonin. Increases in tryptophan have been shown to increase synthesis of the neurotransmitters in brain, blood, and other body organs. Amino acids are selected for protein synthesis by binding with transfer RNA (tRNA) in the cell cytoplasm. The information on the amino acid sequence of each individual protein is contained in the sequence of nucleotides in the messenger RNA (mRNA) molecules, which are synthesized in the nucleus from regions of DNA by the process of transcription. The mRNA molecules then interact with various tRNA molecules attached to specific amino acids in the cytoplasm to synthesize the specific protein by linking together individual amino acids; this process, known as translation, is regulated by amino acids (e.g., leucine), and hormones. Which specific proteins are expressed in any particular cell and the relative rates at which the different cellular proteins are synthesized, are determined by the relative abundances of the different mRNAs and the availability of specific tRNA-amino acid combinations, and hence by the rate of transcription and the stability of the messages. From a nutritional and metabolic point of view, it is important to recognize that protein synthesis is a continuing process that takes place in most cells of the body. In a steady state, when neither net growth nor protein loss is occurring, protein synthesis is balanced by an equal amount of protein degradation. The major consequence of inadequate protein intakes, or diets low or lacking in specific indispensable amino acids relative to other amino acids (often termed limiting amino acids), is a shift in this balance so that rates of synthesis of some body proteins decrease while protein degradation continues, thus providing an endogenous source of those amino acids most in need. /Amino acids/ The mechanism of intracellular protein degradation, by which protein is hydrolyzed to free amino acids, is more complex and is not as well characterized at the mechanistic level as that of synthesis. A wide variety of different enzymes that are capable of splitting peptide bonds are present in cells. However, the bulk of cellular proteolysis seems to be shared between two multienzyme systems: the lysosomal and prote

Pharmacodynamics

Tryptophan is critical for the production of the body's proteins, enzymes and muscle tissue. It is also essential for the production of niacin, the synthesis of the neurotransmitter serotonin and melatonin. Tryptophan supplements can be used as natural relaxants to help relieve insomnia. Tryptophan can also reduce anxiety and depression and has been shown to reduce the intensity of migraine headaches. Other promising indications include the relief of chronic pain, reduction of impulsivity or mania and the treatment of obsessive or compulsive disorders. Tryptophan also appears to help the immune system and can reduce the risk of cardiac spasms. Tryptophan deficiencies may lead to coronary artery spasms. Tryptophan is used as an essential nutrient in infant formulas and intravenous feeding. Tryptophan is marketed as a prescription drug (Tryptan) for those who do not seem to respond well to conventional antidepressants. It may also be used to treat those afflicted with seasonal affective disorder (a winter-onset depression). Tryptopan serves as the precursor for the synthesis of serotonin (5-hydroxytryptamine, 5-HT) and melatonin (N-acetyl-5-methoxytryptamine).

Mechanism of action

Tyrosine is produced in cells by hydroxylating the essential amino acid phenylalanine. This relationship is much like that between cysteine and methionine. Half of the phenylalanine required goes into the production of tyrosine; if the diet is rich in tyrosine itself, the requirements for phenylalanine are reduced by about 50%. The mechanism of L-tyrosine's antidepressant activity can be accounted for by the precursor role of L-tyrosine in the synthesis of the neurotransmitters norepinephrine and dopamine. Elevated brain norepinephrine and dopamine levels are thought to be associated with antidepressant effects.

Pharmacodynamics

Tyrosine is a nonessential amino acid synthesized in the body from phenylalanine. Tyrosine is critical for the production of the body's proteins, enzymes and muscle tissue. Tyrosine is a precursor to the neurotransmitters norepinephrine and dopamine. It can act as a mood elevator and an anti-depressant. It may improve memory and increase mental alertness. Tyrosine aids in the production of melanin and plays a critical role in the production of thyroxin (thyroid hormones). Tyrosine deficiencies are manifested by hypothyroidism, low blood pressure and low body temperature. Supplemental tyrosine has been used to reduce stress and combat narcolepsy and chronic fatigue.

Mechanism of action

(Applies to Valine, Leucine and Isoleucine) This group of essential amino acids are identified as the branched-chain amino acids, BCAAs. Because this arrangement of carbon atoms cannot be made by humans, these amino acids are an essential element in the diet. The catabolism of all three compounds initiates in muscle and yields NADH and FADH2 which can be utilized for ATP generation. The catabolism of all three of these amino acids uses the same enzymes in the first two steps. The first step in each case is a transamination using a single BCAA aminotransferase, with a-ketoglutarate as amine acceptor. As a result, three different a-keto acids are produced and are oxidized using a common branched-chain a-keto acid dehydrogenase, yielding the three different CoA derivatives. Subsequently the metabolic pathways diverge, producing many intermediates. The principal product from valine is propionylCoA, the glucogenic precursor of succinyl-CoA. Isoleucine catabolism terminates with production of acetylCoA and propionylCoA; thus isoleucine is both glucogenic and ketogenic. Leucine gives rise to acetylCoA and acetoacetylCoA, and is thus classified as strictly ketogenic. There are a number of genetic diseases associated with faulty catabolism of the BCAAs. The most common defect is in the branched-chain a-keto acid dehydrogenase. Since there is only one dehydrogenase enzyme for all three amino acids, all three a-keto acids accumulate and are excreted in the urine. The disease is known as Maple syrup urine disease because of the characteristic odor of the urine in afflicted individuals. Mental retardation in these cases is extensive. Unfortunately, since these are essential amino acids, they cannot be heavily restricted in the diet; ultimately, the life of afflicted individuals is short and development is abnormal The main neurological problems are due to poor formation of myelin in the CNS. Amino acids are selected for protein synthesis by binding with transfer RNA (tRNA) in the cell cytoplasm. The information on the amino acid sequence of each individual protein is contained in the sequence of nucleotides in the messenger RNA (mRNA) molecules, which are synthesized in the nucleus from regions of DNA by the process of transcription. The mRNA molecules then interact with various tRNA molecules attached to specific amino acids in the cytoplasm to synthesize the specific protein by linking together individual amino acids; this process, known as translation, is regulated by amino acids (e.g., leucine), and hormones. Which specific proteins are expressed in any particular cell and the relative rates at which the different cellular proteins are synthesized, are determined by the relative abundances of the different mRNAs and the availability of specific tRNA-amino acid combinations, and hence by the rate of transcription and the stability of the messages. From a nutritional and metabolic point of view, it is important to recognize that protein synthesis is a continuing process that takes place in most cells of the body. In a steady state, when neither net growth nor protein loss is occurring, protein synthesis is balanced by an equal amount of protein degradation. The major consequence of inadequate protein intakes, or diets low or lacking in specific indispensable amino acids relative to other amino acids (often termed limiting amino acids), is a shift in this balance so that rates of synthesis of some body proteins decrease while protein degradation continues, thus providing an endogenous source of those amino acids most in need. /Amino acids/ The mechanism of intracellular protein degradation, by which protein is hydrolyzed to free amino acids, is more complex and is not as well characterized at the mechanistic level as that of synthesis. A wide variety of different enzymes that are capable of splitting peptide bonds are present in cells. However, the bulk of cellular proteolysis seems to be shared between two multienzyme systems: the lysoso

Pharmacodynamics

L-valine is a branched-chain essential amino acid (BCAA) that has stimulant activity. It promotes muscle growth and tissue repair. It is a precursor in the penicillin biosynthetic pathway. Valine is one of three branched-chain amino acids (the others are leucine and isoleucine) that enhance energy, increase endurance, and aid in muscle tissue recovery and repair. This group also lowers elevated blood sugar levels and increases growth hormone production. Supplemental valine should always be combined with isoleucine and leucine at a respective milligram ratio of 2:1:2. It is an essential amino acid found in proteins; important for optimal growth in infants and for growth in children and nitrogen balance in adults. The lack of L-valine may influence the growth of body, cause neuropathic obstacle, anaemia. It has wide applications in the field of pharmaceutical and food industry.