Alanine Transaminase
Aspartate Aminotransferases
Alanine
Liver
4-Aminobutyrate Transaminase
Drug-Induced Liver Injury
Transaminases
Liver Function Tests
D-Alanine Transaminase
Carbon Tetrachloride
gamma-Glutamyltransferase
Protective Agents
Plant Extracts
Acetaminophen
Galactosamine
Liver Cirrhosis
Alkaline Phosphatase
Liver Cirrhosis, Experimental
Fatty Liver
Alanine Racemase
Biological Markers
Hepatitis B, Chronic
L-Lactate Dehydrogenase
Reperfusion Injury
Analgesics, Non-Narcotic
Rats, Wistar
Lipid Peroxidation
Thiobarbituric Acid Reactive Substances
Hepatitis C, Chronic
Tyrosine Transaminase
Antioxidants
Necrosis
Rats, Sprague-Dawley
Antiviral Agents
Hepatitis C
Disease Models, Animal
Interferon-alpha
Treatment Outcome
Alanine Dehydrogenase
Hepacivirus
Ornithine-Oxo-Acid Transaminase
Aminooxyacetic Acid
Vigabatrin
Predictive Value of Tests
beta-Alanine-Pyruvate Transaminase
Retrospective Studies
Amino Acids
Mice, Inbred C57BL
Pyridoxal Phosphate
Tumor Necrosis Factor-alpha
Isoleucine
Prospective Studies
Ketoglutaric Acids
Amino Acid Sequence
Molecular Sequence Data
Aminobutyrates
Clinical Enzyme Tests
Pyridoxine
Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing)
Mutagenesis, Site-Directed
Glycine Transaminase
Glutamine
Keto Acids
Aspartic Acid
Glutamates
Pyruvates
Mutation
Succinyldiaminopimelate Transaminase
Pyridoxamine
Valerates
Lyases
Valine
Escherichia coli
Kynurenine
Amination
Succinate-Semialdehyde Dehydrogenase
Amino Acid Substitution
Oxaloacetic Acid
Aminocaproates
Serine
Substrate Specificity
Quantitative aspects in the assessment of liver injury. (1/3443)
Liver function data are usually difficult to use in their original form when one wishes to compare the hepatotoxic properties of several chemical substances. However, procedures are available for the conversion of liver function data into quantal responses. These permit the elaboration of dose-response lines for the substances in question, the calculation of median effective doses and the statistical analysis of differences in liver-damaging potency. These same procedures can be utilized for estimating the relative hazard involved if one compares the liver-damaging potency to the median effective dose for some other pharmacologie parameter. Alterations in hepatic triglycerides, lipid peroxidation, and the activities of various hepatic enzymes can also be quantitiated in a dose-related manner. This permits the selection of equitoxic doses required for certain comparative studies and the selection of doses in chemical interaction studies. The quantitative problems involved in low-frequency adverse reactions and the difficulty these present in the detection of liver injury in laboratory animals are discussed. (+info)Activities of citrate synthase, NAD+-linked and NADP+-linked isocitrate dehydrogenases, glutamate dehydrogenase, aspartate aminotransferase and alanine aminotransferase in nervous tissues from vertebrates and invertebrates. (2/3443)
1. The activities of citrate synthase and NAD+-linked and NADP+-linked isocitrate dehydrogenases were measured in nervous tissue from different animals in an attempt to provide more information about the citric acid cycle in this tissue. In higher animals the activities of citrate synthase are greater than the sum of activities of the isocitrate dehydrogenases, whereas they are similar in nervous tissues from the lower animals. This suggests that in higher animals the isocitrate dehydrogenase reaction is far-removed from equilibrium. If it is assumed that isocitrate dehydrogenase activities provide an indication of the maximum flux through the citric acid cycle, the maximum glycolytic capacity in nervous tissue is considerably greater than that of the cycle. This suggest that glycolysis can provide energy in excess of the aerobic capacity of the tissue. 2. The activities of glutamate dehydrogenase are high in most nervous tissues and the activities of aspartate aminotransferase are high in all nervous tissue investigated. However, the activities of alanine aminotransferase are low in all tissues except the ganglia of the waterbug and cockroach. In these insect tissues, anaerobic glycolysis may result in the formation of alanine rather than lactate. (+info)Blockade of type beta transforming growth factor signaling prevents liver fibrosis and dysfunction in the rat. (3/3443)
We eliminated type beta transforming growth factor (TGF-beta) signaling by adenovirus-mediated local expression of a dominant-negative type II TGF-beta receptor (AdCATbeta-TR) in the liver of rats treated with dimethylnitrosamine, a model of persistent liver fibrosis. In rats that received a single application of AdCATbeta-TR via the portal vein, liver fibrosis as assessed by histology and hydroxyproline content was markedly attenuated. All AdCATbeta-TR-treated rats remained alive, and their serum levels of hyaluronic acid and transaminases remained at low levels, whereas all the AdCATbeta-TR-untreated rats died of liver dysfunction. The results demonstrate that TGF-beta does play a central role in liver fibrogenesis and indicate clearly in a persistent fibrosis model that prevention of fibrosis by anti-TGF-beta intervention could be therapeutically useful. (+info)Phase I and pharmacokinetic study of the topoisomerase II catalytic inhibitor fostriecin. (4/3443)
We conducted a phase I and pharmacokinetic study of the topoisomerase II catalytic inhibitor fostriecin. Fostriecin was administered intravenously over 60 min on days 1-5 at 4-week intervals. Dose was escalated from 2 mg m(-2) day(-1) to 20 mg m(-2) day(-1) in 20 patients. Drug pharmacokinetics was analysed with high performance liquid chromatography with UV-detection. Plasma collected during drug administration was tested in vitro for growth inhibition of a teniposide-resistant small-cell lung cancer (SCLC) cell line. The predominant toxicities were elevated liver transaminases (maximum common toxicity criteria (CTC) grade 4) and serum creatinine (maximum CTC grade 2). These showed only a limited increase with increasing doses, often recovered during drug administration and were fully reversible. Duration of elevated alanine-amino transferase (ALT) was dose-limiting in one patient at 20 mg m(-2). Other frequent toxicities were grade 1-2 nausea/vomiting, fever and mild fatigue. Mean fostriecin plasma half-life was 0.36 h (initial; 95% CI, 0-0.76 h) and 1.51 h (terminal; 95% CI, 0.41-2.61 h). A metabolite, most probably dephosphorylated fostriecin, was detected in plasma and urine. No tumour responses were observed, but the plasma concentrations reached in the patients were insufficient to induce significant growth inhibition in vitro. The maximum tolerated dose (MTD) has not been reached, because drug supply was stopped at the 20 mg m(-2) dose level. However, further escalation seems possible and is warranted to achieve potentially effective drug levels. Fostriecin has a short plasma half-life and longer duration of infusion should be considered. (+info)Influences of Kupffer cell stimulation and suppression on immunological liver injury in mice. (5/3443)
AIM: To study the possible involvement of Kupffer cells (KC) in immunological liver injury in mice. METHODS: Liver injury was induced by i.v. injection of Bacillus Calmette-Guerin (BCG) 5 x 10(7) viable bacilli followed by i.v. injection of lipopolysaccharides (LPS) 7.5 micrograms to each mouse. Indian ink and silica were i.v. injected to suppress KC and retinol was given po to stimulate KC in these mice. Plasma alanine aminotransferase (AlaAT), aspatate aminotransferase (AspAT), nitric oxide (NO), and liver tissue were examined. RESULTS: Injection of LPS following BCG injection resulted in a remarkable elevation of plasma NO, AlaAT, and AspAT levels, and severe liver damage. The damages were enhanced by the activation of KC with retinol and reduced by suppression of KC with silica and Indian ink. CONCLUSION: The degree of liver injury induced by BCG + LPS is closely correlated with the status of KC, and NO from KC plays an important role in the pathogenesis of the liver damage in mice. (+info)Effect of epidermal growth factor on cultured rat hepatocytes poisoned by CCl4. (6/3443)
AIM: To study the effects of epidermal growth factor (EGF) on CCl4-induced primary cultured hepatocytes injury. METHODS: Alanine amino-transferase (AlaAT) and aspartate aminotransferase (AspAT) activities and K+ concentractions were determined by the Auto-biochemistry Assay System. Malondialdehyde (MDA) was determined by thiobarbituric acid method. Radioactivity was determined by liquid scintillometry. Light microscopy and electron microscopy were used. RESULTS: EGF 40 micrograms.L-1 decreased CCl4 (10 mmol.L-1)-induced damages of rat primary cultured hepatocytes by decreasing AlaAT and AspAT leakage and MDA production, and promoted RNA and DNA synthesis, with a high positive correlation between intracellular K+ leakage and DNA syntheses (r = 0.99, P < 0.01). Cytopathological study showed that EGF decreased damage of liver cells. CONCLUSION: EGF maintains the stability of cellular lipid membrane and promotes syntheses of RNA and DNA of hepatocytes, and intracellular K+ transference is a promotor of the message transmission of DNA synthesis. (+info)Continuous versus intermittent portal triad clamping for liver resection: a controlled study. (7/3443)
OBJECTIVE: The authors compared the intra- and postoperative course of patients undergoing liver resections under continuous pedicular clamping (CPC) or intermittent pedicular clamping (IPC). SUMMARY BACKGROUND DATA: Reduced blood loss during liver resection is achieved by pedicular clamping. There is controversy about the benefits of IPC over CPC in humans in terms of hepatocellular injury and blood loss control in normal and abnormal liver parenchyma. METHODS: Eighty-six patients undergoing liver resections were included in a prospective randomized study comparing the intra- and postoperative course under CPC (n = 42) or IPC (n = 44) with periods of 15 minutes of clamping and 5 minutes of unclamping. The data were further analyzed according to the presence (steatosis >20% and chronic liver disease) or absence of abnormal liver parenchyma. RESULTS: The two groups of patients were similar in terms of age, sex, nature of the liver tumors, results of preoperative assessment, proportion of patients undergoing major or minor hepatectomy, and nature of nontumorous liver parenchyma. Intraoperative blood loss during liver transsection was significantly higher in the IPC group. In the CPC group, postoperative liver enzymes and serum bilirubin levels were significantly higher in the subgroup of patients with abnormal liver parenchyma. Major postoperative deterioration of liver function occurred in four patients with abnormal liver parenchyma, with two postoperative deaths. All of them were in the CPC group. CONCLUSIONS: This clinical controlled study clearly demonstrated the better parenchymal tolerance to IPC over CPC, especially in patients with abnormal liver parenchyma. (+info)Folate nutriture alters choline status of women and men fed low choline diets. (8/3443)
Choline and folate share methylation pathways and, in studies of rats, were shown to be metabolically inter-related. To determine whether choline status is related to folate intake in humans, we measured the effect of controlled folate depletion and repletion on the plasma choline and phosphatidylcholine concentrations of 11 healthy men (33-46 y) and 10 healthy women (49-63 y) fed low-choline diets in two separate metabolic unit studies. Total folate intake was varied by supplementing low folate (25 and 56 microg/d for men and women, respectively) and low choline (238 and 147 mg/d for men and women, respectively) diets with pteroylglutamic acid for 2-6 wk following folate-depletion periods of 4-5 wk. The low folate/choline intakes resulted in subclinical folate deficiencies; mean plasma choline decreases of 28 and 25% in the men and women, respectively; and a plasma phosphatidylcholine decrease of 26% in the men (P < 0. 05). No functional choline deficiency occurred, as measured by serum transaminase and lipid concentrations. The decreases in choline status measures returned to baseline or higher upon moderate folate repletion and were more responsive to folate repletion than plasma folate and homocysteine. Feeding methionine supplements to the men did not prevent plasma choline depletion, indicating that folate is a more limiting nutrient for these methylation pathways. The results indicate that 1) choline is utilized as a methyl donor when folate intake is low, 2) the de novo synthesis of phosphatidylcholine is insufficient to maintain choline status when intakes of folate and choline are low, and 3) dietary choline is required by adults in an amount > 250 mg/d to maintain plasma choline and phosphatidylcholine when folate intake is low. (+info)Alanine transaminase (ALT) is a type of enzyme found primarily in the cells of the liver and, to a lesser extent, in the cells of other tissues such as the heart, muscles, and kidneys. Its primary function is to catalyze the reversible transfer of an amino group from alanine to another alpha-keto acid, usually pyruvate, to form pyruvate and another amino acid, usually glutamate. This process is known as the transamination reaction.
When liver cells are damaged or destroyed due to various reasons such as hepatitis, alcohol abuse, nonalcoholic fatty liver disease, or drug-induced liver injury, ALT is released into the bloodstream. Therefore, measuring the level of ALT in the blood is a useful diagnostic tool for evaluating liver function and detecting liver damage. Normal ALT levels vary depending on the laboratory, but typically range from 7 to 56 units per liter (U/L) for men and 6 to 45 U/L for women. Elevated ALT levels may indicate liver injury or disease, although other factors such as muscle damage or heart disease can also cause elevations in ALT.
Aspartate aminotransferases (ASTs) are a group of enzymes found in various tissues throughout the body, including the heart, liver, and muscles. They play a crucial role in the metabolic process of transferring amino groups between different molecules.
In medical terms, AST is often used as a blood test to measure the level of this enzyme in the serum. Elevated levels of AST can indicate damage or injury to tissues that contain this enzyme, such as the liver or heart. For example, liver disease, including hepatitis and cirrhosis, can cause elevated AST levels due to damage to liver cells. Similarly, heart attacks can also result in increased AST levels due to damage to heart muscle tissue.
It is important to note that an AST test alone cannot diagnose a specific medical condition, but it can provide valuable information when used in conjunction with other diagnostic tests and clinical evaluation.
Alanine is an alpha-amino acid that is used in the biosynthesis of proteins. The molecular formula for alanine is C3H7NO2. It is a non-essential amino acid, which means that it can be produced by the human body through the conversion of other nutrients, such as pyruvate, and does not need to be obtained directly from the diet.
Alanine is classified as an aliphatic amino acid because it contains a simple carbon side chain. It is also a non-polar amino acid, which means that it is hydrophobic and tends to repel water. Alanine plays a role in the metabolism of glucose and helps to regulate blood sugar levels. It is also involved in the transfer of nitrogen between tissues and helps to maintain the balance of nitrogen in the body.
In addition to its role as a building block of proteins, alanine is also used as a neurotransmitter in the brain and has been shown to have a calming effect on the nervous system. It is found in many foods, including meats, poultry, fish, eggs, dairy products, and legumes.
The liver is a large, solid organ located in the upper right portion of the abdomen, beneath the diaphragm and above the stomach. It plays a vital role in several bodily functions, including:
1. Metabolism: The liver helps to metabolize carbohydrates, fats, and proteins from the food we eat into energy and nutrients that our bodies can use.
2. Detoxification: The liver detoxifies harmful substances in the body by breaking them down into less toxic forms or excreting them through bile.
3. Synthesis: The liver synthesizes important proteins, such as albumin and clotting factors, that are necessary for proper bodily function.
4. Storage: The liver stores glucose, vitamins, and minerals that can be released when the body needs them.
5. Bile production: The liver produces bile, a digestive juice that helps to break down fats in the small intestine.
6. Immune function: The liver plays a role in the immune system by filtering out bacteria and other harmful substances from the blood.
Overall, the liver is an essential organ that plays a critical role in maintaining overall health and well-being.
4-Aminobutyrate transaminase (GABA transaminase or GABA-T) is an enzyme that catalyzes the reversible transfer of an amino group from 4-aminobutyrate (GABA) to 2-oxoglutarate, forming succinic semialdehyde and glutamate. This enzyme plays a crucial role in the metabolism of the major inhibitory neurotransmitter gamma-aminobutyric acid (GABA) in the central nervous system. Inhibition of GABA transaminase is a therapeutic strategy for the treatment of various neurological disorders, such as epilepsy and anxiety, due to its ability to increase GABA levels in the brain.
Drug-Induced Liver Injury (DILI) is a medical term that refers to liver damage or injury caused by the use of medications or drugs. This condition can vary in severity, from mild abnormalities in liver function tests to severe liver failure, which may require a liver transplant.
The exact mechanism of DILI can differ depending on the drug involved, but it generally occurs when the liver metabolizes the drug into toxic compounds that damage liver cells. This can happen through various pathways, including direct toxicity to liver cells, immune-mediated reactions, or metabolic idiosyncrasies.
Symptoms of DILI may include jaundice (yellowing of the skin and eyes), fatigue, abdominal pain, nausea, vomiting, loss of appetite, and dark urine. In severe cases, it can lead to complications such as ascites, encephalopathy, and bleeding disorders.
The diagnosis of DILI is often challenging because it requires the exclusion of other potential causes of liver injury. Liver function tests, imaging studies, and sometimes liver biopsies may be necessary to confirm the diagnosis. Treatment typically involves discontinuing the offending drug and providing supportive care until the liver recovers. In some cases, medications that protect the liver or promote its healing may be used.
Transaminases, also known as aminotransferases, are a group of enzymes found in various tissues of the body, particularly in the liver, heart, muscle, and kidneys. They play a crucial role in the metabolism of amino acids, the building blocks of proteins.
There are two major types of transaminases: aspartate aminotransferase (AST) and alanine aminotransferase (ALT). Both enzymes are normally present in low concentrations in the bloodstream. However, when tissues that contain these enzymes are damaged or injured, such as during liver disease or muscle damage, the levels of AST and ALT in the blood may significantly increase.
Measurement of serum transaminase levels is a common laboratory test used to assess liver function and detect liver injury or damage. Increased levels of these enzymes in the blood can indicate conditions such as hepatitis, liver cirrhosis, drug-induced liver injury, heart attack, and muscle disorders. It's important to note that while elevated transaminase levels may suggest liver disease, they do not specify the type or cause of the condition, and further diagnostic tests are often required for accurate diagnosis and treatment.
Liver function tests (LFTs) are a group of blood tests that are used to assess the functioning and health of the liver. These tests measure the levels of various enzymes, proteins, and waste products that are produced or metabolized by the liver. Some common LFTs include:
1. Alanine aminotransferase (ALT): An enzyme found primarily in the liver, ALT is released into the bloodstream in response to liver cell damage. Elevated levels of ALT may indicate liver injury or disease.
2. Aspartate aminotransferase (AST): Another enzyme found in various tissues, including the liver, heart, and muscles. Like ALT, AST is released into the bloodstream following tissue damage. High AST levels can be a sign of liver damage or other medical conditions.
3. Alkaline phosphatase (ALP): An enzyme found in several organs, including the liver, bile ducts, and bones. Elevated ALP levels may indicate a blockage in the bile ducts, liver disease, or bone disorders.
4. Gamma-glutamyl transferase (GGT): An enzyme found mainly in the liver, pancreas, and biliary system. Increased GGT levels can suggest liver disease, alcohol consumption, or the use of certain medications.
5. Bilirubin: A yellowish pigment produced when hemoglobin from red blood cells is broken down. Bilirubin is processed by the liver and excreted through bile. High bilirubin levels can indicate liver dysfunction, bile duct obstruction, or certain types of anemia.
6. Albumin: A protein produced by the liver that helps maintain fluid balance in the body and transports various substances in the blood. Low albumin levels may suggest liver damage, malnutrition, or kidney disease.
7. Total protein: A measure of all proteins present in the blood, including albumin and other types of proteins produced by the liver. Decreased total protein levels can indicate liver dysfunction or other medical conditions.
These tests are often ordered together as part of a routine health checkup or when evaluating symptoms related to liver function or disease. The results should be interpreted in conjunction with clinical findings, medical history, and other diagnostic tests.
Liver diseases refer to a wide range of conditions that affect the normal functioning of the liver. The liver is a vital organ responsible for various critical functions such as detoxification, protein synthesis, and production of biochemicals necessary for digestion.
Liver diseases can be categorized into acute and chronic forms. Acute liver disease comes on rapidly and can be caused by factors like viral infections (hepatitis A, B, C, D, E), drug-induced liver injury, or exposure to toxic substances. Chronic liver disease develops slowly over time, often due to long-term exposure to harmful agents or inherent disorders of the liver.
Common examples of liver diseases include hepatitis, cirrhosis (scarring of the liver tissue), fatty liver disease, alcoholic liver disease, autoimmune liver diseases, genetic/hereditary liver disorders (like Wilson's disease and hemochromatosis), and liver cancers. Symptoms may vary widely depending on the type and stage of the disease but could include jaundice, abdominal pain, fatigue, loss of appetite, nausea, and weight loss.
Early diagnosis and treatment are essential to prevent progression and potential complications associated with liver diseases.
D-Alanine transaminase (DAT or Dalat) is an enzyme that catalyzes the reversible transfer of an amino group from D-alanine to α-ketoglutarate, producing pyruvate and D-glutamate. It is found in various bacteria and plays a role in their metabolism. However, it is not typically considered a medically significant enzyme in humans, as it is not commonly used as a clinical marker of liver or other organ function.
Carbon tetrachloride is a colorless, heavy, and nonflammable liquid with a mild ether-like odor. Its chemical formula is CCl4. It was previously used as a solvent and refrigerant, but its use has been largely phased out due to its toxicity and ozone-depleting properties.
Inhalation, ingestion, or skin contact with carbon tetrachloride can cause harmful health effects. Short-term exposure can lead to symptoms such as dizziness, headache, nausea, and vomiting. Long-term exposure has been linked to liver and kidney damage, as well as an increased risk of cancer.
Carbon tetrachloride is also a potent greenhouse gas and contributes to climate change. Its production and use are regulated by international agreements aimed at protecting human health and the environment.
Gamma-glutamyltransferase (GGT), also known as gamma-glutamyl transpeptidase, is an enzyme found in many tissues, including the liver, bile ducts, and pancreas. GGT is involved in the metabolism of certain amino acids and plays a role in the detoxification of various substances in the body.
GGT is often measured as a part of a panel of tests used to evaluate liver function. Elevated levels of GGT in the blood may indicate liver disease or injury, bile duct obstruction, or alcohol consumption. However, it's important to note that several other factors can also affect GGT levels, so abnormal results should be interpreted in conjunction with other clinical findings and diagnostic tests.
In the context of medicine and toxicology, protective agents are substances that provide protection against harmful or damaging effects of other substances. They can work in several ways, such as:
1. Binding to toxic substances: Protective agents can bind to toxic substances, rendering them inactive or less active, and preventing them from causing harm. For example, activated charcoal is sometimes used in the emergency treatment of certain types of poisoning because it can bind to certain toxins in the stomach and intestines and prevent their absorption into the body.
2. Increasing elimination: Protective agents can increase the elimination of toxic substances from the body, for example by promoting urinary or biliary excretion.
3. Reducing oxidative stress: Antioxidants are a type of protective agent that can reduce oxidative stress caused by free radicals and reactive oxygen species (ROS). These agents can protect cells and tissues from damage caused by oxidation.
4. Supporting organ function: Protective agents can support the function of organs that have been damaged by toxic substances, for example by improving blood flow or reducing inflammation.
Examples of protective agents include chelating agents, antidotes, free radical scavengers, and anti-inflammatory drugs.
Bilirubin is a yellowish pigment that is produced by the liver when it breaks down old red blood cells. It is a normal byproduct of hemoglobin metabolism and is usually conjugated (made water-soluble) in the liver before being excreted through the bile into the digestive system. Elevated levels of bilirubin can cause jaundice, a yellowing of the skin and eyes. Increased bilirubin levels may indicate liver disease or other medical conditions such as gallstones or hemolysis. It is also measured to assess liver function and to help diagnose various liver disorders.
A plant extract is a preparation containing chemical constituents that have been extracted from a plant using a solvent. The resulting extract may contain a single compound or a mixture of several compounds, depending on the extraction process and the specific plant material used. These extracts are often used in various industries including pharmaceuticals, nutraceuticals, cosmetics, and food and beverage, due to their potential therapeutic or beneficial properties. The composition of plant extracts can vary widely, and it is important to ensure their quality, safety, and efficacy before use in any application.
Acetaminophen is a medication used to relieve pain and reduce fever. It is a commonly used over-the-counter drug and is also available in prescription-strength formulations. Acetaminophen works by inhibiting the production of prostaglandins, chemicals in the body that cause inflammation and trigger pain signals.
Acetaminophen is available in many different forms, including tablets, capsules, liquids, and suppositories. It is often found in combination with other medications, such as cough and cold products, sleep aids, and opioid pain relievers.
While acetaminophen is generally considered safe when used as directed, it can cause serious liver damage or even death if taken in excessive amounts. It is important to follow the dosing instructions carefully and avoid taking more than the recommended dose, especially if you are also taking other medications that contain acetaminophen.
If you have any questions about using acetaminophen or are concerned about potential side effects, it is always best to consult with a healthcare professional.
Galactosamine is not a medical condition but a chemical compound. Medically, it might be referred to in the context of certain medical tests or treatments. Here's the scientific definition:
Galactosamine is an amino sugar, a type of monosaccharide (simple sugar) that contains a functional amino group (-NH2) as well as a hydroxyl group (-OH). More specifically, galactosamine is a derivative of galactose, with the chemical formula C6H13NO5. It is an important component of many glycosaminoglycans (GAGs), which are complex carbohydrates found in animal tissues, particularly in connective tissue and cartilage.
In some medical applications, galactosamine has been used as a building block for the synthesis of GAG analogs or as a component of substrates for enzyme assays. It is also used in research to study various biological processes, such as cell growth and differentiation.
Liver cirrhosis is a chronic, progressive disease characterized by the replacement of normal liver tissue with scarred (fibrotic) tissue, leading to loss of function. The scarring is caused by long-term damage from various sources such as hepatitis, alcohol abuse, nonalcoholic fatty liver disease, and other causes. As the disease advances, it can lead to complications like portal hypertension, fluid accumulation in the abdomen (ascites), impaired brain function (hepatic encephalopathy), and increased risk of liver cancer. It is generally irreversible, but early detection and treatment of underlying causes may help slow down its progression.
Alkaline phosphatase (ALP) is an enzyme found in various body tissues, including the liver, bile ducts, digestive system, bones, and kidneys. It plays a role in breaking down proteins and minerals, such as phosphate, in the body.
The medical definition of alkaline phosphatase refers to its function as a hydrolase enzyme that removes phosphate groups from molecules at an alkaline pH level. In clinical settings, ALP is often measured through blood tests as a biomarker for various health conditions.
Elevated levels of ALP in the blood may indicate liver or bone diseases, such as hepatitis, cirrhosis, bone fractures, or cancer. Therefore, physicians may order an alkaline phosphatase test to help diagnose and monitor these conditions. However, it is essential to interpret ALP results in conjunction with other diagnostic tests and clinical findings for accurate diagnosis and treatment.
Experimental liver cirrhosis refers to a controlled research setting where various factors and substances are intentionally introduced to induce liver cirrhosis in animals or cell cultures. The purpose is to study the mechanisms, progression, potential treatments, and prevention strategies for liver cirrhosis. This could involve administering chemicals, drugs, alcohol, viruses, or manipulating genes associated with liver damage and fibrosis. It's important to note that results from experimental models may not directly translate to human conditions, but they can provide valuable insights into disease pathophysiology and therapeutic development.
Phytotherapy is the use of extracts of natural origin, especially plants or plant parts, for therapeutic purposes. It is also known as herbal medicine and is a traditional practice in many cultures. The active compounds in these plant extracts are believed to have various medicinal properties, such as anti-inflammatory, analgesic, or sedative effects. Practitioners of phytotherapy may use the whole plant, dried parts, or concentrated extracts to prepare teas, capsules, tinctures, or ointments for therapeutic use. It is important to note that the effectiveness and safety of phytotherapy are not always supported by scientific evidence, and it should be used with caution and preferably under the guidance of a healthcare professional.
Fatty liver, also known as hepatic steatosis, is a medical condition characterized by the abnormal accumulation of fat in the liver. The liver's primary function is to process nutrients, filter blood, and fight infections, among other tasks. When excess fat builds up in the liver cells, it can impair liver function and lead to inflammation, scarring, and even liver failure if left untreated.
Fatty liver can be caused by various factors, including alcohol consumption, obesity, nonalcoholic fatty liver disease (NAFLD), viral hepatitis, and certain medications or medical conditions. NAFLD is the most common cause of fatty liver in the United States and other developed countries, affecting up to 25% of the population.
Symptoms of fatty liver may include fatigue, weakness, weight loss, loss of appetite, nausea, abdominal pain or discomfort, and jaundice (yellowing of the skin and eyes). However, many people with fatty liver do not experience any symptoms, making it essential to diagnose and manage the condition through regular check-ups and blood tests.
Treatment for fatty liver depends on the underlying cause. Lifestyle changes such as weight loss, exercise, and dietary modifications are often recommended for people with NAFLD or alcohol-related fatty liver disease. Medications may also be prescribed to manage related conditions such as diabetes, high cholesterol, or metabolic syndrome. In severe cases of liver damage, a liver transplant may be necessary.
Alanine racemase is an enzyme that catalyzes the conversion of the amino acid alanine between its two stereoisomeric forms, D-alanine and L-alanine. This enzyme plays a crucial role in the biosynthesis of peptidoglycan, a major component of bacterial cell walls. In humans, alanine racemase is found in the cytosol of many tissues, including the liver, kidneys, and brain. It is also an important enzyme in the metabolism of amino acids and has been implicated in various disease processes, including neurodegenerative disorders and cancer.
A biological marker, often referred to as a biomarker, is a measurable indicator that reflects the presence or severity of a disease state, or a response to a therapeutic intervention. Biomarkers can be found in various materials such as blood, tissues, or bodily fluids, and they can take many forms, including molecular, histologic, radiographic, or physiological measurements.
In the context of medical research and clinical practice, biomarkers are used for a variety of purposes, such as:
1. Diagnosis: Biomarkers can help diagnose a disease by indicating the presence or absence of a particular condition. For example, prostate-specific antigen (PSA) is a biomarker used to detect prostate cancer.
2. Monitoring: Biomarkers can be used to monitor the progression or regression of a disease over time. For instance, hemoglobin A1c (HbA1c) levels are monitored in diabetes patients to assess long-term blood glucose control.
3. Predicting: Biomarkers can help predict the likelihood of developing a particular disease or the risk of a negative outcome. For example, the presence of certain genetic mutations can indicate an increased risk for breast cancer.
4. Response to treatment: Biomarkers can be used to evaluate the effectiveness of a specific treatment by measuring changes in the biomarker levels before and after the intervention. This is particularly useful in personalized medicine, where treatments are tailored to individual patients based on their unique biomarker profiles.
It's important to note that for a biomarker to be considered clinically valid and useful, it must undergo rigorous validation through well-designed studies, including demonstrating sensitivity, specificity, reproducibility, and clinical relevance.
Chronic Hepatitis B is a persistent infection of the liver caused by the hepatitis B virus (HBV), which can lead to chronic inflammation and scarring of the liver over time. It is defined as the presence of hepatitis B surface antigen (HBsAg) in the blood for more than six months.
The infection can be asymptomatic or may cause nonspecific symptoms such as fatigue, loss of appetite, nausea, and joint pain. A small percentage of people with chronic HBV infection may develop serious complications, including cirrhosis, liver failure, and liver cancer. Treatment options for chronic hepatitis B include antiviral medications that can help to suppress the virus and reduce the risk of liver damage. Vaccination is available to prevent hepatitis B infection.
L-Lactate Dehydrogenase (LDH) is an enzyme found in various tissues within the body, including the heart, liver, kidneys, muscles, and brain. It plays a crucial role in the process of energy production, particularly during anaerobic conditions when oxygen levels are low.
In the presence of the coenzyme NADH, LDH catalyzes the conversion of pyruvate to lactate, generating NAD+ as a byproduct. Conversely, in the presence of NAD+, LDH can convert lactate back to pyruvate using NADH. This reversible reaction is essential for maintaining the balance between lactate and pyruvate levels within cells.
Elevated blood levels of LDH may indicate tissue damage or injury, as this enzyme can be released into the circulation following cellular breakdown. As a result, LDH is often used as a nonspecific biomarker for various medical conditions, such as myocardial infarction (heart attack), liver disease, muscle damage, and certain types of cancer. However, it's important to note that an isolated increase in LDH does not necessarily pinpoint the exact location or cause of tissue damage, and further diagnostic tests are usually required for confirmation.
Reperfusion injury is a complex pathophysiological process that occurs when blood flow is restored to previously ischemic tissues, leading to further tissue damage. This phenomenon can occur in various clinical settings such as myocardial infarction (heart attack), stroke, or peripheral artery disease after an intervention aimed at restoring perfusion.
The restoration of blood flow leads to the generation of reactive oxygen species (ROS) and inflammatory mediators, which can cause oxidative stress, cellular damage, and activation of the immune system. This results in a cascade of events that may lead to microvascular dysfunction, capillary leakage, and tissue edema, further exacerbating the injury.
Reperfusion injury is an important consideration in the management of ischemic events, as interventions aimed at restoring blood flow must be carefully balanced with potential harm from reperfusion injury. Strategies to mitigate reperfusion injury include ischemic preconditioning (exposing the tissue to short periods of ischemia before a prolonged ischemic event), ischemic postconditioning (applying brief periods of ischemia and reperfusion after restoring blood flow), remote ischemic preconditioning (ischemia applied to a distant organ or tissue to protect the target organ), and pharmacological interventions that scavenge ROS, reduce inflammation, or improve microvascular function.
Analgesics, non-narcotic are a class of medications used to relieve pain that do not contain narcotics or opioids. They work by blocking the transmission of pain signals in the nervous system or by reducing inflammation and swelling. Examples of non-narcotic analgesics include acetaminophen (Tylenol), ibuprofen (Advil, Motrin), naproxen (Aleve), and aspirin. These medications are often used to treat mild to moderate pain, such as headaches, menstrual cramps, muscle aches, and arthritis symptoms. They can be obtained over-the-counter or by prescription, depending on the dosage and formulation. It is important to follow the recommended dosages and usage instructions carefully to avoid adverse effects.
"Wistar rats" are a strain of albino rats that are widely used in laboratory research. They were developed at the Wistar Institute in Philadelphia, USA, and were first introduced in 1906. Wistar rats are outbred, which means that they are genetically diverse and do not have a fixed set of genetic characteristics like inbred strains.
Wistar rats are commonly used as animal models in biomedical research because of their size, ease of handling, and relatively low cost. They are used in a wide range of research areas, including toxicology, pharmacology, nutrition, cancer, cardiovascular disease, and behavioral studies. Wistar rats are also used in safety testing of drugs, medical devices, and other products.
Wistar rats are typically larger than many other rat strains, with males weighing between 500-700 grams and females weighing between 250-350 grams. They have a lifespan of approximately 2-3 years. Wistar rats are also known for their docile and friendly nature, making them easy to handle and work with in the laboratory setting.
Lipid peroxidation is a process in which free radicals, such as reactive oxygen species (ROS), steal electrons from lipids containing carbon-carbon double bonds, particularly polyunsaturated fatty acids (PUFAs). This results in the formation of lipid hydroperoxides, which can decompose to form a variety of compounds including reactive carbonyl compounds, aldehydes, and ketones.
Malondialdehyde (MDA) is one such compound that is commonly used as a marker for lipid peroxidation. Lipid peroxidation can cause damage to cell membranes, leading to changes in their fluidity and permeability, and can also result in the modification of proteins and DNA, contributing to cellular dysfunction and ultimately cell death. It is associated with various pathological conditions such as atherosclerosis, neurodegenerative diseases, and cancer.
Thiobarbituric acid reactive substances (TBARS) is not a medical term per se, but rather a method used to measure lipid peroxidation in biological samples. Lipid peroxidation is a process by which free radicals steal electrons from lipids, leading to cellular damage and potential disease progression.
The TBARS assay measures the amount of malondialdehyde (MDA), a byproduct of lipid peroxidation, that reacts with thiobarbituric acid (TBA) to produce a pink-colored complex. The concentration of this complex is then measured and used as an indicator of lipid peroxidation in the sample.
While TBARS has been widely used as a measure of oxidative stress, it has limitations, including potential interference from other compounds that can react with TBA and produce similar-colored complexes. Therefore, more specific and sensitive methods for measuring lipid peroxidation have since been developed.
Chronic Hepatitis C is a liver infection caused by the hepatitis C virus (HCV) that lasts for more than six months. This long-term infection can lead to scarring of the liver (cirrhosis), which can cause serious health problems, such as liver failure or liver cancer, in some individuals. The infection is usually asymptomatic until complications arise, but it can be detected through blood tests that identify antibodies to the virus or viral RNA. Chronic hepatitis C is typically managed with antiviral therapy, which can help clear the virus from the body and reduce the risk of liver damage.
Tyrosine transaminase, also known as tyrosine aminotransferase or TAT, is an enzyme that plays a crucial role in the metabolism of the amino acid tyrosine. This enzyme catalyzes the transfer of an amino group from tyrosine to a ketoacid, such as alpha-ketoglutarate, resulting in the formation of a new amino acid, glutamate, and a ketone derivative of tyrosine.
Tyrosine transaminase is primarily found in the liver and its activity can be used as a biomarker for liver function. Increased levels of this enzyme in the blood may indicate liver damage or disease, such as hepatitis or cirrhosis. Therefore, measuring tyrosine transaminase activity is often part of routine liver function tests.
Antioxidants are substances that can prevent or slow damage to cells caused by free radicals, which are unstable molecules that the body produces as a reaction to environmental and other pressures. Antioxidants are able to neutralize free radicals by donating an electron to them, thus stabilizing them and preventing them from causing further damage to the cells.
Antioxidants can be found in a variety of foods, including fruits, vegetables, nuts, and grains. Some common antioxidants include vitamins C and E, beta-carotene, and selenium. Antioxidants are also available as dietary supplements.
In addition to their role in protecting cells from damage, antioxidants have been studied for their potential to prevent or treat a number of health conditions, including cancer, heart disease, and age-related macular degeneration. However, more research is needed to fully understand the potential benefits and risks of using antioxidant supplements.
Necrosis is the premature death of cells or tissues due to damage or injury, such as from infection, trauma, infarction (lack of blood supply), or toxic substances. It's a pathological process that results in the uncontrolled and passive degradation of cellular components, ultimately leading to the release of intracellular contents into the extracellular space. This can cause local inflammation and may lead to further tissue damage if not treated promptly.
There are different types of necrosis, including coagulative, liquefactive, caseous, fat, fibrinoid, and gangrenous necrosis, each with distinct histological features depending on the underlying cause and the affected tissues or organs.
Sprague-Dawley rats are a strain of albino laboratory rats that are widely used in scientific research. They were first developed by researchers H.H. Sprague and R.C. Dawley in the early 20th century, and have since become one of the most commonly used rat strains in biomedical research due to their relatively large size, ease of handling, and consistent genetic background.
Sprague-Dawley rats are outbred, which means that they are genetically diverse and do not suffer from the same limitations as inbred strains, which can have reduced fertility and increased susceptibility to certain diseases. They are also characterized by their docile nature and low levels of aggression, making them easier to handle and study than some other rat strains.
These rats are used in a wide variety of research areas, including toxicology, pharmacology, nutrition, cancer, and behavioral studies. Because they are genetically diverse, Sprague-Dawley rats can be used to model a range of human diseases and conditions, making them an important tool in the development of new drugs and therapies.
Antiviral agents are a class of medications that are designed to treat infections caused by viruses. Unlike antibiotics, which target bacteria, antiviral agents interfere with the replication and infection mechanisms of viruses, either by inhibiting their ability to replicate or by modulating the host's immune response to the virus.
Antiviral agents are used to treat a variety of viral infections, including influenza, herpes simplex virus (HSV) infections, human immunodeficiency virus (HIV) infection, hepatitis B and C, and respiratory syncytial virus (RSV) infections.
These medications can be administered orally, intravenously, or topically, depending on the type of viral infection being treated. Some antiviral agents are also used for prophylaxis, or prevention, of certain viral infections.
It is important to note that antiviral agents are not effective against all types of viruses and may have significant side effects. Therefore, it is essential to consult with a healthcare professional before starting any antiviral therapy.
Hepatitis C is a liver infection caused by the hepatitis C virus (HCV). It's primarily spread through contact with contaminated blood, often through sharing needles or other equipment to inject drugs. For some people, hepatitis C is a short-term illness but for most — about 75-85% — it becomes a long-term, chronic infection that can lead to serious health problems like liver damage, liver failure, and even liver cancer. The virus can infect and inflame the liver, causing symptoms like jaundice (yellowing of the skin and eyes), abdominal pain, fatigue, and dark urine. Many people with hepatitis C don't have any symptoms, so they might not know they have the infection until they experience complications. There are effective treatments available for hepatitis C, including antiviral medications that can cure the infection in most people. Regular testing is important to diagnose and treat hepatitis C early, before it causes serious health problems.
Animal disease models are specialized animals, typically rodents such as mice or rats, that have been genetically engineered or exposed to certain conditions to develop symptoms and physiological changes similar to those seen in human diseases. These models are used in medical research to study the pathophysiology of diseases, identify potential therapeutic targets, test drug efficacy and safety, and understand disease mechanisms.
The genetic modifications can include knockout or knock-in mutations, transgenic expression of specific genes, or RNA interference techniques. The animals may also be exposed to environmental factors such as chemicals, radiation, or infectious agents to induce the disease state.
Examples of animal disease models include:
1. Mouse models of cancer: Genetically engineered mice that develop various types of tumors, allowing researchers to study cancer initiation, progression, and metastasis.
2. Alzheimer's disease models: Transgenic mice expressing mutant human genes associated with Alzheimer's disease, which exhibit amyloid plaque formation and cognitive decline.
3. Diabetes models: Obese and diabetic mouse strains like the NOD (non-obese diabetic) or db/db mice, used to study the development of type 1 and type 2 diabetes, respectively.
4. Cardiovascular disease models: Atherosclerosis-prone mice, such as ApoE-deficient or LDLR-deficient mice, that develop plaque buildup in their arteries when fed a high-fat diet.
5. Inflammatory bowel disease models: Mice with genetic mutations affecting intestinal barrier function and immune response, such as IL-10 knockout or SAMP1/YitFc mice, which develop colitis.
Animal disease models are essential tools in preclinical research, but it is important to recognize their limitations. Differences between species can affect the translatability of results from animal studies to human patients. Therefore, researchers must carefully consider the choice of model and interpret findings cautiously when applying them to human diseases.
Interferon-alpha (IFN-α) is a type I interferon, which is a group of signaling proteins made and released by host cells in response to the presence of viruses, parasites, and tumor cells. It plays a crucial role in the immune response against viral infections. IFN-α has antiviral, immunomodulatory, and anti-proliferative effects.
IFN-α is produced naturally by various cell types, including leukocytes (white blood cells), fibroblasts, and epithelial cells, in response to viral or bacterial stimulation. It binds to specific receptors on the surface of nearby cells, triggering a signaling cascade that leads to the activation of genes involved in the antiviral response. This results in the production of proteins that inhibit viral replication and promote the presentation of viral antigens to the immune system, enhancing its ability to recognize and eliminate infected cells.
In addition to its role in the immune response, IFN-α has been used as a therapeutic agent for various medical conditions, including certain types of cancer, chronic hepatitis B and C, and multiple sclerosis. However, its use is often limited by side effects such as flu-like symptoms, depression, and neuropsychiatric disorders.
Treatment outcome is a term used to describe the result or effect of medical treatment on a patient's health status. It can be measured in various ways, such as through symptoms improvement, disease remission, reduced disability, improved quality of life, or survival rates. The treatment outcome helps healthcare providers evaluate the effectiveness of a particular treatment plan and make informed decisions about future care. It is also used in clinical research to compare the efficacy of different treatments and improve patient care.
In the field of medicine, "time factors" refer to the duration of symptoms or time elapsed since the onset of a medical condition, which can have significant implications for diagnosis and treatment. Understanding time factors is crucial in determining the progression of a disease, evaluating the effectiveness of treatments, and making critical decisions regarding patient care.
For example, in stroke management, "time is brain," meaning that rapid intervention within a specific time frame (usually within 4.5 hours) is essential to administering tissue plasminogen activator (tPA), a clot-busting drug that can minimize brain damage and improve patient outcomes. Similarly, in trauma care, the "golden hour" concept emphasizes the importance of providing definitive care within the first 60 minutes after injury to increase survival rates and reduce morbidity.
Time factors also play a role in monitoring the progression of chronic conditions like diabetes or heart disease, where regular follow-ups and assessments help determine appropriate treatment adjustments and prevent complications. In infectious diseases, time factors are crucial for initiating antibiotic therapy and identifying potential outbreaks to control their spread.
Overall, "time factors" encompass the significance of recognizing and acting promptly in various medical scenarios to optimize patient outcomes and provide effective care.
Alanine Dehydrogenase (ADH) is an enzyme that catalyzes the reversible conversion between alanine and pyruvate with the reduction of nicotinamide adenine dinucleotide (NAD+) to nicotinamide adenine dinucleotide hydride (NADH). This reaction plays a role in the metabolism of amino acids, particularly in the catabolism of alanine.
In humans, there are multiple isoforms of ADH that are expressed in different tissues and have different functions. The isoform known as ALDH4A1 is primarily responsible for the conversion of alanine to pyruvate in the liver. Deficiencies or mutations in this enzyme can lead to a rare genetic disorder called 4-hydroxybutyric aciduria, which is characterized by elevated levels of 4-hydroxybutyric acid in the urine and neurological symptoms.
Hepacivirus is a genus of viruses in the family Flaviviridae. The most well-known member of this genus is Hepatitis C virus (HCV), which is a major cause of liver disease worldwide. HCV infection can lead to chronic hepatitis, cirrhosis, and liver cancer.
Hepaciviruses are enveloped viruses with a single-stranded, positive-sense RNA genome. They have a small icosahedral capsid and infect a variety of hosts, including humans, non-human primates, horses, and birds. The virus enters the host cell by binding to specific receptors on the cell surface and is then internalized through endocytosis.
HCV has a high degree of genetic diversity and is classified into seven major genotypes and numerous subtypes based on differences in its RNA sequence. This genetic variability can affect the virus's ability to evade the host immune response, making treatment more challenging.
In addition to HCV, other hepaciviruses have been identified in various animal species, including equine hepacivirus (EHCV), rodent hepacivirus (RHV), and bat hepacivirus (BtHepCV). These viruses are being studied to better understand the biology of hepaciviruses and their potential impact on human health.
Ornithine-oxo-acid transaminase (OAT), also known as ornithine aminotransferase, is a urea cycle enzyme that catalyzes the reversible transfer of an amino group from ornithine to α-ketoglutarate, producing glutamate semialdehyde and glutamate. This reaction is an essential part of the urea cycle, which is responsible for the detoxification of ammonia in the body. Deficiencies in OAT can lead to a genetic disorder called ornithine transcarbamylase deficiency (OTCD), which can cause hyperammonemia and neurological symptoms.
Aminooxyacetic acid (AOAA) is a chemical compound that is an irreversible inhibitor of pyridoxal phosphate-dependent enzymes. Pyridoxal phosphate is a cofactor involved in several important biochemical reactions, including the transamination of amino acids. By inhibiting these enzymes, AOAA can alter the normal metabolism of amino acids and other related compounds in the body.
AOAA has been studied for its potential therapeutic uses, such as in the treatment of neurodegenerative disorders like Huntington's disease and epilepsy. However, more research is needed to fully understand its mechanisms of action and potential side effects before it can be used as a routine therapy.
It is important to note that AOAA is not a naturally occurring substance in the human body and should only be used under medical supervision.
Vigabatrin is an anticonvulsant medication used to treat certain types of seizures in adults and children. It works by reducing the abnormal excitement in the brain. The medical definition of Vigabatrin is: a irreversible inhibitor of GABA transaminase, which results in increased levels of gamma-aminobutyric acid (GABA) in the central nervous system. This medication is used as an adjunctive treatment for complex partial seizures and is available in oral form for administration.
It's important to note that Vigabatrin can cause serious side effects, including permanent vision loss, and its use should be closely monitored by a healthcare professional. It is also classified as a pregnancy category C medication, which means it may harm an unborn baby and should only be used during pregnancy if the potential benefit justifies the potential risk to the fetus.
The Predictive Value of Tests, specifically the Positive Predictive Value (PPV) and Negative Predictive Value (NPV), are measures used in diagnostic tests to determine the probability that a positive or negative test result is correct.
Positive Predictive Value (PPV) is the proportion of patients with a positive test result who actually have the disease. It is calculated as the number of true positives divided by the total number of positive results (true positives + false positives). A higher PPV indicates that a positive test result is more likely to be a true positive, and therefore the disease is more likely to be present.
Negative Predictive Value (NPV) is the proportion of patients with a negative test result who do not have the disease. It is calculated as the number of true negatives divided by the total number of negative results (true negatives + false negatives). A higher NPV indicates that a negative test result is more likely to be a true negative, and therefore the disease is less likely to be present.
The predictive value of tests depends on the prevalence of the disease in the population being tested, as well as the sensitivity and specificity of the test. A test with high sensitivity and specificity will generally have higher predictive values than a test with low sensitivity and specificity. However, even a highly sensitive and specific test can have low predictive values if the prevalence of the disease is low in the population being tested.
Beta-alanine-pyruvate transaminase is also known as alanine transaminase 2 (ALT2) or glyoxylate aminotransferase 2 (GATM2). It is an enzyme that catalyzes the reversible transfer of an amino group from beta-alanine to pyruvate, forming alanine and 2-oxoglutarate in the process. This reaction plays a role in the metabolism of certain amino acids and alpha-keto acids in the body.
The gene that encodes this enzyme is located on chromosome 6q14.3 and is expressed primarily in the liver, kidney, and pancreas. Mutations in the GATM2 gene have been associated with certain inherited metabolic disorders, such as hyperglycinuria and primary hyperoxaluria type II.
It's worth noting that beta-alanine-pyruvate transaminase is not to be confused with alanine aminotransferase (ALT), which is a different enzyme that is commonly measured in clinical laboratory tests as a marker of liver function and damage.
Retrospective studies, also known as retrospective research or looking back studies, are a type of observational study that examines data from the past to draw conclusions about possible causal relationships between risk factors and outcomes. In these studies, researchers analyze existing records, medical charts, or previously collected data to test a hypothesis or answer a specific research question.
Retrospective studies can be useful for generating hypotheses and identifying trends, but they have limitations compared to prospective studies, which follow participants forward in time from exposure to outcome. Retrospective studies are subject to biases such as recall bias, selection bias, and information bias, which can affect the validity of the results. Therefore, retrospective studies should be interpreted with caution and used primarily to generate hypotheses for further testing in prospective studies.
Amino acids are organic compounds that serve as the building blocks of proteins. They consist of a central carbon atom, also known as the alpha carbon, which is bonded to an amino group (-NH2), a carboxyl group (-COOH), a hydrogen atom (H), and a variable side chain (R group). The R group can be composed of various combinations of atoms such as hydrogen, oxygen, sulfur, nitrogen, and carbon, which determine the unique properties of each amino acid.
There are 20 standard amino acids that are encoded by the genetic code and incorporated into proteins during translation. These include:
1. Alanine (Ala)
2. Arginine (Arg)
3. Asparagine (Asn)
4. Aspartic acid (Asp)
5. Cysteine (Cys)
6. Glutamine (Gln)
7. Glutamic acid (Glu)
8. Glycine (Gly)
9. Histidine (His)
10. Isoleucine (Ile)
11. Leucine (Leu)
12. Lysine (Lys)
13. Methionine (Met)
14. Phenylalanine (Phe)
15. Proline (Pro)
16. Serine (Ser)
17. Threonine (Thr)
18. Tryptophan (Trp)
19. Tyrosine (Tyr)
20. Valine (Val)
Additionally, there are several non-standard or modified amino acids that can be incorporated into proteins through post-translational modifications, such as hydroxylation, methylation, and phosphorylation. These modifications expand the functional diversity of proteins and play crucial roles in various cellular processes.
Amino acids are essential for numerous biological functions, including protein synthesis, enzyme catalysis, neurotransmitter production, energy metabolism, and immune response regulation. Some amino acids can be synthesized by the human body (non-essential), while others must be obtained through dietary sources (essential).
C57BL/6 (C57 Black 6) is an inbred strain of laboratory mouse that is widely used in biomedical research. The term "inbred" refers to a strain of animals where matings have been carried out between siblings or other closely related individuals for many generations, resulting in a population that is highly homozygous at most genetic loci.
The C57BL/6 strain was established in 1920 by crossing a female mouse from the dilute brown (DBA) strain with a male mouse from the black strain. The resulting offspring were then interbred for many generations to create the inbred C57BL/6 strain.
C57BL/6 mice are known for their robust health, longevity, and ease of handling, making them a popular choice for researchers. They have been used in a wide range of biomedical research areas, including studies of cancer, immunology, neuroscience, cardiovascular disease, and metabolism.
One of the most notable features of the C57BL/6 strain is its sensitivity to certain genetic modifications, such as the introduction of mutations that lead to obesity or impaired glucose tolerance. This has made it a valuable tool for studying the genetic basis of complex diseases and traits.
Overall, the C57BL/6 inbred mouse strain is an important model organism in biomedical research, providing a valuable resource for understanding the genetic and molecular mechanisms underlying human health and disease.
Pyridoxal phosphate (PLP) is the active form of vitamin B6 and functions as a cofactor in various enzymatic reactions in the human body. It plays a crucial role in the metabolism of amino acids, carbohydrates, lipids, and neurotransmitters. Pyridoxal phosphate is involved in more than 140 different enzyme-catalyzed reactions, making it one of the most versatile cofactors in human biochemistry.
As a cofactor, pyridoxal phosphate helps enzymes carry out their functions by facilitating chemical transformations in substrates (the molecules on which enzymes act). In particular, PLP is essential for transamination, decarboxylation, racemization, and elimination reactions involving amino acids. These processes are vital for the synthesis and degradation of amino acids, neurotransmitters, hemoglobin, and other crucial molecules in the body.
Pyridoxal phosphate is formed from the conversion of pyridoxal (a form of vitamin B6) by the enzyme pyridoxal kinase, using ATP as a phosphate donor. The human body obtains vitamin B6 through dietary sources such as whole grains, legumes, vegetables, nuts, and animal products like poultry, fish, and pork. It is essential to maintain adequate levels of pyridoxal phosphate for optimal enzymatic function and overall health.
Tumor Necrosis Factor-alpha (TNF-α) is a cytokine, a type of small signaling protein involved in immune response and inflammation. It is primarily produced by activated macrophages, although other cell types such as T-cells, natural killer cells, and mast cells can also produce it.
TNF-α plays a crucial role in the body's defense against infection and tissue injury by mediating inflammatory responses, activating immune cells, and inducing apoptosis (programmed cell death) in certain types of cells. It does this by binding to its receptors, TNFR1 and TNFR2, which are found on the surface of many cell types.
In addition to its role in the immune response, TNF-α has been implicated in the pathogenesis of several diseases, including autoimmune disorders such as rheumatoid arthritis, inflammatory bowel disease, and psoriasis, as well as cancer, where it can promote tumor growth and metastasis.
Therapeutic agents that target TNF-α, such as infliximab, adalimumab, and etanercept, have been developed to treat these conditions. However, these drugs can also increase the risk of infections and other side effects, so their use must be carefully monitored.
Aspartate aminotransferase (AST), cytoplasmic is an enzyme found primarily in the cytoplasm of hepatic cells and other tissues, including heart, muscle, and kidney. It is also known as aspartate transaminase (AST) or glutamate oxaloacetate transaminase (GOT). This enzyme plays a role in the transfer of an amino group from aspartic acid to alpha-ketoglutarate during amino acid metabolism.
When hepatic cells or other tissues are damaged or injured, AST is released into the bloodstream. Therefore, measuring the level of AST in the blood can help diagnose and monitor liver diseases, heart conditions, muscle damage, and other medical conditions. An elevated cytoplasmic AST level may indicate acute liver injury, hepatitis, cirrhosis, or other liver disorders. However, it is important to note that an isolated increase in AST alone is not specific to the liver and can be seen in various conditions affecting other organs.
In clinical settings, AST levels are often measured along with alanine aminotransferase (ALT) to assess liver function and damage. The ratio of AST to ALT can provide additional information about the type and location of tissue injury.
Isoleucine is an essential branched-chain amino acid, meaning it cannot be synthesized by the human body and must be obtained through dietary sources. Its chemical formula is C6H13NO2. Isoleucine is crucial for muscle protein synthesis, hemoglobin formation, and energy regulation during exercise or fasting. It is found in various foods such as meat, fish, eggs, dairy products, legumes, and nuts. Deficiency of isoleucine may lead to various health issues like muscle wasting, fatigue, and mental confusion.
Prospective studies, also known as longitudinal studies, are a type of cohort study in which data is collected forward in time, following a group of individuals who share a common characteristic or exposure over a period of time. The researchers clearly define the study population and exposure of interest at the beginning of the study and follow up with the participants to determine the outcomes that develop over time. This type of study design allows for the investigation of causal relationships between exposures and outcomes, as well as the identification of risk factors and the estimation of disease incidence rates. Prospective studies are particularly useful in epidemiology and medical research when studying diseases with long latency periods or rare outcomes.
Alpha-ketoglutaric acid, also known as 2-oxoglutarate, is not an acid in the traditional sense but is instead a key molecule in the Krebs cycle (citric acid cycle), which is a central metabolic pathway involved in cellular respiration. Alpha-ketoglutaric acid is a crucial intermediate in the process of converting carbohydrates, fats, and proteins into energy through oxidation. It plays a vital role in amino acid synthesis and the breakdown of certain amino acids. Additionally, it serves as an essential cofactor for various enzymes involved in numerous biochemical reactions within the body. Any medical conditions or disorders related to alpha-ketoglutaric acid would typically be linked to metabolic dysfunctions or genetic defects affecting the Krebs cycle.
An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.
Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.
Aminobutyrates are compounds that contain an amino group (-NH2) and a butyric acid group (-CH2-CH2-CH2-COOH). The most common aminobutyrate is gamma-aminobutyric acid (GABA), which is a major inhibitory neurotransmitter in the central nervous system. GABA plays a crucial role in regulating brain excitability and is involved in various physiological processes, including sleep, memory, and anxiety regulation. Abnormalities in GABAergic neurotransmission have been implicated in several neurological and psychiatric disorders, such as epilepsy, anxiety disorders, and chronic pain. Other aminobutyrates may also have important biological functions, but their roles are less well understood than that of GABA.
Clinical enzyme tests are laboratory tests that measure the amount or activity of certain enzymes in biological samples, such as blood or bodily fluids. These tests are used to help diagnose and monitor various medical conditions, including organ damage, infection, inflammation, and genetic disorders.
Enzymes are proteins that catalyze chemical reactions in the body. Some enzymes are found primarily within specific organs or tissues, so elevated levels of these enzymes in the blood can indicate damage to those organs or tissues. For example, high levels of creatine kinase (CK) may suggest muscle damage, while increased levels of aspartate aminotransferase (AST) and alanine aminotransferase (ALT) can indicate liver damage.
There are several types of clinical enzyme tests, including:
1. Serum enzyme tests: These measure the level of enzymes in the blood serum, which is the liquid portion of the blood after clotting. Examples include CK, AST, ALT, alkaline phosphatase (ALP), and lactate dehydrogenase (LDH).
2. Urine enzyme tests: These measure the level of enzymes in the urine. An example is N-acetyl-β-D-glucosaminidase (NAG), which can indicate kidney damage.
3. Enzyme immunoassays (EIAs): These use antibodies to detect and quantify specific enzymes or proteins in a sample. They are often used for the diagnosis of infectious diseases, such as HIV or hepatitis.
4. Genetic enzyme tests: These can identify genetic mutations that cause deficiencies in specific enzymes, leading to inherited metabolic disorders like phenylketonuria (PKU) or Gaucher's disease.
It is important to note that the interpretation of clinical enzyme test results should be done by a healthcare professional, taking into account the patient's medical history, symptoms, and other diagnostic tests.
Pyridoxine is the chemical name for Vitamin B6. According to the medical definition, Pyridoxine is a water-soluble vitamin that is part of the B-vitamin complex and is essential for the metabolism of proteins, carbohydrates, and fats. It plays a vital role in the regulation of homocysteine levels in the body, the formation of neurotransmitters such as serotonin and dopamine, and the synthesis of hemoglobin.
Pyridoxine can be found naturally in various foods, including whole grains, legumes, vegetables, nuts, seeds, meat, poultry, and fish. It is also available as a dietary supplement and may be prescribed by healthcare providers to treat or prevent certain medical conditions, such as vitamin B6 deficiency, anemia, seizures, and carpal tunnel syndrome.
Like other water-soluble vitamins, Pyridoxine cannot be stored in the body and must be replenished regularly through diet or supplementation. Excessive intake of Pyridoxine can lead to toxicity symptoms such as nerve damage, skin lesions, and light sensitivity.
Aspartate aminotransferase (AST), mitochondrial isoform, is an enzyme found primarily in the mitochondria of cells. It is involved in the transfer of an amino group from aspartic acid to alpha-ketoglutarate, resulting in the formation of oxaloacetate and glutamate. This enzyme plays a crucial role in the cellular energy production process, particularly within the mitochondria.
Elevated levels of AST, mitochondrial isoform, can be found in various medical conditions, including liver disease, muscle damage, and heart injury. However, it's important to note that most clinical laboratories measure a combined level of both cytosolic and mitochondrial AST isoforms when testing for this enzyme. Therefore, the specific contribution of the mitochondrial isoform may not be easily discernible in routine medical tests.
Site-directed mutagenesis is a molecular biology technique used to introduce specific and targeted changes to a specific DNA sequence. This process involves creating a new variant of a gene or a specific region of interest within a DNA molecule by introducing a planned, deliberate change, or mutation, at a predetermined site within the DNA sequence.
The methodology typically involves the use of molecular tools such as PCR (polymerase chain reaction), restriction enzymes, and/or ligases to introduce the desired mutation(s) into a plasmid or other vector containing the target DNA sequence. The resulting modified DNA molecule can then be used to transform host cells, allowing for the production of large quantities of the mutated gene or protein for further study.
Site-directed mutagenesis is a valuable tool in basic research, drug discovery, and biotechnology applications where specific changes to a DNA sequence are required to understand gene function, investigate protein structure/function relationships, or engineer novel biological properties into existing genes or proteins.
In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."
1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.
2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.
3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.
4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).
Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.
Glycine transaminase, also known as alanine-glyoxylate aminotransferase (AGT) or glyoxylate transaminase (GOT2), is an enzyme that plays a role in the metabolism of glyoxylate and glycine. It catalyzes the transfer of an amino group from glycine to glutamate, forming α-ketoglutarate and creatine.
Deficiency of this enzyme can lead to a rare genetic disorder called primary hyperoxaluria type 1 (PH1), which is characterized by the overproduction of oxalate and subsequent deposition in various tissues, leading to kidney stones and kidney failure.
Glutamine is defined as a conditionally essential amino acid in humans, which means that it can be produced by the body under normal circumstances, but may become essential during certain conditions such as stress, illness, or injury. It is the most abundant free amino acid found in the blood and in the muscles of the body.
Glutamine plays a crucial role in various biological processes, including protein synthesis, energy production, and acid-base balance. It serves as an important fuel source for cells in the intestines, immune system, and skeletal muscles. Glutamine has also been shown to have potential benefits in wound healing, gut function, and immunity, particularly during times of physiological stress or illness.
In summary, glutamine is a vital amino acid that plays a critical role in maintaining the health and function of various tissues and organs in the body.
Keto acids, also known as ketone bodies, are not exactly the same as "keto acids" in the context of amino acid metabolism.
In the context of metabolic processes, ketone bodies are molecules that are produced as byproducts when the body breaks down fat for energy instead of carbohydrates. When carbohydrate intake is low, the liver converts fatty acids into ketone bodies, which can be used as a source of energy by the brain and other organs. The three main types of ketone bodies are acetoacetate, beta-hydroxybutyrate, and acetone.
However, in the context of amino acid metabolism, "keto acids" refer to the carbon skeletons of certain amino acids that remain after their nitrogen-containing groups have been removed during the process of deamination. These keto acids can then be converted into glucose or used in other metabolic pathways. For example, the keto acid produced from the amino acid leucine is called beta-ketoisocaproate.
Therefore, it's important to clarify the context when discussing "keto acids" as they can refer to different things depending on the context.
Aspartic acid is an α-amino acid with the chemical formula HO2CCH(NH2)CO2H. It is one of the twenty standard amino acids, and it is a polar, negatively charged, and hydrophilic amino acid. In proteins, aspartic acid usually occurs in its ionized form, aspartate, which has a single negative charge.
Aspartic acid plays important roles in various biological processes, including metabolism, neurotransmitter synthesis, and energy production. It is also a key component of many enzymes and proteins, where it often contributes to the formation of ionic bonds and helps stabilize protein structure.
In addition to its role as a building block of proteins, aspartic acid is also used in the synthesis of other important biological molecules, such as nucleotides, which are the building blocks of DNA and RNA. It is also a component of the dipeptide aspartame, an artificial sweetener that is widely used in food and beverages.
Like other amino acids, aspartic acid is essential for human health, but it cannot be synthesized by the body and must be obtained through the diet. Foods that are rich in aspartic acid include meat, poultry, fish, dairy products, eggs, legumes, and some fruits and vegetables.
Glutamates are the salt or ester forms of glutamic acid, which is a naturally occurring amino acid and the most abundant excitatory neurotransmitter in the central nervous system. Glutamate plays a crucial role in various brain functions, such as learning, memory, and cognition. However, excessive levels of glutamate can lead to neuronal damage or death, contributing to several neurological disorders, including stroke, epilepsy, and neurodegenerative diseases like Alzheimer's and Parkinson's.
Glutamates are also commonly found in food as a natural flavor enhancer, often listed under the name monosodium glutamate (MSG). While MSG has been extensively studied, its safety remains a topic of debate, with some individuals reporting adverse reactions after consuming foods containing this additive.
Pyruvate is a negatively charged ion or group of atoms, called anion, with the chemical formula C3H3O3-. It is formed from the decomposition of glucose and other sugars in the process of cellular respiration. Pyruvate plays a crucial role in the metabolic pathways that generate energy for cells.
In the cytoplasm, pyruvate is produced through glycolysis, where one molecule of glucose is broken down into two molecules of pyruvate, releasing energy and producing ATP (adenosine triphosphate) and NADH (reduced nicotinamide adenine dinucleotide).
In the mitochondria, pyruvate can be further metabolized through the citric acid cycle (also known as the Krebs cycle) to produce more ATP. The process involves the conversion of pyruvate into acetyl-CoA, which then enters the citric acid cycle and undergoes a series of reactions that generate energy in the form of ATP, NADH, and FADH2 (reduced flavin adenine dinucleotide).
Overall, pyruvate is an important intermediate in cellular respiration and plays a central role in the production of energy for cells.
A mutation is a permanent change in the DNA sequence of an organism's genome. Mutations can occur spontaneously or be caused by environmental factors such as exposure to radiation, chemicals, or viruses. They may have various effects on the organism, ranging from benign to harmful, depending on where they occur and whether they alter the function of essential proteins. In some cases, mutations can increase an individual's susceptibility to certain diseases or disorders, while in others, they may confer a survival advantage. Mutations are the driving force behind evolution, as they introduce new genetic variability into populations, which can then be acted upon by natural selection.
Hepatitis is a medical condition characterized by inflammation of the liver, often resulting in damage to liver cells. It can be caused by various factors, including viral infections (such as Hepatitis A, B, C, D, and E), alcohol abuse, toxins, medications, and autoimmune disorders. Symptoms may include jaundice, fatigue, abdominal pain, loss of appetite, nausea, vomiting, and dark urine. The severity of the disease can range from mild illness to severe, life-threatening conditions, such as liver failure or cirrhosis.
Succinyldiaminopimelate transaminase (SDP transaminase) is not a widely recognized or used term in medicine or clinical laboratory science. However, based on its name and the biochemical function implied by "transaminase," it can be inferred that this enzyme is likely involved in the transfer of an amino group from an amino donor to a succinylated diamino pimelic acid molecule during the biosynthesis of certain amino acids, such as lysine or meso-diaminopimelate.
Transaminases are enzymes that catalyze the transfer of an amino group (-NH2) from an α-amino acid to an α-keto acid, thus transforming one molecule into another while also reversibly converting the other molecule into a new amino acid. This reaction is crucial for the intermediary metabolism of amino acids in living organisms.
However, SDP transaminase is not a standard clinical laboratory test and does not have an established medical definition or reference range. It may be a term used in research or biochemistry contexts but is not typically encountered in medical practice or patient care.
Pyridoxamine is a form of vitamin B6, which is a water-soluble vitamin that plays an essential role in the body's protein metabolism, neurotransmitter synthesis, and hemoglobin production. Pyridoxamine is a specific chemical compound that is a derivative of pyridoxine, another form of vitamin B6.
Pyridoxamine functions as a cofactor for various enzymes involved in the metabolism of amino acids, the building blocks of proteins. It helps to convert harmful homocysteine into the essential amino acid methionine, which is important for maintaining normal levels of homocysteine and supporting cardiovascular health.
Pyridoxamine has been studied for its potential role in treating or preventing certain medical conditions, such as diabetic nephropathy and neurodegenerative diseases, due to its antioxidant properties and ability to protect against protein glycation, a process that can damage tissues and contribute to aging and disease. However, more research is needed to establish its safety and efficacy for these uses.
"Valerates" is not a recognized medical term. However, it may refer to a salt or ester of valeric acid, which is a carboxylic acid with the formula CH3CH2CH2CO2H. Valeric acid and its salts and esters are used in pharmaceuticals and perfumes. Valerates can have a sedative effect and are sometimes used as a treatment for anxiety or insomnia. One example is sodium valerate, which is used in the manufacture of some types of medical-grade polyester. Another example is diethyl valerate, an ester of valeric acid that is used as a flavoring agent and solvent.
A lyase is a type of enzyme that catalyzes the breaking of various chemical bonds in a molecule, often resulting in the formation of two new molecules. Lyases differ from other types of enzymes, such as hydrolases and oxidoreductases, because they create double bonds or rings as part of their reaction mechanism.
In the context of medical terminology, lyases are not typically discussed on their own, but rather as a type of enzyme that can be involved in various biochemical reactions within the body. For example, certain lyases play a role in the metabolism of carbohydrates, lipids, and amino acids, among other molecules.
One specific medical application of lyase enzymes is in the diagnosis of certain genetic disorders. For instance, individuals with hereditary fructose intolerance (HFI) lack the enzyme aldolase B, which is a type of lyase that helps break down fructose in the liver. By measuring the activity of aldolase B in a patient's blood or tissue sample, doctors can diagnose HFI and recommend appropriate dietary restrictions to manage the condition.
Overall, while lyases are not a medical diagnosis or condition themselves, they play important roles in various biochemical processes within the body and can be useful in the diagnosis of certain genetic disorders.
Leucine is an essential amino acid, meaning it cannot be produced by the human body and must be obtained through the diet. It is one of the three branched-chain amino acids (BCAAs), along with isoleucine and valine. Leucine is critical for protein synthesis and muscle growth, and it helps to regulate blood sugar levels, promote wound healing, and produce growth hormones.
Leucine is found in various food sources such as meat, dairy products, eggs, and certain plant-based proteins like soy and beans. It is also available as a dietary supplement for those looking to increase their intake for athletic performance or muscle recovery purposes. However, it's important to consult with a healthcare professional before starting any new supplement regimen.
Valine is an essential amino acid, meaning it cannot be produced by the human body and must be obtained through diet. It is a hydrophobic amino acid, with a branched side chain, and is necessary for the growth, repair, and maintenance of tissues in the body. Valine is also important for muscle metabolism, and is often used by athletes as a supplement to enhance physical performance. Like other essential amino acids, valine must be obtained through foods such as meat, fish, dairy products, and legumes.
'Escherichia coli' (E. coli) is a type of gram-negative, facultatively anaerobic, rod-shaped bacterium that commonly inhabits the intestinal tract of humans and warm-blooded animals. It is a member of the family Enterobacteriaceae and one of the most well-studied prokaryotic model organisms in molecular biology.
While most E. coli strains are harmless and even beneficial to their hosts, some serotypes can cause various forms of gastrointestinal and extraintestinal illnesses in humans and animals. These pathogenic strains possess virulence factors that enable them to colonize and damage host tissues, leading to diseases such as diarrhea, urinary tract infections, pneumonia, and sepsis.
E. coli is a versatile organism with remarkable genetic diversity, which allows it to adapt to various environmental niches. It can be found in water, soil, food, and various man-made environments, making it an essential indicator of fecal contamination and a common cause of foodborne illnesses. The study of E. coli has contributed significantly to our understanding of fundamental biological processes, including DNA replication, gene regulation, and protein synthesis.
Kynurenine is an organic compound that is produced in the human body as part of the metabolism of the essential amino acid tryptophan. It is an intermediate in the kynurenine pathway, which leads to the production of several neuroactive compounds and NAD+, a coenzyme involved in redox reactions.
Kynurenine itself does not have any known physiological function, but some of its metabolites have been found to play important roles in various biological processes, including immune response, inflammation, and neurological function. For example, the kynurenine pathway produces several neuroactive metabolites that can act as agonists or antagonists at various receptors in the brain, affecting neuronal excitability, synaptic plasticity, and neurotransmission.
Abnormalities in the kynurenine pathway have been implicated in several neurological disorders, including depression, schizophrenia, Alzheimer's disease, and Huntington's disease. Therefore, understanding the regulation of this pathway and its metabolites has become an important area of research in neuroscience and neuropsychopharmacology.
Amination is a chemical process or reaction that involves the addition of an amino group (-NH2) to a molecule. This process is often used in organic chemistry to create amines, which are compounds containing a basic nitrogen atom with a lone pair of electrons.
In the context of biochemistry, amination reactions play a crucial role in the synthesis of various biological molecules, including amino acids, neurotransmitters, and nucleotides. For example, the enzyme glutamine synthetase catalyzes the amination of glutamate to form glutamine, an essential amino acid for many organisms.
It is important to note that there are different types of amination reactions, depending on the starting molecule and the specific amino group donor. The precise mechanism and reagents used in an amination reaction will depend on the particular chemical or biological context.
Succinate-semialdehyde dehydrogenase (SSDH) is an enzyme involved in the metabolism of the neurotransmitter gamma-aminobutyric acid (GABA). Specifically, SSDH catalyzes the conversion of succinic semialdehyde to succinate in the final step of the GABA degradation pathway. This enzyme plays a critical role in maintaining the balance of GABA levels in the brain and is therefore essential for normal neurological function. Deficiencies or mutations in SSDH can lead to neurological disorders, including developmental delays, intellectual disability, and seizures.
An amino acid substitution is a type of mutation in which one amino acid in a protein is replaced by another. This occurs when there is a change in the DNA sequence that codes for a particular amino acid in a protein. The genetic code is redundant, meaning that most amino acids are encoded by more than one codon (a sequence of three nucleotides). As a result, a single base pair change in the DNA sequence may not necessarily lead to an amino acid substitution. However, if a change does occur, it can have a variety of effects on the protein's structure and function, depending on the nature of the substituted amino acids. Some substitutions may be harmless, while others may alter the protein's activity or stability, leading to disease.
Oxaloacetic acid is a chemical compound that plays a significant role in the Krebs cycle, also known as the citric acid cycle. It is a key metabolic intermediate in both glucose and fatty acid catabolism. Oxaloacetic acid is a four-carbon carboxylic acid that has two carboxyl groups and one ketone group.
In the Krebs cycle, oxaloacetic acid reacts with acetyl-CoA (an activated form of acetic acid) to form citric acid, releasing CoA and initiating the cycle. Throughout the cycle, oxaloacetic acid is continuously regenerated from malate, another intermediate in the cycle.
Additionally, oxaloacetic acid plays a role in amino acid metabolism as it can accept an amino group (NH3) to form aspartic acid, which is an essential component of several biochemical processes, including protein synthesis and the urea cycle.
Aminocaproates are a group of chemical compounds that contain an amino group and a carboxylic acid group, as well as a straight or branched alkyl chain with 6-10 carbon atoms. They are often used in medical settings as anti-fibrinolytic agents, which means they help to prevent the breakdown of blood clots.
One example of an aminocaproate is epsilon-aminocaproic acid (EACA), which is a synthetic analogue of the amino acid lysine. EACA works by inhibiting the activation of plasminogen to plasmin, which is an enzyme that breaks down blood clots. By doing so, EACA can help to reduce bleeding and improve clot stability in certain medical conditions, such as hemophilia or following surgery.
Other aminocaproates include tranexamic acid (TXA) and 4-aminoethylbenzoic acid (AEBA), which also have anti-fibrinolytic properties and are used in similar clinical settings. However, it's important to note that these medications can increase the risk of thrombosis (blood clots) if not used properly, so they should only be administered under the close supervision of a healthcare provider.
Serine is an amino acid, which is a building block of proteins. More specifically, it is a non-essential amino acid, meaning that the body can produce it from other compounds, and it does not need to be obtained through diet. Serine plays important roles in the body, such as contributing to the formation of the protective covering of nerve fibers (myelin sheath), helping to synthesize another amino acid called tryptophan, and taking part in the metabolism of fatty acids. It is also involved in the production of muscle tissues, the immune system, and the forming of cell structures. Serine can be found in various foods such as soy, eggs, cheese, meat, peanuts, lentils, and many others.
Blood chemical analysis, also known as clinical chemistry or chemistry panel, is a series of tests that measure the levels of various chemicals in the blood. These tests can help evaluate the function of organs such as the kidneys and liver, and can also detect conditions such as diabetes and heart disease.
The tests typically include:
* Glucose: to check for diabetes
* Electrolytes (such as sodium, potassium, chloride, and bicarbonate): to check the body's fluid and electrolyte balance
* Calcium: to check for problems with bones, nerves, or kidneys
* Creatinine: to check for kidney function
* Urea Nitrogen (BUN): to check for kidney function
* Albumin: to check for liver function and nutrition status
* ALT (Alanine Transaminase) and AST (Aspartate Transaminase): to check for liver function
* Alkaline Phosphatase: to check for liver or bone disease
* Total Bilirubin: to check for liver function and gallbladder function
* Cholesterol: to check for heart disease risk
* Triglycerides: to check for heart disease risk
These tests are usually ordered by a doctor as part of a routine check-up, or to help diagnose and monitor specific medical conditions. The results of the blood chemical analysis are compared to reference ranges provided by the laboratory performing the test, which take into account factors such as age, sex, and race.
Recombinant proteins are artificially created proteins produced through the use of recombinant DNA technology. This process involves combining DNA molecules from different sources to create a new set of genes that encode for a specific protein. The resulting recombinant protein can then be expressed, purified, and used for various applications in research, medicine, and industry.
Recombinant proteins are widely used in biomedical research to study protein function, structure, and interactions. They are also used in the development of diagnostic tests, vaccines, and therapeutic drugs. For example, recombinant insulin is a common treatment for diabetes, while recombinant human growth hormone is used to treat growth disorders.
The production of recombinant proteins typically involves the use of host cells, such as bacteria, yeast, or mammalian cells, which are engineered to express the desired protein. The host cells are transformed with a plasmid vector containing the gene of interest, along with regulatory elements that control its expression. Once the host cells are cultured and the protein is expressed, it can be purified using various chromatography techniques.
Overall, recombinant proteins have revolutionized many areas of biology and medicine, enabling researchers to study and manipulate proteins in ways that were previously impossible.
Substrate specificity in the context of medical biochemistry and enzymology refers to the ability of an enzyme to selectively bind and catalyze a chemical reaction with a particular substrate (or a group of similar substrates) while discriminating against other molecules that are not substrates. This specificity arises from the three-dimensional structure of the enzyme, which has evolved to match the shape, charge distribution, and functional groups of its physiological substrate(s).
Substrate specificity is a fundamental property of enzymes that enables them to carry out highly selective chemical transformations in the complex cellular environment. The active site of an enzyme, where the catalysis takes place, has a unique conformation that complements the shape and charge distribution of its substrate(s). This ensures efficient recognition, binding, and conversion of the substrate into the desired product while minimizing unwanted side reactions with other molecules.
Substrate specificity can be categorized as:
1. Absolute specificity: An enzyme that can only act on a single substrate or a very narrow group of structurally related substrates, showing no activity towards any other molecule.
2. Group specificity: An enzyme that prefers to act on a particular functional group or class of compounds but can still accommodate minor structural variations within the substrate.
3. Broad or promiscuous specificity: An enzyme that can act on a wide range of structurally diverse substrates, albeit with varying catalytic efficiencies.
Understanding substrate specificity is crucial for elucidating enzymatic mechanisms, designing drugs that target specific enzymes or pathways, and developing biotechnological applications that rely on the controlled manipulation of enzyme activities.
Aminoethylphosphonic acid is a chemical compound with the formula (HO)â‚‚P(O)CHâ‚‚CHâ‚‚NHâ‚‚. It is an organophosphorus compound that contains both phosphonic and amino groups. This compound is a colorless solid that is soluble in water and has various applications in industry, including as a corrosion inhibitor and a scale inhibitor in water treatment systems. It may also have potential uses in medicine, such as in the treatment of kidney stones, although its use in this context is still being studied.
Alanine transaminase
Alanine-oxomalonate transaminase
Alanine-glyoxylate transaminase
Beta-alanine-pyruvate transaminase
Alanine-oxo-acid transaminase
D-amino-acid transaminase
Pyruvic acid
Bonny Light oil
Serine-pyruvate transaminase
Cefovecin
Ribociclib
Transaminase
Grazoprevir
Elevated transaminases
Liver disease
Phenelzine
Valine-pyruvate transaminase
Dicarboxylic aminoaciduria
Hepatic artery thrombosis
Aspartate transaminase
Ruxolitinib
Wilson's disease
Entecavir
Pirfenidone
Primary hyperoxaluria
Glutamic--pyruvic transaminase 2
Tocilizumab
TBC1D10A
4-aminobutyrate transaminase
Α-Ketoglutaric acid
Alanine transaminase - Wikipedia
Alanine Transaminase - SGPT Summary Report | CureHunter
ALT - Alanine Transaminase | Liver Tests - PFPC Fluoride Education Project
ALANINE TRANSAMINASE (SGPT)
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Glutamic-pyruvic transaminase4
- It is also called alanine aminotransferase (ALT or ALAT) and was formerly called serum glutamate-pyruvate transaminase or serum glutamic-pyruvic transaminase (SGPT) and was first characterized in the mid-1950s by Arthur Karmen and colleagues. (wikipedia.org)
- Alanine Transaminase (ALT), also known as Serum Glutamic-Pyruvic Transaminase (SGPT), is an enzyme found primarily in the liver. (prognohealth.com)
- ALT used to be called SGPT, which stands for serum glutamic-pyruvic transaminase. (medlineplus.gov)
- An ALT test is also known as a serum glutamic-pyruvic transaminase (SGPT) test or an alanine transaminase test. (healthline.com)
Aspartate aminotransferase4
- In 2000, the American Association for Clinical Chemistry determined that the appropriate terminology for AST and ALT are aspartate aminotransferase and alanine aminotransferase. (wikipedia.org)
- In vivo , Pts treatment effectively protected against APAP-induced severe liver injury by decreasing the lethality rate, the serum alanine transaminase (ALT) and aspartate aminotransferase (AST) levels, liver histological injury, liver malondialdehyde (MDA) formation and myeloperoxidase (MPO) levels and by increasing liver glutathione (GSH) and superoxide dismutase (SOD) levels. (karger.com)
- Moderate wine drinking showed a significant alanine transaminase (ALT)- and aspartate aminotransferase-lowering effect compared to that of the nondrinkers. (biomedcentral.com)
- The liver enzyme panel tests that checks for inflamation are ALT [Alanine Transaminase] and AST [Aspartate aminotransferase]. (medhelp.org)
Pyruvate and L-glutamate2
- ALT catalyzes the transfer of an amino group from L-alanine to α-ketoglutarate, the products of this reversible transamination reaction being pyruvate and L-glutamate. (wikipedia.org)
- An enzyme that catalyzes the conversion of L-alanine and 2-oxoglutarate to pyruvate and L-glutamate. (curehunter.com)
Assay2
- Alanine Transaminase Microplate Assay Kit-Assay Kit-Bioworld Technology, Inc. (bioworlde.com)
- The enzymatic assay targets alanine and employs alanine transaminase (ALT), pyruvate oxidase (POx), and horseradish peroxidase (HRP). (ojp.gov)
Abnormal2
- Moreover, most cases are biopsied only after 6 months or more of abnormal alanine aminotransferase levels have been documented. (nih.gov)
- We examined whether central adiposity and metabolic markers explain the association of body mass index (BMI as kg/m(2)) with abnormal serum alanine aminotransferase (ALT) activity in a national, population-based study. (nih.gov)
Level4
- Serum ALT level, serum AST (aspartate transaminase) level, and their ratio (AST/ALT ratio) are commonly measured clinically as biomarkers for liver health. (wikipedia.org)
- Their mean serum alanine aminotransferase level at the initiation of therapy was 37.5 +/- 2.1 IU/l with a range of 10-59 (normal values being 40 IU/l or less). (nih.gov)
- 5 A normal alanine transaminase level and/or a normal liver ultrasound does not rule out fibrosis. (cmaj.ca)
- An alanine aminotransferase (ALT) test measures the level of the enzyme ALT in your blood. (healthline.com)
Significantly1
- It is important to note that alanine has a significantly higher concentration than arginine in the fingerprint content of both males and females. (ojp.gov)
Tests1
- Aspartate transaminase Liver function tests Karmen A, Wroblewski F, Ladue JS (January 1955). (wikipedia.org)
Chronic1
- Despite having normal or near normal serum alanine aminotransferase levels, 9 subjects had chronic persistent hepatitis, 13 had chronic active hepatitis and 15 had chronic active hepatitis + cirrhosis documented by histopathologic assessment of their liver biopsies. (nih.gov)
Diagnose1
- Clinicians currently rely on another PCR-based test for the alanine transaminase (ALT) enzyme to diagnose liver toxicity, noted Dear. (genomeweb.com)
Catalyzes1
- It catalyzes the two parts of the alanine cycle. (wikipedia.org)
Activity1
- Detection and Quantification of Alanine Transaminase Activity. (bioworlde.com)
Increase1
- The UL-VWFM disappeared transiently on day 9, but reappeared on day 11, coinciding with a mild increase of transaminase. (wjgnet.com)
Virus1
- RÉSUMÉ Nous avons passé en revue les manifestations dermatologiques liées à l'infection chronique par le virus de l'hépatite C (VHC) et leur rapport avec l'état hépatique. (who.int)
Normal alanine transaminase3
- Approximately 20-30% of patients chronically infected with hepatitis C virus (HCV) have persistently normal alanine transaminase (PNALT) levels. (medscape.com)
- Controversies about the histological features of chronic HCV patients with persistently normal alanine transaminase levels: what can be done about the present definition? (pasteur.fr)
- Improved Performance of Serum Alpha-Fetoprotein for Hepatocellular Carcinoma Diagnosis in HCV Cirrhosis with Normal Alanine Transaminase. (nih.gov)
Aminotransferase5
- It is also called alanine aminotransferase (ALT or ALAT) and was formerly called serum glutamate-pyruvate transaminase or serum glutamic-pyruvic transaminase (SGPT) and was first characterized in the mid-1950s by Arthur Karmen and colleagues. (wikipedia.org)
- In 2000, the American Association for Clinical Chemistry determined that the appropriate terminology for AST and ALT are aspartate aminotransferase and alanine aminotransferase. (wikipedia.org)
- Serum triglyceride (TG), total-cholesterol (T-cho), glucose (Glu), alanine transaminase (ALT), aspartate aminotransferase (AST), alkaline phosphatase (ALP), geranylgeranyltransferase (GGT) and albumin (Alb) levels were measured. (spandidos-publications.com)
- First, look at liver enzymes: alanine transaminase (ALT) or aspartate aminotransferase (AST). (nih.gov)
- Plasma alanine aminotransferase levels, hepatic expression of tumor necrosis factor-α, interleukin-6, fatty acid synthesis-related genes, oxidative stress biomarker 8-hydroxydeoxyguanosine (8-OHdG), and apoptosis marker terminal deoxynucleotidyl transferase-mediated deoxyuridine triphosphate nick-end labeling (TUNEL)-positive cells in the liver were decreased in the HW and PGZ groups. (researchgate.net)
Aspartate transaminase3
- Serum ALT level, serum AST (aspartate transaminase) level, and their ratio (AST/ALT ratio) are commonly measured clinically as biomarkers for liver health. (wikipedia.org)
- Aspartate transaminase Liver function tests Karmen A, Wroblewski F, Ladue JS (January 1955). (wikipedia.org)
- For example, elevated alanine transaminase and aspartate transaminase disproportional to bilirubin and alkaline phosphatase levels often indicates liver disease. (healthline.com)
Elevations1
- Hepatotoxicity: Monitor liver laboratory tests every 2 weeks during the first 3 months of treatment, then once a month and as clinically indicated, with more frequent testing in patients who develop transaminase and bilirubin elevations. (nih.gov)
Serum1
- Is Serum Alanine Transaminase Level a Reliable Marker of Histological Disease in Chronic Hepatitis C Infection? (medscape.com)
Pyruvate2
- ALT catalyzes the transfer of an amino group from L-alanine to α-ketoglutarate, the products of this reversible transamination reaction being pyruvate and L-glutamate. (wikipedia.org)
- citation needed] L-alanine + α-ketoglutarate ⇌ pyruvate + L-glutamate ALT (and all aminotransferases) require the coenzyme pyridoxal phosphate, which is converted into pyridoxamine in the first phase of the reaction, when an amino acid is converted into a keto acid. (wikipedia.org)
Enzyme2
- Alanine transaminase (ALT) is a transaminase enzyme (EC 2.6.1.2). (wikipedia.org)
- The alanine transaminase (ALT) blood test measures the level of the enzyme ALT in the blood. (medlineplus.gov)
Liver disease1
- The term transaminase is outdated and no longer used in liver disease. (wikipedia.org)
Protein1
- Alanine transaminase (ALT) is used by your body to metabolize protein. (healthline.com)
Blood1
- Their blood was used to measure alanine transaminase (ALT), asparagine transaminase (AST), cholesterol, creatinine and glycosylated haemoglobin (HbA 1 C). (aaem.pl)
Greater1
- This research is being done to determine if men with rising PSA after initial therapy for localized prostate cancer who display the Alanine/Alanine SOD2 genotype of MnSOD and supplement their diet with MPX have greater decrease in PSA slope following treatment compared to men that do not supplement with MPX. (dana-farber.org)