A constituent of STRIATED MUSCLE and LIVER. It is an amino acid derivative and an essential cofactor for fatty acid metabolism.
An enzyme that catalyzes reversibly the conversion of palmitoyl-CoA to palmitoylcarnitine in the inner mitochondrial membrane. EC 2.3.1.21.
A key enzyme in SPHINGOLIPIDS biosynthesis, this enzyme catalyzes the pyridoxal-5'-phosphate-dependent condensation of L-SERINE and PALMITOYL COENZYME A to 3-dehydro-D-sphinganine. The enzyme consists of two different subunits.
A coenzyme A derivative which plays a key role in the fatty acid synthesis in the cytoplasmic and microsomal systems.
A fatty acid coenzyme derivative which plays a key role in fatty acid oxidation and biosynthesis.
Enzymes from the transferase class that catalyze the transfer of acyl groups from donor to acceptor, forming either esters or amides. (From Enzyme Nomenclature 1992) EC 2.3.
Acyltransferases in the inner mitochondrial membrane that catalyze the reversible transfer of acyl groups from acyl-CoA to L-carnitine and thereby mediate the transport of activated fatty acids through that membrane. EC 2.3.1.
An enzyme that catalyzes the formation of O-acetylcarnitine from acetyl-CoA plus carnitine. EC 2.3.1.7.
S-Acyl coenzyme A. Fatty acid coenzyme A derivatives that are involved in the biosynthesis and oxidation of fatty acids as well as in ceramide formation.
Mitochondria in hepatocytes. As in all mitochondria, there are an outer membrane and an inner membrane, together creating two separate mitochondrial compartments: the internal matrix space and a much narrower intermembrane space. In the liver mitochondrion, an estimated 67% of the total mitochondrial proteins is located in the matrix. (From Alberts et al., Molecular Biology of the Cell, 2d ed, p343-4)
A long-chain fatty acid ester of carnitine which facilitates the transfer of long-chain fatty acids from cytoplasm into mitochondria during the oxidation of fatty acids.
A class of membrane lipids that have a polar head and two nonpolar tails. They are composed of one molecule of the long-chain amino alcohol sphingosine (4-sphingenine) or one of its derivatives, one molecule of a long-chain acid, a polar head alcohol and sometimes phosphoric acid in diester linkage at the polar head group. (Lehninger et al, Principles of Biochemistry, 2nd ed)
Organic compounds that include a cyclic ether with three ring atoms in their structure. They are commonly used as precursors for POLYMERS such as EPOXY RESINS.
An acetic acid ester of CARNITINE that facilitates movement of ACETYL COA into the matrices of mammalian MITOCHONDRIA during the oxidation of FATTY ACIDS.
A group of inherited disorders characterized by degeneration of dorsal root and autonomic ganglion cells, and clinically by loss of sensation and autonomic dysfunction. There are five subtypes. Type I features autosomal dominant inheritance and distal sensory involvement. Type II is characterized by autosomal inheritance and distal and proximal sensory loss. Type III is DYSAUTONOMIA, FAMILIAL. Type IV features insensitivity to pain, heat intolerance, and mental deficiency. Type V is characterized by a selective loss of pain with intact light touch and vibratory sensation. (From Joynt, Clinical Neurology, 1995, Ch51, pp142-4)
Organic, monobasic acids derived from hydrocarbons by the equivalent of oxidation of a methyl group to an alcohol, aldehyde, and then acid. Fatty acids are saturated and unsaturated (FATTY ACIDS, UNSATURATED). (Grant & Hackh's Chemical Dictionary, 5th ed)
Salts and esters of the 16-carbon saturated monocarboxylic acid--palmitic acid.
Lengthy and continuous deprivation of food. (Stedman, 25th ed)
The metabolic substances ACETONE; 3-HYDROXYBUTYRIC ACID; and acetoacetic acid (ACETOACETATES). They are produced in the liver and kidney during FATTY ACIDS oxidation and used as a source of energy by the heart, muscle and brain.
A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.
A common saturated fatty acid found in fats and waxes including olive oil, palm oil, and body lipids.
A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).
An enzyme that catalyzes the HYDROXYLATION of gamma-butyrobetaine to L-CARNITINE. It is the last enzyme in the biosynthetic pathway of L-CARNITINE and is dependent on alpha-ketoglutarate; IRON; ASCORBIC ACID; and OXYGEN.
Genetically identical individuals developed from brother and sister matings which have been carried out for twenty or more generations or by parent x offspring matings carried out with certain restrictions. This also includes animals with a long history of closed colony breeding.
A family of proteins involved in the transport of organic cations. They play an important role in the elimination of a variety of endogenous substances, xenobiotics, and their metabolites from the body.
The various filaments, granules, tubules or other inclusions within mitochondria.
Errors in the metabolism of LIPIDS resulting from inborn genetic MUTATIONS that are heritable.
A group of 16-carbon fatty acids that contain no double bonds.
Mitochondria of skeletal and smooth muscle. It does not include myocardial mitochondria for which MITOCHONDRIA, HEART is available.
Members of the class of neutral glycosphingolipids. They are the basic units of SPHINGOLIPIDS. They are sphingoids attached via their amino groups to a long chain fatty acyl group. They abnormally accumulate in FABRY DISEASE.
Electron-dense cytoplasmic particles bounded by a single membrane, such as PEROXISOMES; GLYOXYSOMES; and glycosomes.
Covalent attachment of LIPIDS and FATTY ACIDS to other compounds and PROTEINS.
The rate dynamics in chemical or physical systems.
Derivatives of caprylic acid. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain a carboxy terminated eight carbon aliphatic structure.
The mitochondria of the myocardium.
Enzyme that catalyzes the first step of the tricarboxylic acid cycle (CITRIC ACID CYCLE). It catalyzes the reaction of oxaloacetate and acetyl CoA to form citrate and coenzyme A. This enzyme was formerly listed as EC 4.1.3.7.
A genus of gram-negative, aerobic, rod-shaped bacteria characterized by an outer membrane that contains glycosphingolipids but lacks lipopolysaccharide. They have the ability to degrade a broad range of substituted aromatic compounds.
A glycoside obtained from Digitalis purpurea; the aglycone is digitogenin which is bound to five sugars. Digitonin solubilizes lipids, especially in membranes and is used as a tool in cellular biochemistry, and reagent for precipitating cholesterol. It has no cardiac effects.
An enzyme that catalyzes the acyltransferase of SPHINGOSINE to N-acylsphingosine using acyl-COENZYME A as donor and COENZYME A as acceptor. The enzyme is mainly localized in the MITOCHONDRIA.
Thin structures that encapsulate subcellular structures or ORGANELLES in EUKARYOTIC CELLS. They include a variety of membranes associated with the CELL NUCLEUS; the MITOCHONDRIA; the GOLGI APPARATUS; the ENDOPLASMIC RETICULUM; LYSOSOMES; PLASTIDS; and VACUOLES.
Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.
Physiological processes in biosynthesis (anabolism) and degradation (catabolism) of LIPIDS.
A verocytotoxin-producing serogroup belonging to the O subfamily of Escherichia coli which has been shown to cause severe food-borne disease. A strain from this serogroup, serotype H7, which produces SHIGA TOXINS, has been linked to human disease outbreaks resulting from contamination of foods by E. coli O157 from bovine origin.
An amino alcohol with a long unsaturated hydrocarbon chain. Sphingosine and its derivative sphinganine are the major bases of the sphingolipids in mammals. (Dorland, 28th ed)
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
A naturally occurring compound that has been of interest for its role in osmoregulation. As a drug, betaine hydrochloride has been used as a source of hydrochloric acid in the treatment of hypochlorhydria. Betaine has also been used in the treatment of liver disorders, for hyperkalemia, for homocystinuria, and for gastrointestinal disturbances. (From Martindale, The Extra Pharmacopoeia, 30th ed, p1341)
Antibiotic substance produced by Streptomyces garyphalus.
A carboxylating enzyme that catalyzes the conversion of ATP, acetyl-CoA, and HCO3- to ADP, orthophosphate, and malonyl-CoA. It is a biotinyl-protein that also catalyzes transcarboxylation. The plant enzyme also carboxylates propanoyl-CoA and butanoyl-CoA (From Enzyme Nomenclature, 1992) EC 6.4.1.2.
A class of sphingolipids found largely in the brain and other nervous tissue. They contain phosphocholine or phosphoethanolamine as their polar head group so therefore are the only sphingolipids classified as PHOSPHOLIPIDS.
Fatty acids which are unsaturated in only one position.
A group of fatty acids that contain 18 carbon atoms and a double bond at the omega 9 carbon.
Semiautonomous, self-reproducing organelles that occur in the cytoplasm of all cells of most, but not all, eukaryotes. Each mitochondrion is surrounded by a double limiting membrane. The inner membrane is highly invaginated, and its projections are called cristae. Mitochondria are the sites of the reactions of oxidative phosphorylation, which result in the formation of ATP. They contain distinctive RIBOSOMES, transfer RNAs (RNA, TRANSFER); AMINO ACYL T RNA SYNTHETASES; and elongation and termination factors. Mitochondria depend upon genes within the nucleus of the cells in which they reside for many essential messenger RNAs (RNA, MESSENGER). Mitochondria are believed to have arisen from aerobic bacteria that established a symbiotic relationship with primitive protoeukaryotes. (King & Stansfield, A Dictionary of Genetics, 4th ed)
Compounds of the general formula R-O-R arranged in a ring or crown formation.
The muscle tissue of the HEART. It is composed of striated, involuntary muscle cells (MYOCYTES, CARDIAC) connected to form the contractile pump to generate blood flow.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
A subtype of striated muscle, attached by TENDONS to the SKELETON. Skeletal muscles are innervated and their movement can be consciously controlled. They are also called voluntary muscles.
An unsaturated fatty acid that is the most widely distributed and abundant fatty acid in nature. It is used commercially in the preparation of oleates and lotions, and as a pharmaceutical solvent. (Stedman, 26th ed)
A fibric acid derivative used in the treatment of HYPERLIPOPROTEINEMIA TYPE III and severe HYPERTRIGLYCERIDEMIA. (From Martindale, The Extra Pharmacopoeia, 30th ed, p986)
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in enzyme synthesis.
An enzyme that catalyzes the first and rate-determining steps of peroxisomal beta-oxidation of fatty acids. It acts on COENZYME A derivatives of fatty acids with chain lengths from 8 to 18, using FLAVIN-ADENINE DINUCLEOTIDE as a cofactor.
Enzymes that reversibly catalyze the oxidation of a 3-hydroxyacyl CoA to 3-ketoacyl CoA in the presence of NAD. They are key enzymes in the oxidation of fatty acids and in mitochondrial fatty acid synthesis.
A flavoprotein oxidoreductase that has specificity for long-chain fatty acids. It forms a complex with ELECTRON-TRANSFERRING FLAVOPROTEINS and conveys reducing equivalents to UBIQUINONE.
A flavoprotein oxidoreductase that has specificity for medium-chain fatty acids. It forms a complex with ELECTRON TRANSFERRING FLAVOPROTEINS and conveys reducing equivalents to UBIQUINONE.
Contractile tissue that produces movement in animals.
A strain of albino rat developed at the Wistar Institute that has spread widely at other institutions. This has markedly diluted the original strain.
RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.
Yeast-like ascomycetous fungi of the family Saccharomycetaceae, order SACCHAROMYCETALES isolated from exuded tree sap.
The rate at which oxygen is used by a tissue; microliters of oxygen STPD used per milligram of tissue per hour; the rate at which oxygen enters the blood from alveolar gas, equal in the steady state to the consumption of oxygen by tissue metabolism throughout the body. (Stedman, 25th ed, p346)
A nuclear transcription factor. Heterodimerization with RETINOID X RECEPTOR GAMMA is important to metabolism of LIPIDS. It is the target of FIBRATES to control HYPERLIPIDEMIAS.
Enzymes that catalyze the formation of acyl-CoA derivatives. EC 6.2.1.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
An antilipemic agent that lowers CHOLESTEROL and TRIGLYCERIDES. It decreases LOW DENSITY LIPOPROTEINS and increases HIGH DENSITY LIPOPROTEINS.
The process of converting an acid into an alkyl or aryl derivative. Most frequently the process consists of the reaction of an acid with an alcohol in the presence of a trace of mineral acid as catalyst or the reaction of an acyl chloride with an alcohol. Esterification can also be accomplished by enzymatic processes.
A colorless liquid with a sharp burning taste and slight odor. It is used as a local anesthetic and to reduce pain associated with LIDOCAINE injection. Also, it is used in the manufacture of other benzyl compounds, as a pharmaceutic aid, and in perfumery and flavoring.
Purifying or cleansing agents, usually salts of long-chain aliphatic bases or acids, that exert cleansing (oil-dissolving) and antimicrobial effects through a surface action that depends on possessing both hydrophilic and hydrophobic properties.
An enzyme that transfers methyl groups from O(6)-methylguanine, and other methylated moieties of DNA, to a cysteine residue in itself, thus repairing alkylated DNA in a single-step reaction. EC 2.1.1.63.
Amidohydrolases that are specific for the cleavage of the N-acyl linkage of CERAMIDES. Ceramidases are classified as acidic, neutral or basic according to the optimal pH with which they function.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
FATTY ACIDS found in the plasma that are complexed with SERUM ALBUMIN for transport. These fatty acids are not in glycerol ester form.
A condition due to deficiency in any member of the VITAMIN B COMPLEX. These B vitamins are water-soluble and must be obtained from the diet because they are easily lost in the urine. Unlike the lipid-soluble vitamins, they cannot be stored in the body fat.
A group of MYCOTOXINS found in CORN contaminated with FUSARIUM fungus. They are chains of about 20 carbons with acidic ester, acetylamino and sometimes other substituents. They inhibit ceramide synthetase conversion of SPHINGOLIPIDS to CERAMIDES.
Diabetes mellitus induced experimentally by administration of various diabetogenic agents or by PANCREATECTOMY.
The chemical reactions involved in the production and utilization of various forms of energy in cells.
Necrosis or disintegration of skeletal muscle often followed by myoglobinuria.
A life-threatening complication of diabetes mellitus, primarily of TYPE 1 DIABETES MELLITUS with severe INSULIN deficiency and extreme HYPERGLYCEMIA. It is characterized by KETOSIS; DEHYDRATION; and depressed consciousness leading to COMA.
A strain of albino rat used widely for experimental purposes because of its calmness and ease of handling. It was developed by the Sprague-Dawley Animal Company.
Identification of proteins or peptides that have been electrophoretically separated by blot transferring from the electrophoresis gel to strips of nitrocellulose paper, followed by labeling with antibody probes.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.
An enzyme that catalyzes the hydrolysis of sphingomyelin to ceramide (N-acylsphingosine) plus choline phosphate. A defect in this enzyme leads to NIEMANN-PICK DISEASE. EC 3.1.4.12.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.
The addition of an organic acid radical into a molecule.
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.
Refers to animals in the period of time just after birth.
A naturally occurring metabolite of HISTIDINE that has antioxidant properties.
Nonionic surfactant mixtures varying in the number of repeating ethoxy (oxy-1,2-ethanediyl) groups. They are used as detergents, emulsifiers, wetting agents, defoaming agents, etc. Octoxynol-9, the compound with 9 repeating ethoxy groups, is a spermatocide.
Any substances taken in by the body that provide nourishment.
Elements of limited time intervals, contributing to particular results or situations.
The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9)
Single-stranded complementary DNA synthesized from an RNA template by the action of RNA-dependent DNA polymerase. cDNA (i.e., complementary DNA, not circular DNA, not C-DNA) is used in a variety of molecular cloning experiments as well as serving as a specific hybridization probe.
Short sequences (generally about 10 base pairs) of DNA that are complementary to sequences of messenger RNA and allow reverse transcriptases to start copying the adjacent sequences of mRNA. Primers are used extensively in genetic and molecular biology techniques.
BUTYRIC ACID substituted in the beta or 3 position. It is one of the ketone bodies produced in the liver.
Artifactual vesicles formed from the endoplasmic reticulum when cells are disrupted. They are isolated by differential centrifugation and are composed of three structural features: rough vesicles, smooth vesicles, and ribosomes. Numerous enzyme activities are associated with the microsomal fraction. (Glick, Glossary of Biochemistry and Molecular Biology, 1990; from Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed)
Compounds or agents that combine with an enzyme in such a manner as to prevent the normal substrate-enzyme combination and the catalytic reaction.
A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.
The two lipoprotein layers in the MITOCHONDRION. The outer membrane encloses the entire mitochondrion and contains channels with TRANSPORT PROTEINS to move molecules and ions in and out of the organelle. The inner membrane folds into cristae and contains many ENZYMES important to cell METABOLISM and energy production (MITOCHONDRIAL ATP SYNTHASE).
Intracellular signaling protein kinases that play a signaling role in the regulation of cellular energy metabolism. Their activity largely depends upon the concentration of cellular AMP which is increased under conditions of low energy or metabolic stress. AMP-activated protein kinases modify enzymes involved in LIPID METABOLISM, which in turn provide substrates needed to convert AMP into ATP.
An enzyme that catalyzes the synthesis of hydroxymethylglutaryl-CoA from acetyl-CoA and acetoacetyl-CoA. This is a key enzyme in steroid biosynthesis. This enzyme was formerly listed as EC 4.1.3.5.
A form of encephalopathy with fatty infiltration of the LIVER, characterized by brain EDEMA and VOMITING that may rapidly progress to SEIZURES; COMA; and DEATH. It is caused by a generalized loss of mitochondrial function leading to disturbances in fatty acid and CARNITINE metabolism.
Abstaining from all food.
A primary source of energy for living organisms. It is naturally occurring and is found in fruits and other parts of plants in its free state. It is used therapeutically in fluid and nutrient replacement.
The concentration of a compound needed to reduce population growth of organisms, including eukaryotic cells, by 50% in vitro. Though often expressed to denote in vitro antibacterial activity, it is also used as a benchmark for cytotoxicity to eukaryotic cells in culture.
A 51-amino acid pancreatic hormone that plays a major role in the regulation of glucose metabolism, directly by suppressing endogenous glucose production (GLYCOGENOLYSIS; GLUCONEOGENESIS) and indirectly by suppressing GLUCAGON secretion and LIPOLYSIS. Native insulin is a globular protein comprised of a zinc-coordinated hexamer. Each insulin monomer containing two chains, A (21 residues) and B (30 residues), linked by two disulfide bonds. Insulin is used as a drug to control insulin-dependent diabetes mellitus (DIABETES MELLITUS, TYPE 1).
Regular course of eating and drinking adopted by a person or animal.
A thermogenic form of adipose tissue composed of BROWN ADIPOCYTES. It is found in newborns of many species including humans, and in hibernating mammals. Brown fat is richly vascularized, innervated, and densely packed with MITOCHONDRIA which can generate heat directly from the stored lipids.
A 29-amino acid pancreatic peptide derived from proglucagon which is also the precursor of intestinal GLUCAGON-LIKE PEPTIDES. Glucagon is secreted by PANCREATIC ALPHA CELLS and plays an important role in regulation of BLOOD GLUCOSE concentration, ketone metabolism, and several other biochemical and physiological processes. (From Gilman et al., Goodman and Gilman's The Pharmacological Basis of Therapeutics, 9th ed, p1511)
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
A generic term for fats and lipoids, the alcohol-ether-soluble constituents of protoplasm, which are insoluble in water. They comprise the fats, fatty oils, essential oils, waxes, phospholipids, glycolipids, sulfolipids, aminolipids, chromolipids (lipochromes), and fatty acids. (Grant & Hackh's Chemical Dictionary, 5th ed)
Intracellular receptors that can be found in the cytoplasm or in the nucleus. They bind to extracellular signaling molecules that migrate through or are transported across the CELL MEMBRANE. Many members of this class of receptors occur in the cytoplasm and are transported to the CELL NUCLEUS upon ligand-binding where they signal via DNA-binding and transcription regulation. Also included in this category are receptors found on INTRACELLULAR MEMBRANES that act via mechanisms similar to CELL SURFACE RECEPTORS.
Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.
Enzymes that catalyze the synthesis of FATTY ACIDS from acetyl-CoA and malonyl-CoA derivatives.
The phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION.
Transport proteins that carry specific substances in the blood or across cell membranes.
The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION.
Elevated level of AMMONIA in the blood. It is a sign of defective CATABOLISM of AMINO ACIDS or ammonia to UREA.
A family of SERINE ENDOPEPTIDASES isolated from Bacillus subtilis. EC 3.4.21.-
Established cell cultures that have the potential to propagate indefinitely.
Fats present in food, especially in animal products such as meat, meat products, butter, ghee. They are present in lower amounts in nuts, seeds, and avocados.
Techniques to partition various components of the cell into SUBCELLULAR FRACTIONS.
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
Characteristic restricted to a particular organ of the body, such as a cell type, metabolic response or expression of a particular protein or antigen.
Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.
A subfamily in the family MURIDAE, comprising the hamsters. Four of the more common genera are Cricetus, CRICETULUS; MESOCRICETUS; and PHODOPUS.
The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.
An essential amino acid that is required for the production of HISTAMINE.
Hydrazines substituted by one or more methyl groups in any position.
Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.
A toxic thiol mercury salt formerly used as a diuretic. It inhibits various biochemical functions, especially in mitochondria, and is used to study those functions.
The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.
Proteins encoded by the mitochondrial genome or proteins encoded by the nuclear genome that are imported to and resident in the MITOCHONDRIA.
Lipid infiltration of the hepatic parenchymal cells resulting in a yellow-colored liver. The abnormal lipid accumulation is usually in the form of TRIGLYCERIDES, either as a single large droplet or multiple small droplets. Fatty liver is caused by an imbalance in the metabolism of FATTY ACIDS.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control (induction or repression) of gene action at the level of transcription or translation.
A non-essential amino acid that occurs in high levels in its free state in plasma. It is produced from pyruvate by transamination. It is involved in sugar and acid metabolism, increases IMMUNITY, and provides energy for muscle tissue, BRAIN, and the CENTRAL NERVOUS SYSTEM.

Modification of left ventricular hypertrophy by chronic etomixir treatment. (1/672)

1. Etomoxir (2[6(4-chlorophenoxy)hexyl]oxirane-2-carboxylate), an irreversible carnitine palmitoyl-transferase 1 inhibitor, reduces the expression of the myocardial foetal gene programme and the functional deterioration during heart adaption to a pressure-overload. Etomoxir may, however, also improve the depressed myocardial function of hypertrophied ventricles after a prolonged pressure overload. 2. To test this hypothesis, we administered racemic etomoxir (15 mg kg(-1) day(-1) for 6 weeks) to rats with ascending aortic constriction beginning 6 weeks after imposing the pressure overload. 3. The right ventricular/body weight ratio increased (P<0.05) by 20% in etomoxir treated rats (n = 10) versus untreated rats with ascending aortic constriction (n = 10). Left ventricular weight was increased (P<0.05) by 8%. Etomoxir blunted the increase in left ventricular chamber volume. Etomoxir raised the proportion of V1 isomyosin (35+/-4% versus 24+/-2%; P<0.05) and decreased the percentage of V3 isomyosin (36+/-4% versus 48+/-3%; P<0.05). 4. Maximum isovolumically developed pressure was higher in etomoxir treated rats than in untreated pressure overloaded rats (371+/-22 versus 315+/-23 mmHg; P<0.05). Maximum rates of ventricular pressure development (14,800+/-1310 versus 12,340+/-1030mmHg s(-1); P<0.05) and decline (6440+/-750 versus 5040+/-710 mmHg s(-1); P<0.05) were increased as well. Transformation of pressure values to ventricular wall stress data revealed an improved myocardial function which could partially account for the enhanced function of the whole left ventricle. 5. The co-ordinated action of etomoxir on ventricular mass, geometry and myocardial phenotype enhanced thus the pressure generating capacity of hypertrophied pressure-overloaded left ventricles and delayed the deleterious dilative remodelling.  (+info)

Pharmacokinetic analysis of the cardioprotective effect of 3-(2,2, 2-trimethylhydrazinium) propionate in mice: inhibition of carnitine transport in kidney. (2/672)

The site of action of 3-(2,2,2-trimethylhydrazinium) propionate (THP), a new cardioprotective agent, was investigated in mice and rats. I.p. administration of THP decreased the concentrations of free carnitine and long-chain acylcarnitine in heart tissue. In isolated myocytes, THP inhibited free carnitine transport with a Ki of 1340 microM, which is considerably higher than the observed serum concentration of THP. The major cause of the decreased free carnitine concentration in heart was found to be the decreased serum concentration of free carnitine that resulted from the increased renal clearance of carnitine by THP. The estimated Ki of THP for inhibiting the reabsorption of free carnitine in kidneys was 52.2 microM, which is consistent with the serum THP concentration range. No inhibition of THP on the carnitine palmitoyltransferase activity in isolated mitochondrial fractions was observed. These results indicate that the principal site of action of THP as a cardioprotective agent is the carnitine transport carrier in the kidney, but not the carrier in the heart.  (+info)

A single amino acid change (substitution of glutamate 3 with alanine) in the N-terminal region of rat liver carnitine palmitoyltransferase I abolishes malonyl-CoA inhibition and high affinity binding. (3/672)

We have recently shown by deletion mutation analysis that the conserved first 18 N-terminal amino acid residues of rat liver carnitine palmitoyltransferase I (L-CPTI) are essential for malonyl-CoA inhibition and binding (Shi, J., Zhu, H., Arvidson, D. N. , Cregg, J. M., and Woldegiorgis, G. (1998) Biochemistry 37, 11033-11038). To identify specific residue(s) involved in malonyl-CoA binding and inhibition of L-CPTI, we constructed two more deletion mutants, Delta12 and Delta6, and three substitution mutations within the conserved first six amino acid residues. Mutant L-CPTI, lacking either the first six N-terminal amino acid residues or with a change of glutamic acid 3 to alanine, was expressed at steady-state levels similar to wild type and had near wild type catalytic activity. However, malonyl-CoA inhibition of these mutant enzymes was reduced 100-fold, and high affinity malonyl-CoA binding was lost. A mutant L-CPTI with a change of histidine 5 to alanine caused only partial loss of malonyl-CoA inhibition, whereas a mutant L-CPTI with a change of glutamine 6 to alanine had wild type properties. These results demonstrate that glutamic acid 3 and histidine 5 are necessary for malonyl-CoA binding and inhibition of L-CPTI by malonyl-CoA but are not required for catalysis.  (+info)

Comparisons of flux control exerted by mitochondrial outer-membrane carnitine palmitoyltransferase over ketogenesis in hepatocytes and mitochondria isolated from suckling or adult rats. (4/672)

The primary aim of this paper was to calculate and report flux control coefficients for mitochondrial outer-membrane carnitine palmitoyltransferase (CPT I) over hepatic ketogenesis because its role in controlling this pathway during the neonatal period is of academic importance and immediate clinical relevance. Using hepatocytes isolated from suckling rats as our model system, we measured CPT I activity and carbon flux from palmitate to ketone bodies and to CO2 in the absence and presence of a range of concentrations of etomoxir. (This is converted in situ to etomoxir-CoA which is a specific inhibitor of the enzyme.) From these data we calculated the individual flux control coefficients for CPT I over ketogenesis, CO2 production and total carbon flux (0.51 +/- 0.03; -1.30 +/- 0.26; 0.55 +/- 0.07, respectively) and compared them with equivalent coefficients calculated by similar analyses [Drynan, L., Quant, P.A. & Zammit, V.A. (1996) Biochem. J. 317, 791-795] in hepatocytes isolated from adult rats (0.85 +/- 0.20; 0.23 +/- 0.06; 1.06 +/- 0.29). CPT I exerts significantly less control over ketogenesis in hepatocytes isolated from suckling rats than those from adult rats. In the suckling systems the flux control coefficients for CPT I over ketogenesis specifically and over total carbon flux (< 0.6) are not consistent with the enzyme being rate-limiting. Broadly similar results were obtained and conclusions drawn by reanalysis of previous data {from experiments in mitochondria isolated from suckling or adult rats [Krauss, S., Lascelles, C.V., Zammit, V.A. & Quant, P.A. (1996) Biochem. J. 319, 427-433]} using a different approach of control analysis, although it is not strictly valid to compare flux control coefficients from different systems. Our overall conclusion is that flux control coefficients for CPT I over oxidative fluxes from palmitate (or palmitoyl-CoA) differ markedly according to (a) the metabolic state, (b) the stage of development, (c) the specific pathway studied and (d) the model system.  (+info)

Evidence that carnitine palmitoyltransferase I (CPT I) is expressed in microsomes and peroxisomes of rat liver. Distinct immunoreactivity of the N-terminal domain of the microsomal protein. (5/672)

Mitochondria, microsomes and peroxisomes all express overt (cytosol-facing) carnitine palmitoyltransferase activity that is inhibitable by malonyl-CoA. The overt carnitine palmitoyltransferase activity (CPTo) associated with the different fractions was measured. Mitochondria accounted for 65% of total cellular CPTo activity, with the microsomal and peroxisomal contributions accounting for the remaining 25% and 10%, respectively. In parallel experiments, rat livers were perfused in situ with medium containing dinitrophenyl (DNP)-etomoxir in order to inhibit quantitatively and label covalently (with DNP-etomoxiryl-CoA) the molecular species responsible for CPTo activity in each of the membrane systems under near-physiological conditions. In all three membrane fractions, a single protein with an identical molecular mass of approximately 88,000 kDa (p88) was labelled after DNP-etomoxir perfusion of the liver. The abundance of labelled p88 was quantitatively related to the respective specific activities of CPTo in each fraction. On Western blots the same protein was immunoreactive with three anti-peptide antibodies raised against linear epitopes of the cytosolic N- and C-domains and of the inter-membrane space loop (L) domain of the mitochondrial enzyme (L-CPT I). However, the reaction of the microsomal protein with the anti-N peptide antibody (raised against epitope Val-14-Lys-29 of CPT I) was an order of magnitude stronger than expected from either microsomal CPTo activity or its DNP-etomoxiryl-CoA labelling. This suggests that the N-terminal domain of the microsomal protein differs from that in the mitochondrial or peroxisomal protein. This conclusion was confirmed using antibody back-titration experiments, in which the binding of anti-N and anti-C antibodies by mitochondria and microsomes was quantified.  (+info)

Expression of the rat liver carnitine palmitoyltransferase I (CPT-Ialpha) gene is regulated by Sp1 and nuclear factor Y: chromosomal localization and promoter characterization. (6/672)

Carnitine palmitoyltransferase (CPT)-I catalyses the transfer of long-chain fatty acids from CoA to carnitine for translocation across the mitochondrial inner membrane. Expression of the 'liver' isoform of the CPT-I gene (CPT-Ialpha) is subject to developmental, hormonal and tissue-specific regulation. To understand the basis for control of CPT-Ialpha gene expression, we have characterized the proximal promoter of the CPT-Ialpha gene. Here, we report the sequence of 6839 base pairs of the promoter and the localization of the rat CPT-Ialpha gene to region q43 on chromosome 1. Our studies show that the first 200 base pairs of the promoter are sufficient to drive transcription of the CPT-Ialpha gene. Within this region are two sites that bind both Sp1 and Sp3 transcription factors. In addition, nuclear factor Y (NF-Y) binds the proximal promoter. Mutation at the Sp1 or NF-Y sites severely decreases transcription from the CPT-Ialpha promoter. Other protein binding sites were identified within the first 200 base pairs of the promoter by DNase I footprinting, and these elements contribute to CPT-Ialpha gene expression. Our studies demonstrate that CPT-Ialpha is a TATA-less gene which utilizes NF-Y and Sp proteins to drive basal expression.  (+info)

Peroxisome proliferator-activated receptor alpha mediates the adaptive response to fasting. (7/672)

Prolonged deprivation of food induces dramatic changes in mammalian metabolism, including the release of large amounts of fatty acids from the adipose tissue, followed by their oxidation in the liver. The nuclear receptor known as peroxisome proliferator-activated receptor alpha (PPARalpha) was found to play a role in regulating mitochondrial and peroxisomal fatty acid oxidation, suggesting that PPARalpha may be involved in the transcriptional response to fasting. To investigate this possibility, PPARalpha-null mice were subjected to a high fat diet or to fasting, and their responses were compared with those of wild-type mice. PPARalpha-null mice chronically fed a high fat diet showed a massive accumulation of lipid in their livers. A similar phenotype was noted in PPARalpha-null mice fasted for 24 hours, who also displayed severe hypoglycemia, hypoketonemia, hypothermia, and elevated plasma free fatty acid levels, indicating a dramatic inhibition of fatty acid uptake and oxidation. It is shown that to accommodate the increased requirement for hepatic fatty acid oxidation, PPARalpha mRNA is induced during fasting in wild-type mice. The data indicate that PPARalpha plays a pivotal role in the management of energy stores during fasting. By modulating gene expression, PPARalpha stimulates hepatic fatty acid oxidation to supply substrates that can be metabolized by other tissues.  (+info)

Elevated body fat in rats by the dietary nitric oxide synthase inhibitor, L-N omega nitroarginine. (8/672)

The influence of the dietary nitric oxide (NO) synthase inhibitor, L-N omega nitroarginine (L-NNA) on body fat was examined in rats. In experiment 1, all rats were fed with the same amount of diet with or without 0.02% L-NNA for 8 wk. L-NNA intake caused elevations in serum triglyceride and body fat, and reduction in serum nitrate (a metabolite of nitric oxide). The activity of hepatic carnitine palmitoyltransferase was reduced by L-NNA. In experiment 2, rats were fed for 8 wk with the same amount of diets with or without 0.02% L-NNA supplemented or not with 4% L-arginine. The elevation in body fat, and the reductions in serum nitrate and in the activity of hepatic carnitine palmitoyltransferase by L-NNA were all suppressed by supplemental L-arginine. The results suggest that lower NO generation elevated not only serum triglyceride, but also body fat by reduced fatty acid oxidation.  (+info)

There are several types of HSANs, each with distinct clinical features and modes of inheritance. Some of the most common forms of HSANs include:

1. Hereditary sensory and autonomic neuropathy type I (HSANI): This is the most common form of HSAN, also known as Familial Dysautonomia (Riley-Day syndrome). It is caused by a mutation in the IVS gene and affects primarily the sensory and autonomic nerves.
2. Hereditary sensory and autonomic neuropathy type II (HSANII): This form of HSAN is caused by mutations in the PMP22 gene and is characterized by progressive weakness and loss of sensation in the limbs, as well as abnormalities in the functioning of the autonomic nervous system.
3. Hereditary sensory and autonomic neuropathy type III (HSANIII): This form of HSAN is caused by mutations in the GRM1 gene and is characterized by progressive loss of sensation and muscle weakness, as well as abnormalities in the functioning of the autonomic nervous system.
4. Hereditary sensory and autonomic neuropathy type IV (HSANIV): This form of HSAN is caused by mutations in the MAG gene and is characterized by progressive loss of sensation and muscle weakness, as well as abnormalities in the functioning of the autonomic nervous system.

The symptoms of HSANs vary depending on the specific type of disorder and can include:

* Progressive loss of sensation in the hands and feet
* Muscle weakness and wasting
* Abnormalities in the functioning of the autonomic nervous system, such as dysfunction of the cardiovascular and gastrointestinal systems
* Abnormalities in the functioning of the sensory nerves, leading to numbness, tingling, or pain
* Abnormalities in the functioning of the motor nerves, leading to weakness and muscle wasting
* Eye problems, such as optic atrophy or difficulty moving the eyes
* Hearing loss or other ear abnormalities
* Cognitive impairment or developmental delays

There is currently no cure for HSANs, but various treatments can help manage the symptoms. These may include:

* Physical therapy to maintain muscle strength and mobility
* Occupational therapy to improve daily functioning and independence
* Pain management medications and other treatments for neuropathic pain
* Assistive devices, such as canes or wheelchairs, to aid with mobility
* Speech therapy to improve communication skills
* Cognitive and behavioral therapies to help manage cognitive impairment and developmental delays

The progression of HSANs can vary depending on the specific type of disorder and the individual affected. Some forms of HSANs may progress slowly over many years, while others may progress more quickly and have a more severe impact on daily functioning. In some cases, HSANs can be associated with other conditions or diseases that can affect the progression of the disorder. For example, some individuals with HSANs may also have other neurodegenerative diseases, such as amyotrophic lateral sclerosis (ALS) or Alzheimer's disease.

HSANs are rare disorders, and there is currently no cure. However, research into the genetic causes of these disorders is ongoing, and new treatments and therapies are being developed to help manage the symptoms and slow the progression of the disorders. With proper management and support, individuals with HSANs can lead fulfilling lives and achieve their goals.

Starvation is a condition where an individual's body does not receive enough nutrients to maintain proper bodily functions and growth. It can be caused by a lack of access to food, poverty, poor nutrition, or other factors that prevent the intake of sufficient calories and essential nutrients. Starvation can lead to severe health consequences, including weight loss, weakness, fatigue, and even death.

Types of Starvation:

There are several types of starvation, each with different causes and effects. These include:

1. Acute starvation: This occurs when an individual suddenly stops eating or has a limited access to food for a short period of time.
2. Chronic starvation: This occurs when an individual consistently does not consume enough calories and nutrients over a longer period of time, leading to gradual weight loss and other health problems.
3. Malnutrition starvation: This occurs when an individual's diet is deficient in essential nutrients, leading to malnutrition and other health problems.
4. Marasmus: This is a severe form of starvation that occurs in children, characterized by extreme weight loss, weakness, and wasting of muscles and organs.
5. Kwashiorkor: This is a form of malnutrition caused by a diet lacking in protein, leading to edema, diarrhea, and other health problems.

Effects of Starvation on the Body:

Starvation can have severe effects on the body, including:

1. Weight loss: Starvation causes weight loss, which can lead to a decrease in muscle mass and a loss of essential nutrients.
2. Fatigue: Starvation can cause fatigue, weakness, and a lack of energy, making it difficult to perform daily activities.
3. Weakened immune system: Starvation can weaken the immune system, making an individual more susceptible to illnesses and infections.
4. Nutrient deficiencies: Starvation can lead to a deficiency of essential nutrients, including vitamins and minerals, which can cause a range of health problems.
5. Increased risk of disease: Starvation can increase the risk of diseases such as tuberculosis, pellagra, and other infections.
6. Mental health issues: Starvation can lead to mental health issues such as depression, anxiety, and irritability.
7. Reproductive problems: Starvation can cause reproductive problems, including infertility and miscarriage.
8. Hair loss: Starvation can cause hair loss, which can be a sign of malnutrition.
9. Skin problems: Starvation can cause skin problems, such as dryness, irritation, and infections.
10. Increased risk of death: Starvation can lead to increased risk of death, especially in children and the elderly.

It is important to note that these effects can be reversed with proper nutrition and care. If you or someone you know is experiencing starvation, it is essential to seek medical attention immediately.

Here are some possible causes of myoglobinuria:

1. Muscle injury or trauma: This can cause myoglobin to leak into the bloodstream and then into the urine.
2. Muscle disease: Certain muscle diseases, such as muscular dystrophy, can cause myoglobinuria.
3. Kidney damage: Myoglobin can accumulate in the kidneys and cause damage if the kidneys are not functioning properly.
4. Sepsis: Sepsis is a systemic infection that can cause muscle breakdown and myoglobinuria.
5. Burns: Severe burns can cause muscle damage and lead to myoglobinuria.
6. Heart attack: A heart attack can cause muscle damage and myoglobinuria.
7. Rhabdomyolysis: This is a condition where the muscles break down and release myoglobin into the bloodstream. It can be caused by various factors such as medication, infection, or injury.

Symptoms of myoglobinuria may include dark urine, proteinuria (excess protein in the urine), and kidney damage. Treatment depends on the underlying cause and may involve supportive care, medication, or dialysis to remove waste products from the blood.

There are several types of inborn errors of lipid metabolism, each with its own unique set of symptoms and characteristics. Some of the most common include:

* Familial hypercholesterolemia: A condition that causes high levels of low-density lipoprotein (LDL) cholesterol in the blood, which can lead to heart disease and other health problems.
* Fabry disease: A rare genetic disorder that affects the body's ability to break down certain fats, leading to a buildup of toxic substances in the body.
* Gaucher disease: Another rare genetic disorder that affects the body's ability to break down certain lipids, leading to a buildup of toxic substances in the body.
* Lipoid cerebral degeneration: A condition that causes fatty deposits to accumulate in the brain, leading to cognitive decline and other neurological problems.
* Tangier disease: A rare genetic disorder that affects the body's ability to break down certain lipids, leading to a buildup of toxic substances in the body.

Inborn errors of lipid metabolism can be diagnosed through a variety of tests, including blood tests and genetic analysis. Treatment options vary depending on the specific disorder and its severity, but may include dietary changes, medication, and other therapies. With proper treatment and management, many individuals with inborn errors of lipid metabolism can lead active and fulfilling lives.

1. Vitamin B1 (Thiamine): necessary for converting carbohydrates into energy
2. Vitamin B2 (Riboflavin): important for vision health and immune system function
3. Vitamin B3 (Niacin): crucial for energy production and skin health
4. Vitamin B5 (Pantothenic acid): involved in energy production, hormone production, and blood cell formation
5. Vitamin B6: essential for brain function, immune system function, and the synthesis of neurotransmitters
6. Vitamin B7 (Biotin): important for hair, skin, and nail health, as well as energy production
7. Vitamin B9 (Folic acid): crucial for fetal development during pregnancy
8. Vitamin B12: necessary for the production of red blood cells, nerve function, and DNA synthesis.

Vitamin B deficiencies can occur due to several factors, including:

* Poor diet or malnutrition
* Gastrointestinal disorders that impair nutrient absorption (e.g., celiac disease, Crohn's disease)
* Increased demand for vitamins during pregnancy and lactation
* Certain medications (e.g., antacids, proton pump inhibitors) that interfere with nutrient absorption
* Malabsorption due to pancreas or small intestine disorders
* Inherited disorders (e.g., vitamin B12 deficiency due to pernicious anemia)

Symptoms of vitamin B deficiencies can vary depending on the specific vitamin and the severity of the deficiency. Some common symptoms include fatigue, weakness, irritability, depression, skin problems, and impaired cognitive function. Treatment typically involves dietary modifications and supplementation with the appropriate vitamin. In severe cases, hospitalization may be necessary to address any underlying conditions or complications.

The following are some of the most common vitamin B deficiencies:

1. Vitamin B12 deficiency: This is one of the most common vitamin B deficiencies and can cause fatigue, weakness, pale skin, and neurological problems such as numbness or tingling in the hands and feet.
2. Vitamin B6 deficiency: This can cause skin problems, such as acne-like rashes, and neurological symptoms like confusion, convulsions, and weakness in the arms and legs.
3. Folate deficiency: This can cause fatigue, weakness, pale skin, and neurological problems such as memory loss and confusion.
4. Vitamin B2 (riboflavin) deficiency: This can cause cracked lips, skin around the mouth, and tongue, and eyes.
5. Niacin (vitamin B3) deficiency: This can cause pellagra, a condition characterized by diarrhea, dermatitis, and dementia.
6. Vitamin B5 (pantothenic acid) deficiency: This can cause fatigue, weakness, and neurological symptoms like headaches and dizziness.
7. Vitamin B1 (thiamine) deficiency: This can cause beriberi, a condition characterized by weakness, fatigue, and neurological problems such as confusion and memory loss.
8. Biotin deficiency: This is rare but can cause skin problems, such as seborrhea, and neurological symptoms like numbness and tingling in the hands and feet.
9. Vitamin B12 (cobalamin) deficiency: This is common in vegetarians and vegans who do not consume enough animal products, and can cause fatigue, weakness, and neurological problems such as numbness and tingling in the hands and feet.

It's important to note that these deficiencies can have a significant impact on your overall health and well-being, so it's essential to be aware of the signs and symptoms and take steps to ensure you are getting enough of these vitamins in your diet.

Types of Experimental Diabetes Mellitus include:

1. Streptozotocin-induced diabetes: This type of EDM is caused by administration of streptozotocin, a chemical that damages the insulin-producing beta cells in the pancreas, leading to high blood sugar levels.
2. Alloxan-induced diabetes: This type of EDM is caused by administration of alloxan, a chemical that also damages the insulin-producing beta cells in the pancreas.
3. Pancreatectomy-induced diabetes: In this type of EDM, the pancreas is surgically removed or damaged, leading to loss of insulin production and high blood sugar levels.

Experimental Diabetes Mellitus has several applications in research, including:

1. Testing new drugs and therapies for diabetes treatment: EDM allows researchers to evaluate the effectiveness of new treatments on blood sugar control and other physiological processes.
2. Studying the pathophysiology of diabetes: By inducing EDM in animals, researchers can study the progression of diabetes and its effects on various organs and tissues.
3. Investigating the role of genetics in diabetes: Researchers can use EDM to study the effects of genetic mutations on diabetes development and progression.
4. Evaluating the efficacy of new diagnostic techniques: EDM allows researchers to test new methods for diagnosing diabetes and monitoring blood sugar levels.
5. Investigating the complications of diabetes: By inducing EDM in animals, researchers can study the development of complications such as retinopathy, nephropathy, and cardiovascular disease.

In conclusion, Experimental Diabetes Mellitus is a valuable tool for researchers studying diabetes and its complications. The technique allows for precise control over blood sugar levels and has numerous applications in testing new treatments, studying the pathophysiology of diabetes, investigating the role of genetics, evaluating new diagnostic techniques, and investigating complications.

Rhabdomyolysis can be caused by a variety of factors, including:

1. Physical trauma or injury to the muscles
2. Overuse or strain of muscles
3. Poor physical conditioning or training
4. Infections such as viral or bacterial infections that affect the muscles
5. Certain medications or drugs, such as statins and antibiotics
6. Alcohol or drug poisoning
7. Heat stroke or other forms of extreme heat exposure
8. Hypothyroidism (underactive thyroid)
9. Genetic disorders that affect muscle function.

Symptoms of rhabdomyolysis can include:

1. Muscle weakness or paralysis
2. Muscle pain or cramping
3. Confusion or disorientation
4. Dark urine or decreased urine output
5. Fever, nausea, and vomiting
6. Shortness of breath or difficulty breathing
7. Abnormal heart rhythms or cardiac arrest.

If you suspect that someone has rhabdomyolysis, it is important to seek medical attention immediately. Treatment typically involves supportive care, such as fluids and electrolyte replacement, as well as addressing any underlying causes of the condition. In severe cases, hospitalization may be necessary to monitor and treat complications such as kidney failure or cardiac problems.

Symptoms of DKA can include:

* High blood sugar levels (usually above 300 mg/dL)
* High levels of ketones in the blood and urine
* Nausea, vomiting, and abdominal pain
* Fatigue, weakness, and confusion
* Headache and dry mouth
* Flu-like symptoms, such as fever, chills, and muscle aches

If left untreated, DKA can lead to serious complications, such as:

* Dehydration and electrolyte imbalances
* Seizures and coma
* Kidney damage and failure

Treatment of DKA typically involves hospitalization and intravenous fluids to correct dehydration and electrolyte imbalances. Insulin therapy is also started to lower blood sugar levels and promote the breakdown of ketones. In severe cases, medications such as sodium bicarbonate may be given to help neutralize the excess ketones in the blood.

Preventing DKA involves proper management of diabetes, including:

* Taking insulin as prescribed and monitoring blood sugar levels regularly
* Maintaining a healthy diet and exercise program
* Monitoring for signs of infection or illness, which can increase the risk of DKA

Early detection and treatment of DKA are critical to preventing serious complications and improving outcomes for people with diabetes.

Symptoms of Reye Syndrome can include:

* Headache
* Confusion
* Vomiting
* Seizures
* Loss of consciousness
* Yellowing of the skin and eyes (jaundice)
* Fatigue
* Abdominal pain

If you suspect that your child may have Reye Syndrome, it is important to seek medical attention immediately. The condition can be difficult to diagnose, as it can resemble other conditions such as meningitis or encephalitis. A healthcare provider will typically perform a physical examination, take a medical history, and order laboratory tests to confirm the diagnosis.

There is no specific treatment for Reye Syndrome, but the condition is usually managed with supportive care in a hospital setting. Treatment may include:

* Medication to control seizures
* Intravenous fluids and nutrition
* Monitoring of vital signs and liver function
* Antiviral medication in some cases

Reye Syndrome can be fatal if left untreated, so early diagnosis and aggressive management are crucial. The condition is rare, but it is important for parents and healthcare providers to be aware of the signs and symptoms in order to provide prompt and appropriate care.

Causes of Hyperammonemia:

1. Liver disease or failure: The liver is responsible for filtering out ammonia, so if it is not functioning properly, ammonia levels can rise.
2. Urea cycle disorders: These are genetic conditions that affect the body's ability to break down protein and produce urea. As a result, ammonia can build up in the bloodstream.
3. Inborn errors of metabolism: Certain inherited disorders can lead to hyperammonemia by affecting the body's ability to process ammonia.
4. Sepsis: Severe infections can cause inflammation in the body, which can lead to hyperammonemia.
5. Kidney disease or failure: If the kidneys are not functioning properly, they may be unable to remove excess ammonia from the bloodstream, leading to hyperammonemia.

Symptoms of Hyperammonemia:

1. Lethargy and confusion
2. Seizures
3. Coma
4. Vomiting
5. Diarrhea
6. Decreased appetite
7. Weight loss
8. Fatigue
9. Headache
10. Nausea and vomiting

Diagnosis of Hyperammonemia:

1. Blood tests: Measurement of ammonia levels in the blood is the most common method used to diagnose hyperammonemia.
2. Urine tests: Measurement of urea levels in the urine can help determine if the body is able to produce and excrete urea normally.
3. Imaging tests: Imaging tests such as CT or MRI scans may be ordered to look for any underlying liver or kidney damage.
4. Genetic testing: If the cause of hyperammonemia is suspected to be a genetic disorder, genetic testing may be ordered to confirm the diagnosis.

Treatment of Hyperammonemia:

1. Dietary changes: A low-protein diet and avoiding high-aminogram foods can help reduce ammonia production in the body.
2. Medications: Medications such as sodium benzoate, sodium phenylbutyrate, and ribavirin may be used to reduce ammonia production or increase urea production.
3. Dialysis: In severe cases of hyperammonemia, dialysis may be necessary to remove excess ammonia from the blood.
4. Liver transplantation: In cases where the cause of hyperammonemia is liver disease, a liver transplant may be necessary.
5. Nutritional support: Providing adequate nutrition and hydration can help support the body's metabolic processes and prevent complications of hyperammonemia.

Complications of Hyperammonemia:

1. Brain damage: Prolonged elevated ammonia levels in the blood can cause brain damage, leading to cognitive impairment, seizures, and coma.
2. Respiratory failure: Severe hyperammonemia can lead to respiratory failure, which can be life-threatening.
3. Cardiac complications: Hyperammonemia can cause cardiac complications such as arrhythmias and heart failure.
4. Kidney damage: Prolonged elevated ammonia levels in the blood can cause kidney damage and failure.
5. Infections: People with hyperammonemia may be more susceptible to infections due to impaired immune function.

In conclusion, hyperammonemia is a serious condition that can have severe consequences if left untreated. It is essential to identify the underlying cause of hyperammonemia and provide appropriate treatment to prevent complications. Early detection and management of hyperammonemia can improve outcomes and reduce the risk of long-term sequelae.

There are two main types of fatty liver disease:

1. Alcoholic fatty liver disease (AFLD): This type of fatty liver disease is caused by excessive alcohol consumption and is the most common cause of fatty liver disease in the United States.
2. Non-alcoholic fatty liver disease (NAFLD): This type of fatty liver disease is not caused by alcohol consumption and is the most common cause of fatty liver disease worldwide. It is often associated with obesity, diabetes, and high cholesterol.

There are several risk factors for developing fatty liver disease, including:

* Obesity
* Physical inactivity
* High calorie intake
* Alcohol consumption
* Diabetes
* High cholesterol
* High triglycerides
* History of liver disease

Symptoms of fatty liver disease can include:

* Fatigue
* Abdominal discomfort
* Loss of appetite
* Nausea and vomiting
* Abnormal liver function tests

Diagnosis of fatty liver disease is typically made through a combination of physical examination, medical history, and diagnostic tests such as:

* Liver biopsy
* Imaging studies (ultrasound, CT or MRI scans)
* Blood tests (lipid profile, glucose, insulin, and liver function tests)

Treatment of fatty liver disease depends on the underlying cause and severity of the condition. Lifestyle modifications such as weight loss, exercise, and a healthy diet can help improve the condition. In severe cases, medications such as antioxidants, fibric acids, and anti-inflammatory drugs may be prescribed. In some cases, surgery or other procedures may be necessary.

Prevention of fatty liver disease includes:

* Maintaining a healthy weight
* Eating a balanced diet low in sugar and saturated fats
* Engaging in regular physical activity
* Limiting alcohol consumption
* Managing underlying medical conditions such as diabetes and high cholesterol.

Carnitine O-palmitoyltransferase 2, mitochondrial is an enzyme that in humans is encoded by the CPT2 gene. Carnitine ... CPT2 together with carnitine palmitoyltransferase I oxidizes long-chain fatty acids in the mitochondria. Defects in this gene ... Bonnefont JP, Demaugre F, Prip-Buus C, Saudubray JM, Brivet M, Abadi N, Thuillier L (2000). "Carnitine palmitoyltransferase ... Sigauke E, Rakheja D, Kitson K, Bennett MJ (2003). "Carnitine palmitoyltransferase II deficiency: a clinical, biochemical, and ...
... (also called carnitine palmitoyltransferase) is a mitochondrial transferase enzyme (EC 2.3. ... associated with Carnitine palmitoyltransferase I deficiency CPT1B CPT1C CPT2 - associated with carnitine palmitoyltransferase ... in Pfam UMich Orientation of Proteins in Membranes protein/pdbid-2h4t Carnitine+O-Palmitoyltransferase at the US National ... A related transferase is carnitine acyltransferase. Palmitoylcarnitine Palmitoyl CoA There are four different forms of CPT in ...
... (CPT1) also known as carnitine acyltransferase I, CPTI, CAT1, CoA:carnitine acyl transferase ( ... Carnitine palmitoyltransferase I is the first component and rate-limiting step of the carnitine palmitoyltransferase system, ... "Structural model of carnitine palmitoyltransferase I based on the carnitine acetyltransferase crystal". The Biochemical Journal ... The carnitine palmitoyltransferase system is an essential step in the beta-oxidation of long chain fatty acids. This transfer ...
Primary carnitine deficiency Carnitine palmitoyltransferase II deficiency Bennett, Michael J.; Santani, Avni B. (1993-01-01). " ... carnitine palmitoyltransferase I deficiency by producing a defective version of an enzyme called carnitine palmitoyltransferase ... Carnitine palmitoyltransferase I deficiency is a rare metabolic disorder that prevents the body from converting certain fats ... People with this disorder have a faulty enzyme, carnitine palmitoyltransferase I, that prevents these long-chain fatty acids ...
Carnitine O-palmitoyltransferase Carnitine palmitoyltransferase I deficiency Fasciculation Myokymia Primary carnitine ... The Role of Carnitine in Enhancing Physical Performance. National Academies Press (US). "Carnitine palmitoyltransferase II ... Carnitine palmitoyltransferase I (CPT I) is localized to the outer mitochondrial membrane and catalyzes the esterification ... Carnitine palmitoyltransferase II (CPT II) is a peripheral inner mitochondrial membrane protein ubiquitously found as a ...
Carnitine palmitoyltransferase II deficiency (also known as CPT-II deficiency) leads to an excess long chain fatty acids, as ... Weiser, Thomas (1993). "Carnitine Palmitoyltransferase II Deficiency". NIH. Retrieved 22 November 2013. "Galactosemia". ... "Carnitine plamitoyltransferase I deficiency". Genetics Home Reference. National Institute of Health. Retrieved 4 November 2013 ... Treatment generally includes dietary modifications and carnitine supplements. Galactosemia results from an inability to process ...
Anderson RC (Feb 1998). "Carnitine palmitoyltransferase: a viable target for the treatment of NIDDM?". Current Pharmaceutical ... carnitine acetyl coenzyme A transferase, carnitine acetylase, carnitine acetyltransferase, carnitine-acetyl-CoA transferase, ... Like CoA, carnitine forms a hydrogen bond with the ε2 nitrogen on His343. In the case of carnitine, the bond is formed with its ... Carnitine O-acetyltransferase also called carnitine acetyltransferase (CRAT, or CAT) (EC 2.3.1.7) is an enzyme that encoded by ...
... easily solubilized mitochondrial carnitine palmitoyltransferase, and overt mitochondrial carnitine palmitoyltransferase. As of ... Is overt carnitine palmitoyltransferase of liver peroxisomal carnitine octanoyltransferase?". Biochem. J. 249 (1): 231-7. doi: ... "Purification and properties of carnitine octanoyltransferase and carnitine palmitoyltransferase from rat liver". J. Biochem. ... Other names in common use include medium-chain/long-chain carnitine acyltransferase, carnitine medium-chain acyltransferase, ...
"Homo sapiens carnitine palmitoyltransferase 2 (CPT2), mRNA - Nucleotide - NCBI". Ncbi.nlm.nih.gov. 2013-03-25. Retrieved 2013- ... This gene works with carnitine palmitoyltransferase I, and the encoded protein oxidizes long-chain fatty acids in the ... A portion of the 3' UTR of C1orf123 has 100% identity with the mRNA for Homo sapiens carnitine palmityoyltransferase 2 is a ...
In the cytoplasm, malonyl-CoA acts as an inhibitor of the mitochondrial outer membrane enzyme carnitine palmitoyltransferase I ... McGarry, J. Denis; Brown, Nicholas F. (1997-02-15). "The Mitochondrial Carnitine Palmitoyltransferase System - From Concept to ... One study also mentions treatment with L-carnitine in patients with CMAMMA due to ACSF3, but only retrospectively and without ...
... is thought to act by inhibiting mitochondrial carnitine palmitoyltransferase-1. This shifts myocardial metabolism ...
Blepharospasm Carnitine palmitoyltransferase II deficiency Fasciculation Myoclonic jerk (myoclonus) Walton, C.; Kalmar, J. M; ...
... may refer to: Carnitine palmitoyltransferase II, an important metabolic enzyme. Carnitine palmitoyltransferase II ...
"The activities of lipases and carnitine palmitoyltransferase in muscles from vertebrates and invertebrates". The Biochemical ...
"More direct evidence for a malonyl-CoA-carnitine palmitoyltransferase I interaction as a key event in pancreatic beta-cell ... "Glibenclamide inhibits islet carnitine palmitoyltransferase 1 activity, leading to PKC-dependent insulin exocytosis". American ...
"Upstream stimulatory factor represses the induction of carnitine palmitoyltransferase-Ibeta expression by PGC-1". J. Biol. Chem ...
1997). "Structural features of the gene encoding human muscle type carnitine palmitoyltransferase I". FEBS Lett. 409 (3): 401-6 ... "Structural features of the gene encoding human muscle type carnitine palmitoyltransferase I". FEBS Lett. 409 (3): 401-6. doi: ... of equivocal messages containing both regions of choline/ethanolamine kinase and muscle type carnitine palmitoyltransferase I ...
"Upstream stimulatory factor represses the induction of carnitine palmitoyltransferase-Ibeta expression by PGC-1". The Journal ... "Upstream stimulatory factor represses the induction of carnitine palmitoyltransferase-Ibeta expression by PGC-1". The Journal ...
Blepharospasm Carnitine palmitoyltransferase II deficiency Myokymia Fibrillation Blackman G, Cherfi Y, Morrin H, et al. (2019 ...
Malonyl-CoA inhibits the carnitine palmitoyltransferase (CPT) that controls the entry and oxidation of LCFA. The glucose- ...
Carnitine O-palmitoyltransferase Tein, Ingrid (2015-01-01), Darras, Basil T.; Jones, H. Royden; Ryan, Monique M.; De Vivo, ... Once inside the inner mitochondrial membrane, the same Carnitine O-palmitoyltransferase family is then responsible for ... The palmitoyl-CoA is then enzymatically transformed into palmitoylcarnitine via the Carnitine O-palmitoyltransferase family. ... which is bound to the β-hydroxy group of the carnitine. The core carnitine structure, consisting of butanoate with a quaternary ...
Primary carnitine deficiency Carnitine palmitoyltransferase I deficiency Carnitine palmitoyltransferase II deficiency Reference ... Carnitine, a natural substance acquired mostly through the diet, is used by cells to process fats and produce energy. People ... Carnitine-acylcarnitine translocase deficiency is a rare, autosomal recessive metabolic disorder that prevents the body from ... Free long-chain fatty acids or those that are joined with carnitine can affect the electrical properties of cardiac cells ...
"Evidence that the AMP-activated protein kinase stimulates rat liver carnitine palmitoyltransferase I by phosphorylating ...
Carnitine palmitoyltransferase is also upregulated by PPARα, which can affect fatty acid transportation into the mitochondria. ... Malonyl-CoA reduces the activity of carnitine palmitoyltransferase I, an enzyme that brings fatty acids into the mitochondria ...
Acetyl-CoA carboxylase (ACC) converts acetyl-CoA to malonyl-CoA, an inhibitor of carnitine palmitoyltransferase 1 (CPT-1). CPT- ...
... carnitine palmitoyl transferase) converts fatty acyl-CoA to fatty acyl-carnitine. Carnitine biosynthesis inhibitor: Mildronate ... December 2006). "Mildronate, an inhibitor of carnitine biosynthesis, induces an increase in gamma-butyrobetaine contents and ...
... such as pyruvate carboxylase deficiency and carnitine palmitoyltransferase II deficiency. It also appears to increase the ...
2018). "Identifying off-target effects of etomoxir reveals that carnitine palmitoyltransferase I is essential for cancer cell ... Etomoxir, or 2[6(4-chlorophenoxy)hexyl]oxirane-2-carboxylate, is an irreversible inhibitor of carnitine palmitoyltransferase-1 ... This prevents the formation of acyl carnitines, a step that is necessary for the transport of fatty acyl chains from the ...
The carnitine palmitoyltransferase enzymes that regulate the β-oxidation of fatty acids may have a key role in determining some ...
Angel receives a call from the Physician with a complete result and a solid diagnosis of Carnitine Palmitoyltransferase II ...
... syndrome Carnitine palmitoyl transferase deficiency Carnitine palmitoyltransferase I deficiency Carnitine palmitoyltransferase ... II deficiency Carnitine transporter deficiency Carnitine-acylcarnitine translocase deficiency Carnosinase deficiency ...
... carnitine palmitoyltransferase and glycerophosphate acyltransferase compared to peroxisomal β-oxidation and palmitoyl-CoA ...
The co-A is then exchanged with carnitine (via the enzyme carnitine palmitoyltransferase I) to produce a fatty acid-carnitine ... Once inside, carnitine is liberated (catalysed by the enzyme carnitine palmitoyltransferase II) and transported back outside so ... Meldonium has also been shown by NMR to bind to carnitine acetyltransferase. Carnitine acetyltransferase belongs to a family of ... Carnitine is mainly absorbed from the diet, but can be formed through biosynthesis. To produce carnitine, lysine residues are ...
... carnitine palmitoyl transferase, and cholesterol esterification) Propionyl-CoA Butyryl-CoA Myristoyl-CoA Crotonyl-CoA ...
Carnitine <-> Palmitoyl-Carnitine + CoA-SH}}} This transesterification reaction is catalyzed by carnitine palmitoyl transferase ... Carnitine ⟷ Palmitoyl − Carnitine + CoA − SH {\displaystyle {\ce {Palmitoyl-CoA + ... Palmitoyl-Carnitine may translocate across the membrane, and once on matrix side, the reaction proceeds in reverse as CoA-SH is ... Unattached carnitine is then shuttled back to the cytosolic side of mitochondrial membrane. Once inside the mitochondrial ...
... is thought to control fatty acid oxidation by means of the ability of malonyl-CoA to inhibit carnitine palmitoyltransferase I, ...
... as a carnitine is shuttled outside. Acyl-carnitine is converted back to acyl-CoA by carnitine palmitoyltransferase II, located ... Acyl-CoA is transferred to the hydroxyl group of carnitine by carnitine palmitoyltransferase I, located on the cytosolic faces ... The liberated carnitine is shuttled back to the cytosol, as an acyl-carnitine is shuttled into the matrix. If the fatty acyl- ... β-oxidation in the peroxisome requires the use of a peroxisomal carnitine acyltransferase (instead of carnitine acyltransferase ...
... syndrome Familial Mediterranean fever Polyarteritis nodosa Devic's disease Morphea Sarcoidosis Carnitine palmitoyltransferase ...
Transport of acyl-CoA into the mitochondria requires carnitine palmitoyltransferase 1 (CPT1), which converts acyl-CoA into ...
Other causes of myoglobinuria include: McArdle's disease Phosphofructokinase deficiency Carnitine palmitoyltransferase II ...
... cleavage enzyme Protein tyrosine phosphatase Carnitine O-palmitoyltransferase Carnitine O-acetyltransferase Carnitine O- ...
... carnitine palmitoyltransferase I (M-CPT I) and medium-chain acyl-CoA dehydrogenase (MCAD). ATGL deficient mice administered ...
Carnitine Transport Defect Carnitine-acylcarnitine translocase deficiency (CACT) Carnitine Palmitoyl Transferase I & II ( CPT I ... Carnitor - an L-carnitine supplement that has shown to improve the body's metabolism in individuals with low L-carnitine levels ... Longo N, Amat di San Filippo C, Pasquali M (May 2006). "Disorders of carnitine transport and the carnitine cycle". Am J Med ... and VLCADD The fatty acids are transported by carnitine, and defects in this process are associated with several disorders. ...
Phosphoglycerate kinase deficiency Carnitine palmitoyltransferase I deficiency Carnitine palmitoyltransferase II deficiency ...
Carnitine palmitoyltransferase II (CPT II) deficiency is a condition that prevents the body from using certain fats for energy ... Genetic Testing Registry: Carnitine palmitoyltransferase II deficiency *Genetic Testing Registry: Carnitine palmitoyl ... CARNITINE PALMITOYLTRANSFERASE II DEFICIENCY, LETHAL NEONATAL. *CARNITINE PALMITOYLTRANSFERASE II DEFICIENCY, MYOPATHIC, STRESS ... medlineplus.gov/genetics/condition/carnitine-palmitoyltransferase-ii-deficiency/ Carnitine palmitoyltransferase II deficiency. ...
BlueGene E11C0055 Bovine Carnitine Palmitoyltransferase I ELISA Kit is of high quality. We offer this cpt 1 elisa with the ... E11C0055 Bovine Carnitine Palmitoyltransferase I ELISA kit. Bovine Carnitine palmitoyltransferase I ELISA kit is suitable for ... Carnitine palmitoyltransferase I can also be called arnitine acyltransferase I, CPTI, CAT1, CoA, carnitine acyl transferase ( ... Bovine Carnitine Palmitoyltransferase I ELISA kit_copy18 * Metabolism17_copy16_copy20230413_copy20230413 ...
Mouse Carnitine O-palmitoyltransferase 1, liver isoform(CPT1A) ELISA kit. CSB-EL005922MO-24T Cusabio 1 plate of 24 wells. 198 ... Mouse Carnitine O palmitoyltransferase 1, liver isoform (CPT1A/CPT1) ELISA kit. E03C2027-48 BlueGene 1 plate of 48 wells. 624 ... Mouse Carnitine O palmitoyltransferase 1, liver isoform (CPT1A/CPT1) ELISA kit. E03C2027-96 BlueGene 1 plate of 96 wells. 822 ... Rat Carnitine Palmitoyltransferase 1A, Liver (CPT1A) ELISA Kit. SEF368Ra-1x48wellstestplate Cloud-Clone 1x48-wells test plate. ...
The activity and mRNA levels of carnitine palmitoyltransferase I (CPT I) and the rate of beta-oxidation were increased in ... Stearoyl-CoA desaturase-1 deficiency reduces ceramide synthesis by downregulating serine palmitoyltransferase and increasing ... The mRNA levels and activity of serine palmitoyltransferase (SPT), a key enzyme in ceramide synthesis, as well as the ...
Carnitine palmitoyltransferase II (CPT-II) deficiency is an autosomal recessively inherited disorder involving the β-oxidation ... An ignored cause of red urine in children: rhabdomyolysis due to carnitine palmitoyltransferase II (CPT-II) deficiency. ...
Carnitine is a naturally occurring hydrophilic amino acid derivative, produced endogenously in the kidneys and liver and ... Carnitine palmitoyltransferase-1b deficiency aggravates pressure overload-induced cardiac hypertrophy caused by lipotoxicity. ... Primary carnitine deficiency is caused by a deficiency in the plasma membrane carnitine transporter, with urinary carnitine ... Carnitine deficiency is a metabolic state in which carnitine concentrations in plasma and tissues are less than the levels ...
Name: carnitine palmitoyltransferase 1c. Synonyms: CPT I-C, 9630004I06Rik. Type: Gene. Species: Mus musculus (mouse) ...
carnitine palmitoyltransferase 1A. multiple interactions. EXP. valproyl-coenzyme A inhibits the reaction [CPT1A protein results ...
Carnitine is a naturally occurring hydrophilic amino acid derivative, produced endogenously in the kidneys and liver and ... Carnitine palmitoyltransferase-1b deficiency aggravates pressure overload-induced cardiac hypertrophy caused by lipotoxicity. ... Carefully monitor adequate carnitine dose in primary and secondary carnitine deficiencies by evaluating plasma carnitine levels ... Primary carnitine deficiency. Patients with primary carnitine deficiency have excellent prognosis with oral carnitine ...
CPT1A: carnitine palmitoyltransferase 1A (liver). *CREBZF encoding protein CREB/ATF bZIP transcription factor ...
The mitochondrial carnitine palmitoyltransferase system. From concept to molecular analysis.. Eur J Biochem. 1997; 244: 1-14. ... mitochondrial carnitine palmitoyltransferase-I), MetS (metabolic syndrome), NADPH (Nicotinamide adenine dinucleotide phosphate ...
Mitochondrial carnitine palmitoyltransferase 2 is involved in N(epsilon)-(carboxymethyl)-lysine-mediated diabetic nephropathy ...
Patient with SLE, carnitine palmitoyltransferase (CPT) type II deficiency; risk factors for hepatotoxicity (e.g. children ,3 ...
Expression of lipoprotein lipase 1, carnitine palmitoyl transferase 1b, and 3-hydroxyacyl-CoA dehydrogenase was increased in Tg ... carnitine palmitoyl transferase 1b (CPT1b; ENSMUST00000023287), 3-hydroxyacyl-CoA dehydrogenase (HAD; ENSMUST00000029610), ...
Role of membrane curvature on the activation/deactivation of Carnitine Palmitoyltransferase 1A: A coarse grain molecular ...
E71314 Muscle carnitine palmitoyltransferase deficiency E71318 Other disorders of fatty-acid oxidation E7132 Disorders of ...
... with confirmed mutations in the Carnitine palmitoyltransferase II deficiency (CPT2), Very long-chain Acyl-CoA dehydrogenase ...
B) Fatty acid carrier carnitine O-palmitoyltransferase 2 and β-oxidation enzyme enoyl-CoA delta isomerase 2 were significantly ... B) Fatty acid carrier carnitine O-palmitoyltransferase 2 and β-oxidation enzyme enoyl-CoA delta isomerase 2 were significantly ... carnitine acyltransferase I and II as well as the acyl carnitine carrier protein, were elevated, although this reached ... statistical significance only in the case of carnitine acyl transferase II. Furthermore, 17 of 20 proteins involved in ...
A thyroid hormone response unit formed between the promoter and first intron of the carnitine palmitoyltransferase-Ialpha gene ... A thyroid hormone response unit formed between the promoter and first intron of the carnitine palmitoyltransferase-Ialpha gene ... A thyroid hormone response unit formed between the promoter and first intron of the carnitine palmitoyltransferase-Ialpha gene ... mainly owing to increased conjugation of NEFAs with carnitine to facilitate their entrance to mitochondria (20). The resulting ...
Carnitine Acyltransferase I Carnitine O Palmitoyltransferase Carnitine Palmitoyltransferase O-Palmitoyltransferase, Carnitine ... Carnitine Acyltransferase I. Carnitine O Palmitoyltransferase. Carnitine Palmitoyltransferase. Carnitine Palmitoyltransferase I ... Carnitine Palmitoyltransferase II. II, Carnitine Palmitoyltransferase. O-Palmitoyltransferase, Carnitine. Palmitoylcarnitine ... Palmitoyltransferase I, Carnitine. Palmitoyltransferase II, Carnitine. Palmitoyltransferase, Carnitine. Palmitylcarnitine ...
... carnitine palmitoyltransferase 1a, liver; CQ: chloroquine; DGAT1: diacylglycerol O-acyltransferase 1; DGAT2: diacylglycerol O- ...
... carnitine acylcarnitine transferase (CACT), and glucose transporter-4 (GLUT4) in freeze-dried muscle samples from 14 male ... muscle carnitine palmitoyl transferase-1 (mCPT1), fatty acid-binding protein (FABP), ... muscle carnitine palmitoyl transferase-1 (mCPT1), fatty acid-binding protein (FABP), carnitine acylcarnitine transferase (CACT ...
... carnitine palmitoyltransferase-2, very long-chain acylCoA dehydrogenase, trifunctional protein, or long-chain 3-hydroxy acylCoA ...
... including peroxisome proliferator-activated receptor and carnitine palmitoyl transferase 1 in the liver of OVX rats. There was ...
Carnitine palmitoyltransferase I deficiency , muscle From NCATS Genetic and Rare Diseases Information Center ... Carnitine palmitoyltransferase 2 deficiency From NCATS Genetic and Rare Diseases Information Center ...
Carnitine Palmitoyltransferase I Deficiency Carnitine-acylcarnitine Translocase Deficiency Medium-chain Acyl-CoA Dehydrogenase ...
  • Carnitine palmitoyltransferase II (CPT II) deficiency is a condition that prevents the body from using certain fats for energy, particularly during periods without food (fasting). (medlineplus.gov)
  • Carefully review diet compliance in secondary carnitine deficiency, considering avoidance of fasting, intake of fat-restricted, high-carbohydrate diet, and other dietary supplements that may be needed, such as riboflavin or glycine. (medscape.com)
  • Admit patients with carnitine deficiency for medical management of acute metabolic decompensation. (medscape.com)
  • Provide intravenous (IV) carnitine if the patient is known to have carnitine deficiency and a defect affecting the oxidation of long chain fatty acids has been excluded. (medscape.com)
  • Medications include carnitine for primary and secondary carnitine deficiency, as well as other cofactors that may be needed for different conditions associated with secondary carnitine deficiency (eg, riboflavin, coenzyme Q, biotin, hydroxocobalamin, betaine, glycine). (medscape.com)
  • Avoid exercise and dehydration with warm temperatures because attacks of rhabdomyolysis may occur with certain conditions that cause secondary carnitine deficiency. (medscape.com)
  • Patients with primary carnitine deficiency have excellent prognosis with oral carnitine supplementation. (medscape.com)
  • Prognosis of secondary carnitine deficiency depends on the nature of the disorder. (medscape.com)
  • Translocase deficiency and the infantile form of carnitine palmitoyltransferase II (CPT-II) deficiency have very poor prognosis regardless of treatment. (medscape.com)
  • Other metabolic disorders that cause secondary carnitine deficiency, such as organic acidemias, require lifelong diet modification and nutritional supplements. (medscape.com)
  • Family members should receive education once the work-up initiated after newborn screening results suggests primary carnitine deficiency in the newborn or in the mother. (medscape.com)
  • Carnitine deficiency is a metabolic state in which carnitine concentrations in plasma and tissues are less than the levels required for normal function of the organism. (medscape.com)
  • Carnitine deficiency may be primary or secondary. (medscape.com)
  • Primary carnitine deficiency is caused by a deficiency in the plasma membrane carnitine transporter, with urinary carnitine wasting causing systemic carnitine depletion. (medscape.com)
  • [ 1 ] Intracellular carnitine deficiency impairs the entry of long-chain fatty acids into the mitochondrial matrix. (medscape.com)
  • Muscle carnitine deficiency (restricted to muscle) is characterized by depletion of carnitine levels in muscle with normal serum concentrations. (medscape.com)
  • In secondary carnitine deficiency, which is caused by other metabolic disorders (eg, fatty acid oxidation disorders, organic acidemias), carnitine depletion may be secondary to the formation of acylcarnitine adducts and the inhibition of carnitine transport in renal cells by acylcarnitines. (medscape.com)
  • Preterm newborns also may be at risk for developing carnitine deficiency because immature renal tubular function combined with impaired carnitine biosynthesis renders them strictly dependent on exogenous supplies to maintain normal plasma carnitine levels. (medscape.com)
  • Valproic acid may cause an acquired type of secondary carnitine deficiency by directly impairing renal tubular reabsorption of carnitine. (medscape.com)
  • In a Japanese study, primary systemic carnitine deficiency was estimated to occur in 1 per 40,000 births. (medscape.com)
  • In order to abate the mortality and morbidity of undiagnosed primary carnitine deficiency, this condition has been included in the expanded newborn screening program in several states within the United States. (medscape.com)
  • This is a Phase 1b, open-label, multiple-dose study of the safety and tolerability of 2 dose levels of REN001 in subjects with fatty acid oxidation disorders (FAODs) with confirmed mutations in the Carnitine palmitoyltransferase II deficiency (CPT2), Very long-chain Acyl-CoA dehydrogenase deficiency (VLCAD), Long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency (LCHAD) or Trifunctional Protein Deficiency (TFP). (clinicaltrials.gov)
  • If the body is deficient in the enzymes that do this, (fatty acid oxidation disorders), either as a "primary " deficiency associated with genetic abnormalities or "secondary" carnitine deficiency, it can lead to increased amounts of acylcarnitine in the blood which may present with brain dysfunction, a weakened heart, confusion, weakness and other signs and symptoms. (healthmatters.io)
  • Expression of lipoprotein lipase 1, carnitine palmitoyl transferase 1b, and 3-hydroxyacyl-CoA dehydrogenase was increased in Tg-Prkag3 225Q mice, with opposing effects in Prkag3 −/− mice after exercise. (diabetesjournals.org)
  • To examine the potential regulation of genes by PPAR-gamma in human skeletal muscle, we used semiquantitative RT-PCR to determine the expression of PPAR-gamma, lipoprotein lipase (LPL), muscle carnitine palmitoyl transferase-1 (mCPT1), fatty acid-binding protein (FABP), carnitine acylcarnitine transferase (CACT), and glucose transporter-4 (GLUT4) in freeze-dried muscle samples from 14 male subjects. (garvan.org.au)
  • Inclusion of 45 mg/kg of dietary Cu in diets for rabbits improved body mass gain by upregulating mRNA transcription of fatty acid transport protein, fatty acid binding protein, and carnitine palmitoyl transferase 1, indicating that dietary Cu may influence post-absorptive metabolism of lipids. (illinois.edu)
  • 0.10) abundance of fatty acid binding protein 1, peroxisome proliferator-activated receptor alpha, and carnitine palmitoyl transferase 1 B in liver, skeletal muscle, and subcutaneous adipose tissue, respectively. (illinois.edu)
  • Description: A sandwich quantitative ELISA assay kit for detection of Human Carnitine Palmitoyltransferase 1A, Liver (CPT1A) in samples from tissue homogenates, cell lysates or other biological fluids. (worldcarecouncil.org)
  • Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Mouse Carnitine Palmitoyltransferase 1A, Liver (CPT1A) in Tissue homogenates, cell lysates and other biological fluids. (worldcarecouncil.org)
  • Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Mouse Carnitine Palmitoyltransferase 1A, Liver (CPT1A) in samples from Tissue homogenates, cell lysates and other biological fluids with no significant corss-reactivity with analogues from other species. (worldcarecouncil.org)
  • Carefully monitor adequate carnitine dose in primary and secondary carnitine deficiencies by evaluating plasma carnitine levels during follow-up visits. (medscape.com)
  • Bovine Carnitine palmitoyltransferase I ELISA kit is suitable for the detection of samples from Bovine species. (elisakit.cc)
  • Mutations in the CPT2 gene reduce the activity of carnitine palmitoyltransferase 2. (medlineplus.gov)
  • SLC22A5 mutations can affect carnitine transport by impairing maturation of transporters to the plasma membrane. (medscape.com)
  • A group of fats called long-chain fatty acids must be attached to a substance known as carnitine to enter mitochondria. (medlineplus.gov)
  • Once these fatty acids are inside mitochondria, carnitine palmitoyltransferase 2 removes the carnitine and prepares them for fatty acid oxidation. (medlineplus.gov)
  • Without enough of this enzyme, carnitine is not removed from long-chain fatty acids. (medlineplus.gov)
  • Fatty acids and long-chain acylcarnitines (fatty acids still attached to carnitine) may also build up in cells and damage the liver, heart, and muscles. (medlineplus.gov)
  • The activity and mRNA levels of carnitine palmitoyltransferase I (CPT I) and the rate of beta-oxidation were increased in oxidative muscles of SCD1-/- mice. (nih.gov)
  • Carnitine is a naturally occurring hydrophilic amino acid derivative, produced endogenously in the kidneys and liver and derived from meat and dairy products in the diet. (medscape.com)
  • Carnitine is a generic name given to a number of compounds formed primarily from the building blocks of proteins (amino acids) by the kidneys and liver which play an important role in converting fats into energy for cell function (metabolism). (healthmatters.io)
  • This gene provides instructions for making an enzyme called carnitine palmitoyltransferase 2. (medlineplus.gov)
  • The mRNA levels and activity of serine palmitoyltransferase (SPT), a key enzyme in ceramide synthesis, as well as the incorporation of [14C]palmitate into ceramide were decreased by approximately 50% in red muscles of SCD1-/- mice. (nih.gov)
  • For this rare disease, a small double blinded, randomized controlled trial of 32 subjects with LC-FAODs (carnitine palmitoyltransferase-2, very long-chain acylCoA dehydrogenase, trifunctional protein, or long-chain 3-hydroxy acylCoA dehydrogenase deficiencies) were randomly assigned a diet containing 20% of their total daily energy from either triheptanoin or trioctanoin. (medscape.com)
  • Evidence indicates that the causal factor is a defect in the muscle carnitine transporter. (medscape.com)
  • Biologic effects of low carnitine levels may not be clinically significant until they reach less than 10-20% of normal. (medscape.com)
  • Carnitine binds acyl residues and helps in their elimination, decreasing the number of acyl residues conjugated with coenzyme A (CoA) and increasing the ratio between free and acylated CoA. (medscape.com)
  • Improvement of myocardial function and metabolism in diabetic rats by the carnitine palmitoyl transferase inhibitor Etomoxir. (nih.gov)
  • Individuals with hepatic encephalopathy typically present with hypoglycemia, absent or low levels of ketones, and elevated serum concentrations of liver transaminases, ammonia, and total carnitine. (nih.gov)
  • The University of California San Francisco Laboratory reports the normal values of free and total carnitine in adults as 18-69 μmol/L and 20-71 μmol/L, respectively. (medscape.com)
  • Chace et al (2003) examined free and total carnitine levels in newborns. (medscape.com)
  • Free and total carnitine levels within the reference range typically indicate adequate intake, stores, and metabolism. (medscape.com)
  • A group of fats called long-chain fatty acids must be attached to a substance known as carnitine to enter mitochondria. (medlineplus.gov)
  • Once these fatty acids are inside mitochondria, carnitine palmitoyltransferase 2 removes the carnitine and prepares them for fatty acid oxidation. (medlineplus.gov)
  • Without enough of this enzyme, carnitine is not removed from long-chain fatty acids. (medlineplus.gov)
  • Fatty acids and long-chain acylcarnitines (fatty acids still attached to carnitine) may also build up in cells and damage the liver, heart, and muscles. (medlineplus.gov)
  • Carnitine palmitoyltransferase (CPT) deficiencies are common disorders of mitochondrial fatty acid oxidation. (nih.gov)
  • adults need a high-carbohydrate, low-fat diet to provide a constant supply of carbohydrate energy and medium-chain triglycerides to provide approximately one third of total calories (C6-C10 fatty acids do not require the carnitine shuttle for entry into the mitochondrion). (nih.gov)
  • Because of these key functions, carnitine is concentrated in tissues that utilize fatty acids as their primary dietary fuel, such as skeletal and cardiac (heart) muscle. (nih.gov)
  • Carnitine is studied extensively in part because of the important role it plays in fatty acid oxidation and energy production, and because it is a well-tolerated and generally safe therapeutic agent. (nih.gov)
  • Understanding the molecular basis for the disease caused by mutations of the carnitine palmitoyltransferase (CPT)I and CPTII enzymes involved in the transport of fatty acids by L-carnitine into and out of the mitochondria. (nih.gov)
  • Carnitine is an important, small water-soluble molecule that binds to long-chain fatty acids and facilitates their transport across the inner mitochondrial membrane and into the mitochondrial matrix to undergo fatty acid oxidation (metabolism). (medscape.com)
  • Other benefits attributed to carnitine result from the management of secondary carnitine deficiencies. (nih.gov)
  • While there is agreement on carnitine's role as a prescription product for the treatment of primary carnitine deficiencies, its benefits as a dietary supplement in individuals who are carnitine sufficient is debated. (nih.gov)
  • People with this disorder typically also have an enlarged liver (hepatomegaly), muscle weakness, nervous system damage, and elevated levels of carnitine in the blood. (nih.gov)
  • gene provides instructions for making an enzyme called carnitine palmitoyltransferase 1A, which is found in the liver. (nih.gov)
  • In general, healthy adults do not require dietary carnitine as carnitine stores are replenished through endogenous synthesis from lysine and methionine in the liver and kidneys. (nih.gov)
  • The disorder is fatal without treatment, but supplementation with oral carnitine results in elevated carnitine levels and prevents progression of the disease. (medscape.com)
  • gene provides instructions for making a protein called carnitine -acylcarnitine translocase (CACT). (nih.gov)
  • It is proven treatment in children who have recessive defects in the carnitine transporter system and in individuals treated with pivalate containing antibiotics. (nih.gov)
  • they are attached to a substance known as carnitine. (nih.gov)
  • membrane, where it transports a substance known as carnitine into the cell. (nih.gov)
  • Carnitine is a quaternary, water-soluble ammonia compound biosynthesized from lysine and arginine. (medscape.com)
  • disorders of metabolism with elevated butyryl- and isobutyryl- carnitine detected by tandem mass spectrometry newborn screening. (nih.gov)
  • The first day addressed the fundamentals of carnitine physiology and pharmacology, issues related to its replacement in health and disease, its effects on skeletal and cardiac or smooth muscle, and its role in fat metabolism and obesity. (nih.gov)
  • Carnitine is derived from both the diet (meats and milk) and synthesis (very slowly) from trimethyllysine. (medscape.com)
  • Carnitine research needs emerging from this conference can be grouped under three broad headings, i.e. basic research, as a drug in the treatment and management of disease conditions, and as a dietary supplement. (nih.gov)
  • Carnitine is the generic term for a number of compounds that include L-carnitine, L-acetylcarnitine, acetyl-L-carnitine, and L-propionyl carnitine. (nih.gov)
  • Carnitine is termed a conditionally essential nutrient, as under certain conditions its requirements may exceed the individual's capacity to synthesize it. (nih.gov)
  • Carnitine, a natural substance acquired mostly through the diet, is required by cells to process fats and produce energy. (nih.gov)