Molecular Sequence Data
Amino Acid Sequence
Basic-Leucine Zipper Transcription Factors
RNA, Transfer, Leu
Amino Acids, Essential
Sequence Homology, Amino Acid
G-Box Binding Factors
Amino Acid Substitution
Leucine-Responsive Regulatory Protein
Protein Structure, Tertiary
Recombinant Fusion Proteins
Basic Helix-Loop-Helix Leucine Zipper Transcription Factors
TOR Serine-Threonine Kinases
Electrophoresis, Polyacrylamide Gel
Protein Structure, Secondary
3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide)
Proto-Oncogene Proteins c-jun
Amino Acid Motifs
Amino Acid Transport Systems
Ribosomal Protein S6 Kinases
Oncogene Protein p65(gag-jun)
Biological Transport, Active
Rats, Inbred Strains
Amino Acyl-tRNA Synthetases
Saccharomyces cerevisiae Proteins
RNA, Transfer, Ser
Gene Expression Regulation
Dose-Response Relationship, Drug
Ribosomal Protein S6 Kinases, 70-kDa
Plasma Membrane Neurotransmitter Transport Proteins
Promoter Regions, Genetic
Two-Hybrid System Techniques
Amino Acid Transport Systems, Neutral
Magnetic Resonance Spectroscopy
Gas Chromatography-Mass Spectrometry
Hydrophobic and Hydrophilic Interactions
Carcinoma 256, Walker
Proto-Oncogene Proteins c-fos
MAP Kinase Kinase Kinases
Control of ketogenesis from amino acids. IV. Tissue specificity in oxidation of leucine, tyrosine, and lysine. (1/5969)In vitro and in vivo studies were made on the tissue specificity of oxidation of the ketogenic amino acids, leucine, tyrosine, and lysine. In in vitro studies the abilities of slices of various tissues of rats to form 14CO2 from 14C-amino acids were examined. With liver, but not kidney slices, addition of alpha-ketoglutarate was required for the maximum activities with these amino acids. Among the various tissues tested, kidney had the highest activity for lysine oxidation, followed by liver; other tissues showed very low activity. Kidney also had the highest activity for leucine oxidation, followed by diaphragm; liver and adipose tissue had lower activities. Liver had the highest activity for tyrosine oxidation, but kidney also showed considerable activity; other tissues had negligible activity. In in vivo studies the blood flow through the liver or kidney was stopped by ligation of the blood vessels. Then labeled amino acids were injected and recovery of radioactivity in respiratory 14CO2 was measured. In contrast to results with slices, no difference was found in the respiratory 14CO2 when the renal blood vessels were or were not ligated. On the contrary ligation of the hepatic vessels suppressed the oxidations of lysine and tyrosine completely and that of leucine partially. Thus in vivo, lysine and tyrosine seem to be metabolized mainly in the liver, whereas leucine is metabolized mostly in extrahepatic tissues and partly in liver. Use of tissue slices seems to be of only limited value in elucidating the metabolisms of these amino acids. (+info)
A general method for selection of alpha-acetolactate decarboxylase-deficient Lactococcus lactis mutants to improve diacetyl formation. (2/5969)The enzyme acetolactate decarboxylase (Ald) plays a key role in the regulation of the alpha-acetolactate pool in both pyruvate catabolism and the biosynthesis of the branched-chain amino acids, isoleucine, leucine, and valine (ILV). This dual role of Ald, due to allosteric activation by leucine, was used as a strategy for the isolation of Ald-deficient mutants of Lactococcus lactis subsp. lactis biovar diacetylactis. Such mutants can be selected as leucine-resistant mutants in ILV- or IV-prototrophic strains. Most dairy lactococcus strains are auxotrophic for the three amino acids. Therefore, the plasmid pMC004 containing the ilv genes (encoding the enzymes involved in the biosynthesis of IV) of L. lactis NCDO2118 was constructed. Introduction of pMC004 into ILV-auxotrophic dairy strains resulted in an isoleucine-prototrophic phenotype. By plating the strains on a chemically defined medium supplemented with leucine but not valine and isoleucine, spontaneous leucine-resistant mutants were obtained. These mutants were screened by Western blotting with Ald-specific antibodies for the presence of Ald. Selected mutants lacking Ald were subsequently cured of pMC004. Except for a defect in the expression of Ald, the resulting strain, MC010, was identical to the wild-type strain, as shown by Southern blotting and DNA fingerprinting. The mutation resulting in the lack of Ald in MC010 occurred spontaneously, and the strain does not contain foreign DNA; thus, it can be regarded as food grade. Nevertheless, its application in dairy products depends on the regulation of genetically modified organisms. These results establish a strategy to select spontaneous Ald-deficient mutants from transformable L. lactis strains. (+info)
Hmo1p, a high mobility group 1/2 homolog, genetically and physically interacts with the yeast FKBP12 prolyl isomerase. (3/5969)The immunosuppressive drugs FK506 and rapamycin bind to the cellular protein FKBP12, and the resulting FKBP12-drug complexes inhibit signal transduction. FKBP12 is a ubiquitous, highly conserved, abundant enzyme that catalyzes a rate-limiting step in protein folding: peptidyl-prolyl cis-trans isomerization. However, FKBP12 is dispensible for viability in both yeast and mice, and therefore does not play an essential role in protein folding. The functions of FKBP12 may involve interactions with a number of partner proteins, and a few proteins that interact with FKBP12 in the absence of FK506 or rapamycin have been identified, including the ryanodine receptor, aspartokinase, and the type II TGF-beta receptor; however, none of these are conserved from yeast to humans. To identify other targets and functions of FKBP12, we have screened for mutations that are synthetically lethal with an FKBP12 mutation in yeast. We find that mutations in HMO1, which encodes a high mobility group 1/2 homolog, are synthetically lethal with mutations in the yeast FPR1 gene encoding FKBP12. Deltahmo1 and Deltafpr1 mutants share two phenotypes: an increased rate of plasmid loss and slow growth. In addition, Hmo1p and FKBP12 physically interact in FKBP12 affinity chromatography experiments, and two-hybrid experiments suggest that FKBP12 regulates Hmo1p-Hmo1p or Hmo1p-DNA interactions. Because HMG1/2 proteins are conserved from yeast to humans, our findings suggest that FKBP12-HMG1/2 interactions could represent the first conserved function of FKBP12 other than mediating FK506 and rapamycin actions. (+info)
Nuclear export of LIM-kinase 1, mediated by two leucine-rich nuclear-export signals within the PDZ domain. (4/5969)LIM-kinase 1 (LIMK1) is a serine/threonine kinase that phosphorylates cofilin and regulates actin-filament dynamics. LIMK1, which contains two LIM domains and a single PDZ domain, localizes predominantly in the cytoplasm, but its mutant, deleted with the PDZ domain, localizes mainly in the nucleus, thereby indicating that the PDZ domain plays a role in the cytoplasmic localization of LIMK1. Here we provide evidence that the PDZ domain of LIMK1 contains two functional leucine-rich nuclear-export signals (NESs). The PDZ domain of LIMK1 fused with glutathione S-transferase (GST-PDZ), when injected into the nucleus, was rapidly excluded from the nucleus, but its mutant with replacements of conserved hydrophobic residues in two putative NESs by alanines remained in the nucleus. The nuclear export of GST-PDZ was sensitive to leptomycin B (LMB), a specific inhibitor of nuclear export mediated by leucine-rich NESs. Malfunctional mutation of two NESs or LMB treatment prevented the nuclear export of full-length LIMK1 and induced its nuclear accumulation. These results suggest that the predominant localization of LIMK1 in the cytoplasm is supported by two NESs within the PDZ domain and that LIMK1 normally shuttles between the cytoplasm and the nucleus. We also provide evidence that a short basic cluster sequence within the protein-kinase domain is involved in the nuclear import of LIMK1. (+info)
Ion binding and permeation through the lepidopteran amino acid transporter KAAT1 expressed in Xenopus oocytes. (5/5969)1. The transient and steady-state currents induced by voltage jumps in Xenopus oocytes expressing the lepidopteran amino acid co-transporter KAAT1 have been investigated by two-electrode voltage clamp. 2. KAAT1-expressing oocytes exhibited membrane currents larger than controls even in the absence of amino acid substrate (uncoupled current). The selectivity order of this uncoupled current was Li+ > Na+ approximately Rb+ approximately K+ > Cs+; in contrast, the permeability order in non-injected oocytes was Rb+ > K+ > Cs+ > Na+ > Li+. 3. KAAT1-expressing oocytes gave rise to 'pre-steady-state currents' in the absence of amino acid. The characteristics of the charge movement differed according to the bathing ion: the curves in K+ were strongly shifted (> 100 mV) towards more negative potentials compared with those in Na+, while in tetramethylammonium (TMA+) no charge movement was detected. 4. The charge-voltage (Q-V) relationship in Na+ could be fitted by a Boltzmann equation having V of -69 +/- 1 mV and slope factor of 26 +/- 1 mV; lowering the Na+ concentrations shifted the Q-V relationship to more negative potentials; the curves could be described by a generalized Hill equation with a coefficient of 1.6, suggesting two binding sites. The maximal movable charge (Qmax) in Na+, 3 days after injection, was in the range 2.5-10 nC. 5. Addition of the transported substrate leucine increased the steady-state carrier current, the increase being larger in high K+ compared with high Na+ solution; in these conditions the charge movement disappeared. 6. Applying Eyring rate theory, the energy profile of the transporter in the absence of organic substrate included a very high external energy barrier (25.8 RT units) followed by a rather deep well (1.8 RT units). (+info)
A surrogate measure of whole body leucine transport across the cell membrane. (6/5969)Based on a mass-balance model, a surrogate measure of the whole body leucine transport into and out of cells under steady-state conditions was calculated as u/DeltaTTR, where u is the infusion rate of (stable label) leucine tracer and DeltaTTR is the difference between the tracer-to-tracee ratio of extracellular and intracellular leucine. The approach was evaluated in ten healthy subjects [8 males and 2 females; age, 31 +/- 9 (SD) yr; body mass index, 24.0 +/- 1.6 kg/m2] who received a primed (7.58 micromol/kg) constant intravenous infusion (7.58 micromol. kg-1. h-1) of L-[1-13C]leucine over 180 min (7 subjects) or 240 min (3 subjects). Five subjects were studied on two occasions >/=1 wk apart to assess reproducibility. Blood samples taken during the last 30 min of the leucine infusion were used to determine plasma leucine concentration (129 +/- 35 micromol/l), TTR of leucine (9.0 +/- 1.5%), and TTR of alpha-ketoisocaproic acid (6.7 +/- 0.8%). The latter TTR was taken as the measure of the free intracellular leucine TTR. The whole body inward and outward transport was 6.66 +/- 3.82 micromol. kg-1. min-1; the rate of leucine appearance due to proteolysis was 1.93 +/- 0.24 micromol. kg-1. min-1. A positive linear relationship between the inward transport and plasma leucine was observed (P < 0.01), indicating the presence of the mass effect of leucine on its own transport. The transport was highly variable between subjects (between-subject coefficient of variation 57%) but reproducible (within-subject coefficient of variation 17%). We conclude that reproducible estimates of whole body transport of leucine across the cell membrane can be obtained under steady-state conditions with existing experimental and analytical procedures. (+info)
Transthyretin Leu12Pro is associated with systemic, neuropathic and leptomeningeal amyloidosis. (7/5969)We report a middle-aged woman with a novel transthyretin (TTR) variant, Leu12Pro. She had extensive amyloid deposition in the leptomeninges and liver as well as the involvement of the heart and peripheral nervous system which characterizes familial amyloid polyneuropathy caused by variant TTR. Clinical features attributed to her leptomeningeal amyloid included radiculopathy, central hypoventilation, recurrent subarachnoid haemorrhage, depression, seizures and periods of decreased consciousness. MRI showed a marked enhancement throughout her meninges and ependyma, and TTR amyloid deposition was confirmed by meningeal biopsy. The simultaneous presence of extensive visceral amyloid and clinically significant deposits affecting both the peripheral and central nervous system extends the spectrum of amyloid-related disease associated with TTR mutations. The unusual association of severe peripheral neuropathy with symptoms of leptomeningeal amyloid indicates that leptomeningeal amyloidosis should be considered part of the syndrome of TTR-related familial amyloid polyneuropathy. (+info)
Leucine metabolism in preterm infants receiving parenteral nutrition with medium-chain compared with long-chain triacylglycerol emulsions. (8/5969)BACKGROUND: Although medium-chain triacylglycerols (MCTs) may be utilized more efficiently than long-chain triacylglycerols (LCTs), their effect on protein metabolism remains controversial. OBJECTIVE: The aim of the study was to compare the effects of mixed MCT-LCT and pure LCT emulsions on leucine metabolism in preterm infants. DESIGN: Fourteen preterm [gestational age: 30+/-1 wk; birth weight: 1409+/-78 g (x +/- SE)] neonates were randomly assigned to receive, from the first day of life, either a 50:50 MCT-LCT (mixed MCT group; n = 7) or an LCT (LCT group; n = 7) lipid emulsion as part of an isonitrogenous, isoenergetic total parenteral nutrition program. On the fourth day, infants received intravenous feeding providing 3 g lipid, 15 g glucose, and 3 g amino acids kg(-1) x d(-1) and underwent 1) indirect calorimetry and 2) a primed, 2-h infusion of H13CO3Na to assess the recovery of 13C in breath, immediately followed by 3) a 3-h infusion of L-[1-13C]leucine. RESULTS: The respiratory quotient tended to be slightly but not significantly higher in the mixed MCT than in the LCT group (0.96+/-0.06 compared with 0.93+/-0.03). We did not detect a significant difference between the mixed MCT and LCT groups with regard to release of leucine from protein breakdown (B; 309+/-40 compared with 257+/-46 micromol x kg(-1) x h(-1)) and nonoxidative leucine disposal (NOLD; 296+/-36 compared with 285+/-49 micromol x kg(-1) x h(-1)). In contrast, leucine oxidation was greater in the mixed MCT than in the LCT group (113+/-10 compared with 67+/-10 micromol x kg(-1) x h(-1); P = 0.007). Net leucine balance (NOLD - B) was less positive in the mixed MCT than in the LCT group (-14+/-9 compared with 28+/-10 micromol x kg(-1) x h(-1); P = 0.011). CONCLUSION: Mixed MCTs may not be as effective as LCT-containing emulsions in promoting protein accretion in parenterally fed preterm neonates. (+info)
Pellagra is characterized by three main symptoms: diarrhea, dermatitis (skin rashes), and dementia or confusion. The disease can be acute or chronic, depending on the severity of the nutritional deficiency.
The disease was first identified in the early 1900s, and it is named after the Italian physician who first described it, Cesare Pellagri. Pellagra was initially thought to be caused by a bacterial or fungal infection, but it was later discovered that the cause was actually a lack of niacin in the diet.
Treatment of pellagra typically involves supplementation with niacin, and the disease is now relatively rare in developed countries where access to a balanced diet is widespread. However, it can still be found in some developing countries where malnutrition is common.
Causes of Hyperammonemia:
1. Liver disease or failure: The liver is responsible for filtering out ammonia, so if it is not functioning properly, ammonia levels can rise.
2. Urea cycle disorders: These are genetic conditions that affect the body's ability to break down protein and produce urea. As a result, ammonia can build up in the bloodstream.
3. Inborn errors of metabolism: Certain inherited disorders can lead to hyperammonemia by affecting the body's ability to process ammonia.
4. Sepsis: Severe infections can cause inflammation in the body, which can lead to hyperammonemia.
5. Kidney disease or failure: If the kidneys are not functioning properly, they may be unable to remove excess ammonia from the bloodstream, leading to hyperammonemia.
Symptoms of Hyperammonemia:
1. Lethargy and confusion
6. Decreased appetite
7. Weight loss
10. Nausea and vomiting
Diagnosis of Hyperammonemia:
1. Blood tests: Measurement of ammonia levels in the blood is the most common method used to diagnose hyperammonemia.
2. Urine tests: Measurement of urea levels in the urine can help determine if the body is able to produce and excrete urea normally.
3. Imaging tests: Imaging tests such as CT or MRI scans may be ordered to look for any underlying liver or kidney damage.
4. Genetic testing: If the cause of hyperammonemia is suspected to be a genetic disorder, genetic testing may be ordered to confirm the diagnosis.
Treatment of Hyperammonemia:
1. Dietary changes: A low-protein diet and avoiding high-aminogram foods can help reduce ammonia production in the body.
2. Medications: Medications such as sodium benzoate, sodium phenylbutyrate, and ribavirin may be used to reduce ammonia production or increase urea production.
3. Dialysis: In severe cases of hyperammonemia, dialysis may be necessary to remove excess ammonia from the blood.
4. Liver transplantation: In cases where the cause of hyperammonemia is liver disease, a liver transplant may be necessary.
5. Nutritional support: Providing adequate nutrition and hydration can help support the body's metabolic processes and prevent complications of hyperammonemia.
Complications of Hyperammonemia:
1. Brain damage: Prolonged elevated ammonia levels in the blood can cause brain damage, leading to cognitive impairment, seizures, and coma.
2. Respiratory failure: Severe hyperammonemia can lead to respiratory failure, which can be life-threatening.
3. Cardiac complications: Hyperammonemia can cause cardiac complications such as arrhythmias and heart failure.
4. Kidney damage: Prolonged elevated ammonia levels in the blood can cause kidney damage and failure.
5. Infections: People with hyperammonemia may be more susceptible to infections due to impaired immune function.
In conclusion, hyperammonemia is a serious condition that can have severe consequences if left untreated. It is essential to identify the underlying cause of hyperammonemia and provide appropriate treatment to prevent complications. Early detection and management of hyperammonemia can improve outcomes and reduce the risk of long-term sequelae.
Without more information about the context in which this term is being used, it is difficult to provide a clear definition or interpretation of its meaning. However, based on the name "Walker" and the fact that it is followed by a number (256), it is possible that this term may refer to a specific type of cancer or tumor that has been identified in a patient with the last name Walker.
It's important to note that the diagnosis and treatment of cancer can be complex and highly individualized, and any medical information or terminology should only be interpreted and applied by qualified healthcare professionals who have access to the relevant clinical context and patient information.
Starvation is a condition where an individual's body does not receive enough nutrients to maintain proper bodily functions and growth. It can be caused by a lack of access to food, poverty, poor nutrition, or other factors that prevent the intake of sufficient calories and essential nutrients. Starvation can lead to severe health consequences, including weight loss, weakness, fatigue, and even death.
Types of Starvation:
There are several types of starvation, each with different causes and effects. These include:
1. Acute starvation: This occurs when an individual suddenly stops eating or has a limited access to food for a short period of time.
2. Chronic starvation: This occurs when an individual consistently does not consume enough calories and nutrients over a longer period of time, leading to gradual weight loss and other health problems.
3. Malnutrition starvation: This occurs when an individual's diet is deficient in essential nutrients, leading to malnutrition and other health problems.
4. Marasmus: This is a severe form of starvation that occurs in children, characterized by extreme weight loss, weakness, and wasting of muscles and organs.
5. Kwashiorkor: This is a form of malnutrition caused by a diet lacking in protein, leading to edema, diarrhea, and other health problems.
Effects of Starvation on the Body:
Starvation can have severe effects on the body, including:
1. Weight loss: Starvation causes weight loss, which can lead to a decrease in muscle mass and a loss of essential nutrients.
2. Fatigue: Starvation can cause fatigue, weakness, and a lack of energy, making it difficult to perform daily activities.
3. Weakened immune system: Starvation can weaken the immune system, making an individual more susceptible to illnesses and infections.
4. Nutrient deficiencies: Starvation can lead to a deficiency of essential nutrients, including vitamins and minerals, which can cause a range of health problems.
5. Increased risk of disease: Starvation can increase the risk of diseases such as tuberculosis, pellagra, and other infections.
6. Mental health issues: Starvation can lead to mental health issues such as depression, anxiety, and irritability.
7. Reproductive problems: Starvation can cause reproductive problems, including infertility and miscarriage.
8. Hair loss: Starvation can cause hair loss, which can be a sign of malnutrition.
9. Skin problems: Starvation can cause skin problems, such as dryness, irritation, and infections.
10. Increased risk of death: Starvation can lead to increased risk of death, especially in children and the elderly.
It is important to note that these effects can be reversed with proper nutrition and care. If you or someone you know is experiencing starvation, it is essential to seek medical attention immediately.
Body weight is an important health indicator, as it can affect an individual's risk for certain medical conditions, such as obesity, diabetes, and cardiovascular disease. Maintaining a healthy body weight is essential for overall health and well-being, and there are many ways to do so, including a balanced diet, regular exercise, and other lifestyle changes.
There are several ways to measure body weight, including:
1. Scale: This is the most common method of measuring body weight, and it involves standing on a scale that displays the individual's weight in kg or lb.
2. Body fat calipers: These are used to measure body fat percentage by pinching the skin at specific points on the body.
3. Skinfold measurements: This method involves measuring the thickness of the skin folds at specific points on the body to estimate body fat percentage.
4. Bioelectrical impedance analysis (BIA): This is a non-invasive method that uses electrical impulses to measure body fat percentage.
5. Dual-energy X-ray absorptiometry (DXA): This is a more accurate method of measuring body composition, including bone density and body fat percentage.
It's important to note that body weight can fluctuate throughout the day due to factors such as water retention, so it's best to measure body weight at the same time each day for the most accurate results. Additionally, it's important to use a reliable scale or measuring tool to ensure accurate measurements.
The infection occurs when these larvae enter the host's body through contaminated food or water, or through contact with infected feces. Once inside the host's body, the larvae migrate to the small intestine, where they attach to the mucosal surface and begin to feed on the host's blood and tissues.
The symptoms of trichostrongylosis can vary depending on the severity of the infection and the species of Trichostrongylus involved. Some common symptoms include:
* Abdominal pain
* Weight loss
If left untreated, trichostrongylosis can lead to serious complications such as intestinal obstruction, hemorrhage, and damage to the host's immune system. Treatment typically involves the use of anthelmintic drugs to eliminate the parasites from the host's body.
Prevention is key in avoiding trichostrongylosis, and this can be achieved through:
* Proper sanitation and hygiene practices
* Avoiding contact with infected animals or their feces
* Using clean water and feed
* Implementing parasite control measures such as deworming programs
It is important for veterinarians to be aware of the risk of trichostrongylosis in the animals they treat, and to take appropriate steps to prevent and diagnose this condition.
Causes and risk factors:
1. Poverty and lack of access to nutritious food
2. Poor sanitation and hygiene
3. Inadequate healthcare and nutritional education
4. Conflict and displacement
5. Chronic illnesses such as HIV/AIDS and tuberculosis
1. Wasting and stunting of children
2. Poor appetite and weight loss
3. Fatigue, weakness, and lethargy
4. Increased susceptibility to infections
5. Poor wound healing and skin problems
1. Stunted growth and development
2. Weakened immune system
3. Increased risk of infections and diseases such as diarrhea, pneumonia, and malaria
4. Poor cognitive development and reduced educational attainment
5. Increased risk of mortality
1. Clinical evaluation of symptoms and physical examination
2. Anthropometric measurements such as height and weight
3. Laboratory tests to assess nutrient deficiencies and infections
4. Dietary assessment to determine food intake and nutrient adequacy
Treatment and prevention:
1. Providing access to nutrient-dense foods, particularly protein-rich foods such as meat, poultry, fish, beans, and dairy products
2. Addressing underlying causes such as poverty and poor sanitation
3. Implementing nutritional education programs to promote healthy eating habits
4. Providing micronutrient supplements and fortified foods
5. Addressing infectious diseases and providing appropriate medical care
In conclusion, protein-energy malnutrition is a serious condition that affects millions of people worldwide, particularly in developing countries. It can have severe consequences on physical growth, cognitive development, and overall health. Early diagnosis and treatment are crucial to prevent long-term health problems and improve quality of life. Addressing underlying causes such as poverty and poor sanitation is also essential to prevent the condition from occurring in the first place.
There are several factors that can contribute to protein deficiency, including:
1. Poor diet: A diet that is lacking in protein-rich foods, such as meat, poultry, fish, eggs, dairy products, legumes, and nuts, can lead to protein deficiency.
2. Vegetarian or vegan diet: People who follow a vegetarian or vegan diet may be at risk of protein deficiency if they do not consume enough protein-rich plant-based foods.
3. Malabsorption: Certain medical conditions, such as celiac disease, can lead to malabsorption of proteins and other nutrients.
4. Pregnancy and breastfeeding: Women who are pregnant or breastfeeding have a higher protein requirement to support the growth and development of their baby.
5. Chronic diseases: Certain chronic diseases, such as kidney disease, can lead to protein deficiency.
Protein deficiency can cause a range of symptoms, including:
1. Fatigue and weakness
2. Muscle wasting and loss of muscle mass
3. Poor wound healing
4. Hair loss
5. Difficulty concentrating and making decisions
6. Mood changes, such as irritability and depression
7. Increased risk of infections
If protein deficiency is not treated, it can lead to a range of complications, including:
1. Stunted growth in children
2. Weakened immune system
3. Poor wound healing
4. Increased risk of infections
5. Nutrient deficiencies
6. Reproductive problems
7. Cardiovascular disease
Treatment for protein deficiency typically involves increasing the intake of protein-rich foods or supplements. The goal is to provide enough protein to support growth and development, as well as overall health and well-being. In some cases, medication may be prescribed to help manage symptoms or address underlying conditions.
In addition to dietary changes, other treatments for protein deficiency may include:
1. Nutritional supplements: Protein supplements can be taken to increase protein intake.
2. Vitamin and mineral supplements: If the protein deficiency is due to a lack of certain vitamins or minerals, supplements may be prescribed.
3. Hormone replacement therapy: In cases where protein deficiency is caused by hormonal imbalances, hormone replacement therapy may be recommended.
4. Medications: Certain medications, such as antidepressants or anti-anxiety drugs, may be prescribed to help manage symptoms of protein deficiency.
5. Addressing underlying conditions: If the protein deficiency is due to an underlying condition, such as kidney disease, treatment will focus on managing that condition.
Preventing protein deficiency is important for maintaining overall health and well-being. Here are some tips for preventing protein deficiency:
1. Eat a balanced diet: Include a variety of protein-rich foods in your diet, such as lean meats, fish, eggs, dairy products, legumes, and nuts.
2. Consult with a healthcare professional: If you are vegetarian or vegan, or if you have certain medical conditions, consult with a healthcare professional to ensure you are getting enough protein.
3. Consider supplements: If you are unable to get enough protein through your diet alone, consider taking protein supplements.
4. Monitor your symptoms: Pay attention to any symptoms of protein deficiency and seek medical attention if they persist or worsen over time.
Overall, preventing protein deficiency is important for maintaining overall health and well-being. If you suspect you or someone you know may have a protein deficiency, it is important to seek medical attention as soon as possible. With proper diagnosis and treatment, protein deficiency can be effectively managed and symptoms can improve.
There are several types of inborn errors of amino acid metabolism, including:
1. Phenylketonuria (PKU): This is the most common inborn error of amino acid metabolism and is caused by a deficiency of the enzyme phenylalanine hydroxylase. This enzyme is needed to break down the amino acid phenylalanine, which is found in many protein-containing foods. If phenylalanine is not properly broken down, it can build up in the blood and brain and cause serious health problems.
2. Maple syrup urine disease (MSUD): This is a rare genetic disorder that affects the breakdown of the amino acids leucine, isoleucine, and valine. These amino acids are important for growth and development, but if they are not properly broken down, they can build up in the blood and cause serious health problems.
3. Homocystinuria: This is a rare genetic disorder that affects the breakdown of the amino acid methionine. Methionine is important for the body's production of proteins and other compounds, but if it is not properly broken down, it can build up in the blood and cause serious health problems.
4. Arginase deficiency: This is a rare genetic disorder that affects the breakdown of the amino acid arginine. Arginine is important for the body's production of nitric oxide, a compound that helps to relax blood vessels and improve blood flow.
5. Citrullinemia: This is a rare genetic disorder that affects the breakdown of the amino acid citrulline. Citrulline is important for the body's production of proteins and other compounds, but if it is not properly broken down, it can build up in the blood and cause serious health problems.
6. Tyrosinemia: This is a rare genetic disorder that affects the breakdown of the amino acid tyrosine. Tyrosine is important for the body's production of proteins and other compounds, but if it is not properly broken down, it can build up in the blood and cause serious health problems.
7. Maple syrup urine disease (MSUD): This is a rare genetic disorder that affects the breakdown of the amino acids leucine, isoleucine, and valine. These amino acids are important for growth and development, but if they are not properly broken down, they can build up in the blood and cause serious health problems.
8. PKU (phenylketonuria): This is a rare genetic disorder that affects the breakdown of the amino acid phenylalanine. Phenylalanine is important for the body's production of proteins and other compounds, but if it is not properly broken down, it can build up in the blood and cause serious health problems.
9. Methionine adenosyltransferase (MAT) deficiency: This is a rare genetic disorder that affects the breakdown of the amino acid methionine. Methionine is important for the body's production of proteins and other compounds, but if it is not properly broken down, it can build up in the blood and cause serious health problems.
10. Homocystinuria: This is a rare genetic disorder that affects the breakdown of the amino acid homocysteine. Homocysteine is important for the body's production of proteins and other compounds, but if it is not properly broken down, it can build up in the blood and cause serious health problems.
It is important to note that these disorders are rare and affect a small percentage of the population. However, they can be serious and potentially life-threatening, so it is important to be aware of them and seek medical attention if symptoms persist or worsen over time.
There are several types of hypertrophy, including:
1. Muscle hypertrophy: The enlargement of muscle fibers due to increased protein synthesis and cell growth, often seen in individuals who engage in resistance training exercises.
2. Cardiac hypertrophy: The enlargement of the heart due to an increase in cardiac workload, often seen in individuals with high blood pressure or other cardiovascular conditions.
3. Adipose tissue hypertrophy: The excessive growth of fat cells, often seen in individuals who are obese or have insulin resistance.
4. Neurological hypertrophy: The enlargement of neural structures such as brain or spinal cord due to an increase in the number of neurons or glial cells, often seen in individuals with neurodegenerative diseases such as Alzheimer's or Parkinson's.
5. Hepatic hypertrophy: The enlargement of the liver due to an increase in the number of liver cells, often seen in individuals with liver disease or cirrhosis.
6. Renal hypertrophy: The enlargement of the kidneys due to an increase in blood flow and filtration, often seen in individuals with kidney disease or hypertension.
7. Ovarian hypertrophy: The enlargement of the ovaries due to an increase in the number of follicles or hormonal imbalances, often seen in individuals with polycystic ovary syndrome (PCOS).
Hypertrophy can be diagnosed through various medical tests such as imaging studies (e.g., CT scans, MRI), biopsies, and blood tests. Treatment options for hypertrophy depend on the underlying cause and may include medications, lifestyle changes, and surgery.
In conclusion, hypertrophy is a growth or enlargement of cells, tissues, or organs in response to an excessive stimulus. It can occur in various parts of the body, including the brain, liver, kidneys, heart, muscles, and ovaries. Understanding the underlying causes and diagnosis of hypertrophy is crucial for effective treatment and management of related health conditions.
Leucine (data page)
Leucine operon leader
Bacterial Leucine Transporter
Leucine carboxyl methyltransferase 1
Leucine-responsive regulatory protein
Leucine rich repeat containing 15
Leucine-sensitive hypoglycemia of infancy
Leucine rich repeat containing 3
Leucine rich repeat containing 61
Phosphatase 2A protein)-leucine-carboxy methyltransferase
Leucine-rich repeat receptor like protein kinase
Basic helix-loop-helix leucine zipper transcription factors
F-box and leucine rich repeat protein 15
Leucine-rich repeats and iq motif containing 1
Leucine-rich repeats and death domain containing 1
Basic leucine zipper and W2 domain-containing protein 2
Acidic leucine-rich nuclear phosphoprotein 32 family member A
Leucine rich repeat and fibronectin type iii domain containing 4
Leucine | Broad Institute
Leucine aminopeptidase - urine: MedlinePlus Medical Encyclopedia
Glucocorticoid-induced leucine zipper 'quantifies' stressors and increases male susceptibility to PTSD
LRCH4 leucine rich repeats and calponin homology domain containing 4 [Homo sapiens (human)] - Gene - NCBI
What is L-Leucine | Organic Facts
Lrig3 MGI Mouse Gene Detail - MGI:2443955 - leucine-rich repeats and immunoglobulin-like domains 3
MPD: Measures involving L-Leucine
Valine, leucine and isoleucine degradation (WP1451) - Caenorhabditis elegans | WikiPathways
Effects of N-Acetyl-L-Leucine on Niemann-Pick Disease Type C (NPC): A Phase III, Randomized, Placebo-controlled, Double-blind,...
L-Leucine Market Size, Share Analysis | Will Experience An Increase In Growth By 2031
Frontiers | Oryza sativa BRASSINOSTEROID UPREGULATED1 LIKE1 Induces the Expression of a Gene Encoding a Small Leucine-Rich...
Retroviral envelope glycoproteins contain a 'leucine zipper'-like repeat - PubMed
NRL neural retina leucine zipper [Homo sapiens (human)] - Gene - NCBI
DailyMed - VITAL SKIN HAIR NAILS- l-alanine, l-arginine, l-carnitine, cysteinum, l-glutamine, l-histidine, l-isoleucine, l...
Leucine - 100 Servings (50% Off) - MAN Sports
What is leucine? - Cibdol
MedlinePlus - Search Results for: ALANINE OR ARGININE OR CHLORIDE ION OR DEXTROSE OR GLYCINE OR HISTIDINE OR ISOLEUCINE OR...
Supplement Direct* L-LEUCINE 500 GRAMS
Example: Topology of a Leucine Amino Acid
418-P: The Branched-Chain Amino Acids Valine and Leucine Predict All-Cause Mortality in Cardiovascular Disease Patients...
Subject: basic-leucine zipper transcription factors and Malus domestica - PubAg Search Results
Honokiol blocks and reverses cardiac hypertrophy in mice by activating mitochondrial Sirt3 | Nature Communications
Cancer outcomes among Parkinson's disease patients with leucine rich repeat kinase 2 mutations, idiopathic Parkinson's disease...
Leucine-rich diet alters the eukaryotic translation initiation factors expression in skeletal muscle of tumour-bearing rats |...
Articles - Tagged 'Leucine' - 5% Nutrition
leucine-rich repeat-containing gene 8
Leucín (L-leucín, L-Leucine) - ScitecPro.sk
- Leucine aminopeptidase is a type of protein called an enzyme. (medlineplus.gov)
- The leucine aminopeptidase (LAP) test measures how much of this enzyme is in your blood. (nih.gov)
- Leucine aminopeptidase 3:a promising serum biomarker candidate for nonalcoholic steatohepatitis diagnosis. (bvsalud.org)
- Increasing evidence demonstrated that aberrant expression of leucine aminopeptidase 3 (LAP3) is involved in NASH. (bvsalud.org)
- Low valine as well as low leucine predicted mortality independently from the presence of T2DM in the total cohort and, in subgroup analysis, specifically in patients with T2DM. (diabetesjournals.org)
- We conclude that low valine and leucine serum levels predict mortality in patients with established CVD independently from the presence of T2DM. (diabetesjournals.org)
- This gene encodes a protein that contains leucine-rich repeats (LRR) at its amino terminus and that is known to be involved in ligand binding. (nih.gov)
- Leucine-rich repeats and calponin homology containing 4 (Lrch4) regulates the innate immune response. (nih.gov)
- Here, we identified a putative downstream gene of OsBUL1, OsBUL1 DOWNSTREAM GENE1 ( OsBDG1 ) encoding a small protein with short leucine-rich-repeats by cDNA microarray analyses in the lamina joint and panicles of wild-type and osbul1 plants. (frontiersin.org)
- LRRK1 is structurally distinct compared to LRRK2, particularly in the position of the leucine-rich repeats relative to the kinase domain. (nih.gov)
- Leucine rich repeats and calponin homology containing protein 4 (Lrch4) is a gene that encodes a protein predicted to have a C-terminal transmembrane domain, a calponin homology domain, and 5-8 leucine rich repeats (LRRs). (nih.gov)
- Leucine possesses a unique molecular structure with a branched side-chain, making it one of only three branched-chain amino acids (or BCAAs) and giving it a major role in muscle growth and maintenance. (nutrivore.com)
- Along with serving as a building block for protein, leucine is one of only two exclusively ketogenic amino acids (meaning it eventually gets metabolized into ketone bodies), and one of only three branched-chain amino acids (referring to the "branched" structure of their molecular side chains). (nutrivore.com)
- Controversly, insulin, other hormones, and branched-chain amino acids, especially leucine, stimulate protein synthesis and modulate the activity of translation initiation factors involved in protein synthesis. (biomedcentral.com)
- Very few studies investigated the effect of long-term supplementation with leucine on body composition. (ast-ss.com)
- Recent research tested the hypothesis that leucine supplementation during most of the adult life of rats might alter body composition by decreasing body fat and attenuating the loss of lean mass, in addition to promoting metabolic risk indicators of acquired chronic diseases . (ast-ss.com)
- Supplementation with leucine attenuated weight gain, body fat accumulation, and hyperleptinemia associated with aging. (ast-ss.com)
- Long-term supplementation with leucine significantly attenuated fat gain as shown by the mass of visceral fat depots and the percentage of total body fat. (ast-ss.com)
- Lipid and glycemic profiles were not affected by leucine supplementation. (ast-ss.com)
- Supplementation with leucine did not prevent loss of body protein and muscle protein during aging. (ast-ss.com)
- Results from this study confirm previous findings showing that leucine supplementation promotes a decrease in body fat . (ast-ss.com)
- Leucine supplementation did not affect the metabolic indicators of acquired chronic diseases (i.e. total cholesterol, triacylglycerol, glycemia). (ast-ss.com)
- In addition, long-term supplementation with leucine was ineffective in attenuating the negative effects of aging on indicators of protein nutritional status such as muscle RNA, protein concentration, total body protein, and lean mass. (ast-ss.com)
- Long-term leucine supplementation reduces fat mass gain without changing body protein status of aging rats. (ast-ss.com)
- Effects of leucine supplementation on the body composition and protein status of rats submitted to food restriction. (ast-ss.com)
- Keep reading to discover more about the purpose of amino acids, foods rich in leucine, and the potential benefits of supplementation. (cibdol.com)
- A higher dose (2.8 g) of leucine compared to a smaller dose (1.7 g) was effective in stimulating protein synthesis is elderly people whereas both these doses stimulated protein synthesis in younger people. (ast-ss.com)
- Postprandial stimulation of muscle protein synthesis in old rats can be restored by a leucine-supplemented meal. (ast-ss.com)
- L-Leucine is a nonessential amino acid that plays an important role in protein synthesis. (einpresswire.com)
- One of several essential amino acids, leucine plays a crucial role in activating muscle protein synthesis. (cibdol.com)
- Leucine-enriched essential amino acids (LEAAs) enhance muscle protein synthesis (MPS) at rest and after exercise. (springeropen.com)
- Although a recent review suggested that CHO should be consumed with protein to maximize muscle hypertrophy by inducing an additive effect of insulin and leucine on protein synthesis (Stark et al. (springeropen.com)
- Leucine is regarded as the most important BCAA, due to being the greatest activator of protein synthesis. (nutrivore.com)
- Through its ability to both increase muscle synthesis and decrease its breakdown, leucine can be beneficial for protecting against sarcopenia (age-related loss of muscle mass). (nutrivore.com)
- Since the tumour effects are more pronounced when associated with pregnancy, ehancing muscle-wasting proteolysis, in this study, the influence of a leucine-rich diet on the protein synthesis caused by cancer were investigated. (biomedcentral.com)
- The results suggest that a leucine-rich diet increased the protein synthesis in skeletal muscle in tumour-bearing rats possibly through the activation of eIF factors and/or the S6kinase pathway. (biomedcentral.com)
- Knowing this, the aim of this study was to examine the effects of a leucine-rich diet on the increased protein degradation and reduced protein synthesis seen in the skeletal muscle of tumour-bearing pregnant rats. (biomedcentral.com)
- L-leucine is one of the nine essential amino acids. (organicfacts.net)
- Amino acids such as L-leucine are the compounds that make protein and protein are what build up our bones and muscles and skin , essentially our bodies! (organicfacts.net)
- It is well known that resistance exercise alone or that followed by the ingestion of essential amino acids (EAA), leucine-enriched essential amino acids (LEAAs), or protein with or without carbohydrate (CHO) increases MPS in humans (Biolo et al. (springeropen.com)
- Leucine is one of the nine essential amino acids that we must consume from our diets, and one of the 20 proteinogenic amino acids (used to create proteins). (nutrivore.com)
- Leucine is one of only two exclusively ketogenic amino acids-meaning it gets metabolized into ketone bodies rather than glucose. (nutrivore.com)
- Leucine (symbol Leu) is one of the nine essential amino acids that we must consume from our diets, and was one of the very first amino acids to be discovered! (nutrivore.com)
- There may be an additive effect of enhancing leucine concentration in the diet coupled with resistance exercise on the same age group as used in this study. (ast-ss.com)
- If you're looking to build muscle, however, you might consider adding leucine supplements to your daily diet. (organicfacts.net)
- NEW YORK CITY, NEW YORK, UNITED STATES, November 10, 2022 / EINPresswire.com / -- L-Leucine is an amino acid that is used in dietary supplements and foods. (einpresswire.com)
- L-Leucine supplements are safe for most people, but there are some side effects that can occur. (einpresswire.com)
- Instead, we must consume external sources, such as leucine-rich foods and supplements, to get the necessary levels. (cibdol.com)
- Due to its effects on insulin, high-dose leucine supplements can cause issues with low blood sugar. (nutrivore.com)
- This study focuses on PTSD markers in the glucocorticoid pathway, spotlighting glucocorticoid-induced leucine zipper (GILZ), a transcription factor encoded by the gene Tsc22d3 on the X chromosome. (nih.gov)
- If a mutation in the HMGCL gene reduces or eliminates the activity of HMG-CoA lyase, the body is unable to process leucine or make ketones properly. (nih.gov)
- The basic leucine zipper (bZIP) family is one of the largest transcription factor (TF) families in plants, which play crucial roles in plant growth and development. (usda.gov)
- Leucine (l-leucine) is a proteinogenic (protein-building) branched-chain amino acid (BCAA) that contributes to various bodily functions. (cibdol.com)
- Leucine is an essential amino acid (meaning we must get it from our diet) that can be used to synthesize protein. (nutrivore.com)
- Leucine biosynthesis in fungi: entering metabolism through the back door. (wikipathways.org)
- Specifically, it is responsible for processing leucine, an amino acid that is part of many proteins. (nih.gov)
- Elderly rats (6 months old) were divided into two groups, one group received 4% leucine for 40 weeks, and the other group received a control diet for 40 weeks. (ast-ss.com)
- three other groups of pregnant rats were fed a leucine-rich diet: L - pregnant leucine, WL - tumour-bearing, and PL - pair-fed, which received the same amount of food as ingested by the WL group. (biomedcentral.com)
- The 2022 market could see another significant year for L-Leucine. (einpresswire.com)
- When leucine is not processed normally, a buildup of chemical byproducts called organic acids can result in metabolic acidosis. (nih.gov)
- The two human leucine-rich repeat kinases (LRRKs), LRRK1 and LRRK2 are large and unusually complex multi-domain kinases which serve to regulate fundamental cellular processes. (nih.gov)
- However, what makes leucine unique is its "essential" status. (cibdol.com)
- The market for L-Leucine is growing due to the health benefits it provides. (einpresswire.com)
- This graph shows the total number of publications written about "Leucine Transaminase" by people in this website by year, and whether "Leucine Transaminase" was a major or minor topic of these publications. (ouhsc.edu)
- Below are the most recent publications written about "Leucine Transaminase" by people in Profiles. (ouhsc.edu)
- When exercise is combined with taking additional leucine, it is known to improve weight loss over exercise alone. (organicfacts.net)
- This report also includes an L-Leucine market growth analysis that incorporates Porter's five-factor analysis as well as supply chain analysis. (einpresswire.com)
- This report provides critical market information, including L-Leucine market size, growth rates and forecasts in key regions and countries, as well as growth opportunities in niche markets. (einpresswire.com)