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)

Carnitine palmitoyltransferase II deficiency (CPT-II) is an autosomal recessively inherited genetic metabolic disorder characterized by an enzymatic defect that prevents long-chain fatty acids from being transported into the mitochondria for utilization as an energy source. The adult myopathic form of this disease was first characterized in 1973 by DiMauro and DiMauro. It is the most common inherited disorder of lipid metabolism affecting the skeletal muscle of adults. CPT II deficiency is also the most frequent cause of hereditary myoglobinuria. Symptoms of this disease are commonly provoked by prolonged exercise or periods without food. There are three main types of carnitine palmitoyltransferase II deficiency classified on the basis of tissue-specific symptomotology and age of onset: Mild to severe adult myopathic form Severe infantile multisystemic form Lethal neonatal form It should be noted that among the few people diagnosed with CPT2, some have unknown and/or novel mutations that place ...
Carnitine palmitoyltransferase II deficiency is a condition that prevents the body from converting certain fats called long-chain fatty acids into energy, particularly during periods without food (fasting). Carnitine, a natural substance acquired mostly through the diet, is required by cells to process fats and produce energy. People with this disorder have a faulty enzyme that disrupts carnitines role in processing long-chain fatty acids.. The three main types of carnitine palmitoyltransferase II deficiency are: a lethal neonatal form; a severe infantile form that affects the liver, heart, and muscles (hepatocardiomuscular form); and a less severe form that affects only the muscles (myopathic form). Infants with the lethal neonatal form of this disorder usually experience respiratory failure, liver failure, seizures, and an irregular heart beat (arrythmia) leading to cardiac arrest. In many cases, the brain and kidneys are also abnormal. Usually, affected infants do not survive their first ...
CPT2Z : Confirmation of diagnosis of carnitine palmitoyltransferase II deficiency   Carrier screening in cases where there is a family history of carnitine palmitoyltransferase II deficiency, but disease-causing mutations have not been identified in an affected individual
Build: Wed Jun 21 18:33:50 EDT 2017 (commit: 4a3b2dc). National Center for Advancing Translational Sciences (NCATS), 6701 Democracy Boulevard, Bethesda MD 20892-4874 • 301-435-0888. ...
TY - JOUR. T1 - Purification, characterization and partial amino acid sequences of carnitine palmitoyl-transferase from human liver. AU - Finocchiaro, G.. AU - Colombo, I.. AU - DiDonato, S.. PY - 1990/11/12. Y1 - 1990/11/12. N2 - Carnitine palmitoyl-transferase has been extracted with 0.5% Tween-20 from human liver homogenatc and purified to homogeneity. The purified enzyme has a native Mr of 274 kDa. The subunit Mr is of 66 kDa, as shown by SDS-PAGE and immunoblots obtained with antibodies raised against human CPT. Purified CPT shows high affinity for palmitoyl-CoA and palmitoyl-carnitine and is not inhibited by malonyl-CoA, Seven tryptic peptides and the N-terminal of purified human CPT have been sequenced, and found homologous to rat CPT sequence. Both antibodies and peptide sequences are important tools for the investigation of the molecular basis of CPT deficiency in man.. AB - Carnitine palmitoyl-transferase has been extracted with 0.5% Tween-20 from human liver homogenatc and purified to ...
in Clinical genetics (2015). Carnitine palmitoyltransferase II (CPT2) deficiency is a rare inborn error of mitochondrial fatty acid metabolism associated with various phenotypes. Whereas most patients present with postnatal signs of ... [more ▼]. Carnitine palmitoyltransferase II (CPT2) deficiency is a rare inborn error of mitochondrial fatty acid metabolism associated with various phenotypes. Whereas most patients present with postnatal signs of energetic failure affecting muscle and liver, a small subset of patients presents antenatal malformations including brain dysgenesis and neuronal migration defects. Here, we report recurrence of severe cerebral dysgenesis with Dandy-Walker malformation in three successive pregnancies and review previously reported antenatal cases. Interestingly, we also report that acylcarnitines profile, tested retrospectively on the amniotic fluid of last pregnancy, was not sensitive enough to allow reliable prenatal diagnosis of CPT2 deficiency. Finally, because ...
Forensic testing uses DNA sequences to identify an individual for legal purposes. Unlike the tests described above, forensic testing is not used to detect gene mutations associated with disease. This type of testing can identify crime or catastrophe victims, rule out or implicate a crime suspect, or establish biological relationships between people (for example, paternity). 42 Carnitine Palmitoyltransferase I Deficiency How Is Genetic Testing Done? Once a person decides to proceed with genetic testing, a medical geneticist, primary care doctor, specialist, or nurse practitioner can order the test. Unlike the tests described above, forensic testing is not used to detect gene mutations associated with disease. This type of testing can identify crime or catastrophe victims, rule out or implicate a crime suspect, or establish biological relationships between people (for example, paternity). 42 Carnitine Palmitoyltransferase I Deficiency How Is Genetic Testing Done? Once a person decides to proceed ...
Add Carnitor later, that should make him feel better.. Chris dad turns to House, glancing over the cane. Thank you.. House nodded and left as Cameron walked up to Chris and his parents and started explaining.. Chris, you have a F.O.D. A fatty oxidation disorder. There are several kinds and yours is called CPT2.. Normally your body uses glucose as an energy source, and when glucose is not available it uses fat. Therefore it breaks down the long chains of fatty acids into smaller ones with an enzyme. But if that enzyme is missing or not functioning correctly you cant break the fatty acids down and instead the body stores them. Often in places where it doesnt belong - for example in the liver, the kidneys or the heart.. In your case the carnitine palmitoyltransferase II precursor, called CPT2 for short, is not doing its job. So when all the glucose is used up there is nothing else the body can use to get its energy from. That is why we just put you on a glucose drip.. You will get Carnitor ...
It has been suggested that some cancer cells rely upon fatty acid oxidation (FAO) for energy. Here we show that when FAO was reduced approximately 90% by pharmacological inhibition of carnitine palmitoyltransferase I (CPT1) with low concentrations of etomoxir, the proliferation rate of various cancer cells was unaffected. Efforts to pharmacologically inhibit FAO more than 90% revealed that high concentrations of etomoxir (200 μM) have an off-target effect of inhibiting complex I of the electron transport chain. Surprisingly, however, when FAO was reduced further by genetic knockdown of CPT1, the proliferation rate of these same cells decreased nearly 2-fold and could not be restored by acetate or octanoic acid supplementation. Moreover, CPT1 knockdowns had altered mitochondrial morphology and impaired mitochondrial coupling, whereas cells in which CPT1 had been approximately 90% inhibited by etomoxir did not. Lipidomic profiling of mitochondria isolated from CPT1 knockdowns showed depleted ...
Prevalence and incidence statistics for Carnitine palmitoyl transferase II deficiency, lethal neonatal form covering estimated populations and diagnosis rates.
My one year-old daughter was admitted in the hospital because of breathing problems. Her ph level was 6.7 and she was unconscious for eight days. During those days there were many problems. Her doctor said that she had SCOT deficiency OR carnitine palmitoyl transferase 1 deficiency. Now she is normal. Will this happen again ...
TY - JOUR. T1 - Interaction of malonyl-CoA and related compounds with mitochondria from different rat tissues. Relationship between ligand binding and inhibition of carnitine palmitoyltransferase I.. AU - Mills, S. E.. AU - Foster, D. W.. AU - McGarry, J. D.. PY - 1983/7/15. Y1 - 1983/7/15. N2 - The sensitivity of carnitine palmitoyltransferase I (CPT I; EC 2.3.1.21) to inhibition by malonyl-CoA and related compounds was examined in isolated mitochondria from liver, heart and skeletal muscle of the rat. In all three tissues the same order of inhibitory potency emerged: malonyl-CoA much greater than succinyl-CoA greater than methylmalonyl-CoA much greater than propionyl-CoA greater than acetyl-CoA. For any given agent, suppression of CPT I activity was much greater in skeletal muscle than in liver, with the heart enzyme having intermediate sensitivity. With skeletal-muscle mitochondria a high-affinity binding site for [14C]malonyl-CoA was readily demonstrable (Kd approx. 25 nM). The ability of ...
Carnitine is an essential factor in long-chain fatty acid oxidation. Carnitine acts as a carrier of fatty acyl groups from the cytoplasm to the mitochondrion. Long-chain acyl-CoA derivatives do not penetrate the mitochondrial inner membrane. Carnitine palmitoyltransferase A (CPT-A), located on the e …
Inhibition of the overt mitochondrial carnitine palmitoyltransferase by malonyl-CoA is important in the regulation of fatty acid oxidation. In the past, the contribution of peroxisomal carnitine acyltransferase activity to the generation of medium- and long-chain acylcarnitines in the cytoplasm has been ignored. On the basis of marker enzyme levels, we now estimate that peroxisomal palmitoyltransferase activity constitutes about 20% of the peroxisomal plus overt-mitochondrial pool in fed rat liver. When assayed in situ, both the palmitoyltransferase and decanoyltransferase activities of gradient-purified peroxisomes are sensitive to malonyl-CoA, with up to 90% inhibition reached at less than 10 microM-malonyl-CoA. Very similar results were obtained with intact gradient-purified mitochondria from the same livers. In addition, the acyl-CoA substrate chain-length specificity was identical in both the peroxisomes and the mitochondria, with a decanoyltransferase/palmitoyltransferase ratio of 2. Thus ...
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Etomoxir is an irreversible inhibitor of the mitochondrial transport of long-chain fatty acids via blockage of carnitine palmitoyltransferase-I (CPT-1) leading to inhibition of the mitochondrial fatty acid oxidation (FAO). Owing to its inhibitory effect, etomoxir is widely used (40-400 μM) in commercial kits [1,2], however, several studies shed light on the unspecific effect of etomoxir on the mitochondria [3,4]. To assess the specificity of etomoxir on FAO in comparison to its inhibitory effect on mitochondrial respiration involving other mitochondrial pathways, we tested different concentrations of etomoxir (1-200 µM) on permeabilized Huh7 human hepatocellular carcinoma cells and isolated liver mitochondria from mouse, using high-resolution respirometry. Different sources of fatty acids (palmitoylcarnitine, palmityl-CoA + carnitine) were used to test the specific effect of etomoxir towards FAO (F-pathway). We have also investigated the off-target effect of etomoxir on mitochondrial ...
Fatty acid and ketone body metabolism differ considerably between monogastric and ruminant species. The regulation of the key enzymes involved may differ accordingly. Carnitine palmitoyltransferase 1 (CPT 1) is the key locus for the control of long-chain fatty acid β-oxidation and liver ketogenesis. Previously we showed that CPT 1 kinetics in sheep and rat liver mitochondria differ. We cloned cDNAs for both isoforms [liver- (L-) and muscle- (M-)] of ovine CPT 1 in order to elucidate the structural features of these proteins and their genes ( CPT1A and CPT1B ). Their deduced amino acid sequences show a high degree of conservation compared with orthologues from other mammalian species, with the notable exception of the N-terminus of ovine M-CPT 1. These differences were also present in bovine M-CPT 1, whose N-terminal sequence we determined. In addition, the 5′-end of the sheep CPT1B cDNA suggested a different promoter architecture when compared with previously characterized CPT1B genes. ...
The mechanism by which Trojan Horse works is multi-faceted. The primary part of the system requires the combination of hydroxycitrate (HCA) and L-carnitine. These two molecules synergistically do the job with each other to boost the activity with the enzyme carnitine palmitoyltransferase I (CPT), the rate restricting enzymatic phase for transporting fatty acids into the mitochondria for beta oxidation (fat burning). HCA inhibits the production of malonyl CoA, an allosteric inhibitor of CPT. Carnitine is an essential cofactor for CPT action and boosts ketogenesis. All through ketogenesis, extra ADP is produced, which results in an elevated electrochemical proton gradient for ATP synthase. ATP synthase is liable for the creation of ATP and needs a higher electrochemical gradient to operate sufficiently. Pyruvate is the end product or service of glycolysis, the breakdown of carbohydrates for Power. Pyruvate converts into acetyl CoA that enters the Krebs cycle, which generates the electron carriers ...
Kit contents: 1. MICROTITER PLATE * 1 2. ENZYME CONJUGATE*1 vial 3. STANDARD A*1 vial 4. STANDARD B*1 vial 5. STANDARD C*1 vial 6. STANDARD D*1 vial 7. STANDARD E*1 vial 8. STANDARD F*1 vial 9. SUBSTRATE A*1 vial 10. SUBSTRATE B*1 vial 11. STOP ...
Complete information for CPT1B gene (Protein Coding), Carnitine Palmitoyltransferase 1B, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Complete information for CPT1B gene (Protein Coding), Carnitine Palmitoyltransferase 1B, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
CLA increases the activity of the enzyme carnitine palmitoyltransferase (CPT). CPT is present in the skeletal muscles and is responsible for the transport of fatty acids into the mitochondria. Energy production in the body takes place in the mitochondria. Fat can be used as fuel for energy production. With an increased activity of CPT in the skeletal muscle, CLA increases the transport of fat into the mitochondria. All these steps elevate the beta-oxidation, thus helping the body to burn more fat. Physical activity stimulates the fat transport from the bloodstream or the fat cell, to be burned in the muscle cell. With no extra fat coming in to store in the fat cells and increased burning of stored fat, the size of these cells is reduced. Using CLA in combination with a sensible diet and moderate exercise can lead to an improved body shape ...
CPT2 antibody [N1C1] (carnitine palmitoyltransferase 2) for WB. Anti-CPT2 pAb (GTX104115) is tested in Human samples. 100% Ab-Assurance.
CPT2 (aa406-418) antibody, Internal (carnitine palmitoyltransferase 2) for WB. Anti-CPT2 (aa406-418) pAb (GTX88238) is tested in Human samples. 100% Ab-Assurance.
Principal Investigator:OHTANI Yoshinobu, Project Period (FY):1995 - 1997, Research Category:Grant-in-Aid for Scientific Research (C), Section:一般, Research Field:Pediatrics
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The Indians released sinkerballer Derek Lowe on Friday after he cleared waivers. Lowe, who was acquired in an offseason trade with the Braves, was designated for assignment on Aug. 2. He went 8-10 with a 5.52 ERA in 21 starts this year, but the veteran was 2-9 with an 8.28 ERA in his final 13 outings. Right-hander Roberto Hernandez was slated to start for Triple-A Columbus on Friday night in what will likely be his last Minor League rehab outing. Barring any setbacks, the team expects to activate Hernandez from the restricted list and add him to the rotation next week, said Acta. Left-hander Rafael Perez is scheduled to resume his Minor League rehab assignment on Saturday with Triple-A Columbus. Perez (on the 60-day disabled list due to a left lat strain) was recently shut down for a brief period after complaining of shoulder soreness. Setup man Vinnie Pestanos clean eighth inning on Thursday upped his scoreless-innings streak to 21 frames. That marks the longest run
The authors studied a 53 year old woman and her 22 year old son with episodes of paroxysmal muscle cramps and dark urines lasting several hours related to high fat diet and strenuous physical exercise beginning on both at age 14 years. The father, paternal uncle, paternal grandfather and another son of the mother also had paroxysmal muscle cramps. The two studied cases showed normal findings for physical evaluation, blood lactate after ischemic exercise, and muscle histology (light and electron microscopy). The serum creatine kinase was elevated in the son and normal in the mother. However, 72 hour fasting significantly raised the serum creatine kinase level in both cases. Plasma concentration of ketone bodies and acid soluble acyl-carnitine increased normally with prolonged fasting. The biochemical evaluation of the muscle tissue revealed intact anaerobic glycolysis and normal glycogen content but combined partial deficiency of muscle carnitine palmitoyltransferase and carnitine in both ...
Abstract In the present study, the effect of 5-aminoimidazole-4-carboxamide ribonucleoside (AICAR) on long-chain fatty acid oxidation by hepatocytes isolated from suckled neonatal pig liver (a low ketogenic and lipogenic tissue) was tested. Incubation of hepatocytes with AICAR (0.5 mM) in the presence of 1 mM of carnitine and 10 mM of glucose for 1 hour at 37and#176;C had no significant effect on total [1-14C]-palmitate (0.5 mM) oxidation (14CO2 and 14C-Acid soluble products (ASP)). Consistent with the fatty acid oxidation, carnitine palmitoyltransferase I activity and inhibition of its activity by malonyl-CoA (10 and#956;M) assayed in cell homogenate also remained constant. However, addition of AICAR to the hepatocytes decreased 14CO2 production by 18% compared to control (p andlt; 0.06). The reduction of labeled carboxylic carbon accumulated in CO2 caused a significant difference in distribution of oxidative products between 14CO2 and 14C-ASP (p andlt; 0.03) compared with the control. It was ...
Dodecanedioic acid is a dicarboxylic acid which is water soluble and involves in a metabolic pathway intermediate to those of lipids and carbohydrates. (PMID 9591306). Dodecanedioid acid is an indicator of hepatic carnitine palmitoyltransferase I (CPT IA) deficiency. CPT IA deficiency is characterized by hypoketotic dicarboxylic aciduria with high urinary levels of dodecanedioic acid. This C12 dicarboxylic aciduria suggests that carnitine palmitoyltransferase I may play a role in the uptake of long-chain dicarboxylic acids by mitochondria after their initial shortening by beta-oxidation in peroxisomes. (PMID: 16146704 ...
Amri EZ, Bertrand B, Ailhaud G and Grimaldi P (1991). Regulation of adipose cell differentiation. I. Fatty acids are inducers of the aP2 gene expression. J. Lipid Res. 32: 1449-1456. PMid:1753215 Arber S, Barbayannis FA, Hanser H, Schneider C, et al. (1998). Regulation of actin dynamics through phosphorylation of cofilin by LIM-kinase. Nature 393: 805-809. doi:10.1038/31729 PMid:9655397 Ball SG, Shuttleworth CA and Kielty CM (2007). Platelet-derived growth factor receptor-alpha is a key determinant of smooth muscle alpha-actin filaments in bone marrow-derived mesenchymal stem cells. Int. J. Biochem. Cell Biol. 39: 379-391. doi:10.1016/j.biocel.2006.09.005 Britton CH, Mackey DW, Esser V, Foster DW, et al. (1997). Fine chromosome mapping of the genes for human liver and muscle carnitine palmitoyltransferase I (CPT1A and CPT1B). Genomics 40: 209-211. doi:10.1006/geno.1996.4539 PMid:9070950 Brouns F and van der Vusse GJ (1998). Utilization of lipids during exercise in human subjects: metabolic and ...
Looking for online definition of palmitoyltransferase ZDHHC2 in the Medical Dictionary? palmitoyltransferase ZDHHC2 explanation free. What is palmitoyltransferase ZDHHC2? Meaning of palmitoyltransferase ZDHHC2 medical term. What does palmitoyltransferase ZDHHC2 mean?
Peroxisome proliferator-activated receptor (PPAR) alpha is a member of the nuclear receptor superfamily of ligand-activated transcription factors. PPARalpha is activated by peroxisome proliferators and fatty acids and has been shown to be involved in the transcriptional regulation of genes involved in fatty acid metabolism. In rodents, the PPARalpha-mediated change in such genes results in peroxisome proliferation and can lead to the induction of hepatocarcinogenesis. Using the mRNA differential display technique and Northern blot analysis, we have shown that chronic exposure of the prostate cancer epithelial cell line LNCaP to the synthetic androgen mibolerone results in the down-regulation of PPARalpha mRNA. Levels of PPARalpha mRNA are reduced to approximately 40% of control levels in LNCaP cells exposed to 10 nM mibolerone for 96 h. PPARalpha-responsive reporter plasmids derived from human ApoA-II and muscle carnitine palmitoyl-transferase I genes were stimulated by the PPARalpha-activating ligand
Circulation. 2012 Oct 2;126(14):1705-16. doi: 10.1161/CIRCULATIONAHA.111.075978. Epub 2012 Aug 29. Research Support, N.I.H., Extramural
In order to examine the role of fructose 2,6-bisphosphate (Fru-2,6-P2) in non-esterified-fatty-acid-stimulated gluconeogenesis, Fru-2,6-P2 levels were measured in cultured rat hepatocytes under conditions mimicking the fasted state. After addition of either 1.5 mM-palmitate or 10 nM-glucagon, [U-14C]lactate incorporation into glucose increased 2-fold, but only glucagon suppressed Fru-2,6-P2. Prevention of palmitate oxidation with a carnitine palmitoyltransferase-I inhibitor (2-bromopalmitate) diminished glucose production and Fru-2,6-P2 levels. Addition of exogenous glucose to the media increased Fru-2,6-P2 in a dose-related manner, which was further augmented by addition of palmitate. When Fru-2,6-P2 levels were examined in cells cultured under conditions mimicking the fed state (significantly higher basal Fru-2,6-P2 levels and lower glucose production), palmitate oxidation was associated with a significant fall in Fru-2,6-P2. In conclusion, the present studies have demonstrated a dissociation ...
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These reference sequences exist independently of genome builds. Explain. These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above. ...
What Is It: Carnitine will help improve overall body composition by leaning you out through fat loss and preserving muscle mass and prevents muscle catabolism
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To extract energy from stored lipids, fatty acids must first be liberated from triglyceride before their β-oxidation in mitochondria in a coordinated and stepwise manner. To determine the independent and interdependent roles of hepatic triglyceride hydrolysis and fatty acid oxidation, mice were generated with a liver-specific defect in triglyceride hydrolysis (AtglL-/-), fatty acid oxidation (Cpt2L-/-), or both (double knockout). The loss of either gene resulted in the compensatory increase in the other, demonstrating their coordination. The loss of individual components of fatty acid catabolism (carnitine palmitoyl transferase 2 [Cpt2], adipose triglyceride lipase [Atgl], and Pparα) resulted in largely independent effects on hepatocyte morphology, intermediary metabolism, and gene expression in response to fasting. However, high-fat feeding revealed the interdependent role of Atgl and Cpt2, as the loss of only one of the genes resulted in steatosis (fatty liver) but the loss of both ...
Introduction In the treatment of patients with diabetes, one objective is an improvement of cardiac metabolism to alleviate the left ventricular (LV) function. For this study, we compared the effects of acetyl-l-carnitine (one of the carnitine derivatives) and of oxfenicine (a carnitine palmitoyltransferase-1 inhibitor) on cardiac pumping mechanics in streptozotocin-induced diabetes in male Wistar rats, with a particular focus on the pressure-flow-volume relationship. Methods Diabetes was induced by a single tail vein injection of 55 mg kg−1 streptozotocin. The diabetic animals were treated on a daily basis with either acetyl-L-carnitine (1 g L−1 in drinking water) or oxfenicine (150 mg kg−1 by oral gavage) for 8 wk. They were also compared with untreated age-matched diabetic controls. LV pressure and ascending aortic flow signals were recorded to calculate the maximal systolic elastance (E max) and the theoretical maximum flow (Q max).
Accumulating evidence suggests that leptin regulates energy homeostasis through direct actions on peripheral lipid and glucose metabolism.132 Fatty acid (FA) oxidation produces the major source of ATP to sustain contractile function of the heart. AMP-activated protein kinase (AMPK) has a key role as a fuel gauge in the heart and regulates cardiac FA oxidation by phosphorylation and inhibition of acetyl-coenzyme A (CoA) carboxylase, which then lowers malonyl-CoA levels and stimulates carnitine palmitoyltransferase-1-induced FA oxidation.133 AMPK activation is also known to reduce FA incorporation into triacylglycerol.134. Examination of leptin effects on cardiac FA oxidation confirmed that leptin infusion increases FA oxidation and triacylglycerol lipolysis in isolated working rat hearts, although this effect was independent of changes in the AMPK/acetyl-CoA carboxylase/malonyl/CoA axis. Neither did leptin affect glucose oxidation rates.135 Myocardial oxygen consumption was increased, possibly ...
Yoon, M.J., Lee, G.Y., Chung, J.J., Ahn, Y.H., Hong, S.H. and Kim, J.B. (2006) Adiponectin Increases Fatty Acid Oxidation in Skeletal Muscle Cells by Sequential Activation of AMP-Activated Protein Kinase, p38 Mitogen-Activated Protein Kinase, and Peroxisome Proliferator-Activated Receptor Alpha. Diabetes, 55, 2562-2570.
The protein encoded by this gene, a member of the carnitine/choline acetyltransferase family, is the rate-controlling enzyme of the long-chain fatty acid beta-oxidation pathway in muscle mitochondria. This enzyme is required for the net transport of long-chain fatty acyl-CoAs from the cytoplasm into the mitochondria. Multiple transcript variants encoding different isoforms have been found for this gene, and read-through transcripts are expressed from the upstream locus that include exons from this gene. [provided by RefSeq, Jun 2009 ...
Despite recent advances, many cancers remain refractory to available immunotherapeutic strategies. Emerging evidence indicates that the tolerization of local dendritic cells (DCs) within the tumor microenvironment promotes immune evasion. Here, we have described a mechanism by which melanomas establish a site of immune privilege via a paracrine Wnt5a-β-catenin-peroxisome proliferator-activated receptor-γ (PPAR-γ) signaling pathway that drives fatty acid oxidation (FAO) in DCs by upregulating the expression of the carnitine palmitoyltransferase-1A (CPT1A) fatty acid transporter. This FAO shift increased the protoporphyrin IX prosthetic group of indoleamine 2,3-dioxgenase-1 (IDO) while suppressing interleukin(IL)-6 and IL-12 cytokine expression, culminating in enhanced IDO activity and the generation of regulatory T cells. We demonstrated that blockade of this pathway augmented anti-melanoma immunity, enhanced the activity of anti-PD-1 antibody immunotherapy, and suppressed disease progression ...
The following evidence is presented in favour of the old hypothesis that F− inhibition of fatty acid oxidation in intact, coupled rat-liver mitochondria is due to an accumulation of pyrophosphate in the mitochondrial matrix: 1. 1.Addition of fatty acid to mitochondria oxidizing malate in the presence of F− initially causes ... read more an increased rate of O2 uptake, followed by a gradual decrease, indicating the accumulation of an inhibitor as a result of fatty acid oxidation. 2. 2. This inhibition is only found when the fatty acid substrate is activated in the mitochondrial matrix. 3. 3. The matrix acyl-CoA synthetase (acid:CoA ligase (AMP), EC 6.2.1.3) is strongly inhibited by pyrophosphate. 4. 4. Mitochondrial pyrophosphatase (pyrophosphate phosphohydrolase, EC 3.6.1.1) is inhibited by F− and is localized mainly in the matrix. 5. 5. The mitochondrial inner membrane is impermeable to pyrophosphate. 6. 6. Pyrophosphate accumulates in mitochondria oxidizing fatty acid in the presence of ...
Without carnitine, fats cannot be burned for energy. This explains the fascination with carnitine supplementation as a fat burner. In two separate studies, supplementation of carnitine (3 grams per day) for 10 days resulted in significantly higher rates of fat oxidation (1,2). This work was recently validated by researchers in the United Kingdom (3). They studied healthy endurance-trained men who supplemented with 80 grams of carbohydrate 2 times per day for 24 weeks. One group also received 2 grams l-carnitine l-tartrate (LCLT) in their carbohydrate beverage. Resting muscle carnitine was unchanged after 12 weeks but increased by 21% after 24 weeks in the carnitine group. When the carnitine group exercised at a low intensity after 24 weeks of supplementation, they showed the higher muscle carnitine was linked to significant muscle glycogen sparing (55% less) compared to controls. Work output was 35% greater than controls. Several lines of evidence support a role of carnitine in other processes ...
April 11, 2013 A study published in Nature Medicine claims that carnitine, a compound abundant in red meat, sold as a dietary supplement, and present in some energy drinks, may increase the risk of heart disease. Carnitine typically helps the body transport fatty acids into cells to be used as energy. But researchers at the Cleveland Clinic found that in both humans and mice, certain bacteria in the digestive tract convert carnitine to another metabolite, called TMAO, which promotes atherosclerosis, or a thickening of the arteries. The researchers tested the carnitine and TMAO levels of omnivores, vegans, and vegetarians, and examined records of 2,595 patients undergoing cardiac evaluations. In patients with high TMAO levels, the more carnitine in their blood, the more likely they were to develop cardiovascular disease, heart attacks, stroke, and death. The researchers speculated that carnitine could be compounding the danger. Cholesterol is still needed to clog the arteries, but TMAO changes ...
Oxytocin (OT) is a hypothalamic neuropeptide synthesized and secreted by OT neurons. In addition to its conventional role in reproductive physiology, central OT also regulates various social behaviors, such as care, trust, and emotions. Central and subcutaneous OT infusions stimulate lipid metabolism in mice and rats when fed standard or high fat diets. Mice lacking the OT receptor (OTR) or OT peptide develop late-onset obesity with greater fat pad weights, larger adipocyte size and elevated plasma levels of leptin. To study the effects of OT on lipid metabolism, we examined the effects of serial OT doses (0, 10, 30, 100, 150, 300 nM) on 3T3L1 adipocytes, together with long (144 hours, 6 days) and short (24 hours, 1 day) term treatments. The short-term treatment with 150 nM OT increased triacylglycerol (TAG) accumulation and decreased mRNA expressions of carnitine palmitoyltransferase 1α (CPT-1α) and fatty acid binding protein 4 (FABP4). After long-term incubation with 150 nM OT, only the CPT-1α mRNA
In neurons, AMPA receptor (AMPAR) function depends essentially on their constituent components:the ion channel forming subunits and ion channel associated proteins. On the other hand, AMPAR trafficking is tightly regulated by a vast number of intracellular neuronal proteins that bind to AMPAR subunits. It has been recently shown that the interaction between the GluA1 subunit of AMPARs and carnitine palmitoyltransferase 1C (CPT1C), a novel protein partner of AMPARs, is important in modulating surface expression of these ionotropic glutamate receptors. Indeed, synaptic transmission in CPT1C knockout (KO) mice is diminished supporting a positive trafficking role for that protein. However, the molecular mechanisms of such modulation remain unknown although a putative role of CPT1C in depalmitoylating GluA1 has been hypothesized. Here, we explore that possibility and show that CPT1C effect on AMPARs is likely due to changes in the palmitoylation state of GluA1. Based on in silico analysis, Ser 252, His 470
Insulin resistance (IR) is a common pathophysiological feature of Type 2 diabetes. Although the mechanisms leading to IR are still elusive, evidence has shown that aerobic exercise can reverse this process. To investigate the effects of aerobic exercise on IR, the authors created an IR animal model by feeding C57BL/6 mice a high-fat diet for 8 wk. They then compared the effect of 6 wk of treadmill training (60 min/d) at 75% VO2max on mice in normal-diet (NE) and high-fat-diet (HE) groups with their sedentary control groups. Levels of skeletal-muscle AMPKα (AMP-activated protein kinase α), ACC (acetyl-CoA carboxylases), and CPT1 (carnitine palmitoyltransferase 1) mRNA and AMPKα, pAMPK-Thr172, ACC, pACC-Ser79, and CPT1 protein expressions were analyzed. In addition, fasting serum levels of insulin, triglyceride, and cholesterol were measured. The results demonstrate that 6 wk of exercise increased AMPKα mRNA expression by 11% and 25 % (p , .01) in the NE and HE groups, respectively, and AMPKα ...
This Pilot study follows up on a publication entitled A novel X-linked inborn error of carnitine biosynthesis and a neuronal carnitine pathway hypothesis for autism. This paper describes a new genetic condition (called TMLHE deficiency) that results in the loss of ability to make carnitine in the body.
p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.,/p> ,p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.,/p> ,p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).,/p> ,p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x,sup>64,/sup> + x,sup>4,/sup> + x,sup>3,/sup> + x + 1. The algorithm is described in the ISO 3309 standard. ,/p> ,p class=publication>Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.,br /> ,strong>Cyclic redundancy and other checksums,/strong>,br /> ,a href=http://www.nrbook.com/b/bookcpdf.php>Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993),/a>),/p> Checksum:i ...
Although our bodies make carnitine they often dont produce enough. Find out how supplements can fill in the gaps for better health and energy.
May be involved in protein transport from Golgi to cell surface. The ZDHHC9-GOLGA7 complex is a palmitoyltransferase specific for HRAS and NRAS (By similarity).
The IUPHAR/BPS Guide to Pharmacology. malonyl-CoA ligand page. Quantitative data and detailed annnotation of the targets of licensed and experimental drugs.
L-carnitine is a naturally occurring derivative of the amino acid carnitine, which plays a vital role in the metabolism of fat. It functions as a...
Livon-Lypo-Spheric-ACETYL L-CARNITINE is the leading liposomal supplement that contains ALCAR and helps raise the levels of carnitine in your brain. It assimilates di..
Heart Healthy Supplement Involved in Fat Metabolism, Energy Production, Muscle Utilization and More! Carnitine is central to the bodys ability
hello, I am trying to find out if cpt codes 11041 and 17250 can be billed together and how often? the 17250 keeps coming back as bundled but per cci.c
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 ...
Carnitine O-palmitoyltransferase breaks it down into palmitoyl CoA. Carnitine O-palmitoyltransferase v t e Metabolism portal. ... Palmitoylcarnitine is an ester derivative of carnitine involved in the metabolism of fatty acids. ...
"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 ...
... may refer to: Carnitine palmitoyltransferase II, an important metabolic enzyme. Carnitine palmitoyltransferase II ...
Crabtree B, Newsholme EA (December 1972). "The activities of lipases and carnitine palmitoyltransferase in muscles from ...
"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 ...
Blepharospasm Carnitine palmitoyltransferase II deficiency Fasciculation Myoclonic jerk (myoclonus) Superior oblique myokymia ...
Blepharospasm Carnitine palmitoyltransferase II deficiency Myokymia Blackman G, Cherfi Y, Morrin H, et al. (2019). "The ...
"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 ...
Malonyl-CoA inhibits the carnitine palmitoyltransferase (CPT) that controls the entry and oxidation of LCFA. The glucose- ...
"Evidence that the AMP-activated protein kinase stimulates rat liver carnitine palmitoyltransferase I by phosphorylating ...
Carnitine palmitoyltransferase is also regulated 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 ...
2002). "Structural model of a malonyl-CoA-binding site of carnitine octanoyltransferase and carnitine palmitoyltransferase I: ... Peroxisomal carnitine O-octanoyltransferase is an enzyme that in humans is encoded by the CROT gene. Carnitine ... is a carnitine acyltransferase that catalyzes the reversible transfer of fatty acyl groups between CoA and carnitine. This ... "Entrez Gene: CROT carnitine O-octanoyltransferase". Human CROT genome location and CROT gene details page in the UCSC Genome ...
Transport of acyl-CoA into the mitochondria requires carnitine palmitoyltransferase 1 (CPT1), which converts acyl-CoA into ...
... carnitine palmitoyltransferase and glycerophosphate acyltransferase compared to peroxisomal beta-oxidation and palmitoyl-CoA ...
... 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 ... Acyl-carnitine is shuttled inside by a carnitine-acylcarnitine translocase, ... The liberated carnitine is shuttled back to the cytosol, as an acyl-CoA is shuttled into the mitochondrial matrix. Beta ...
... carnitine palmitoyl transferase), leading to lipogenesis and insulin resistance. Further to this, reduced vitamin B12 ...
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 ...
... including uncoupling protein 1 and carnitine palmitoyltransferase 1b. Estrogen-related receptor alpha (ERRa) can activate ...
Acyl CoA is conjugated to carnitine by carnitine acyltransferase I (palmitoyltransferase) I located on the outer mitochondrial ... The liberated carnitine returns to the cytosol. It is important to note that carnitine acyltransferase I undergoes allosteric ... is converted to acyl CoA by carnitine acyltransferase (palmitoyltransferase) II located on the inner mitochondrial membrane. ... membrane Acyl carnitine is shuttled inside by a translocase Acyl carnitine (such as Palmitoylcarnitine) ...
... syndrome Carnitine palmitoyl transferase deficiency Carnitine palmitoyltransferase I deficiency Carnitine palmitoyltransferase ... II deficiency Carnitine transporter deficiency Carnitine-acylcarnitine translocase deficiency Carnosinase deficiency ...
... carnitine palmitoyl transferase, and cholesterol esterification) Propionyl-CoA Butyryl-CoA Myristoyl-CoA Crotonyl-CoA ...
... is thought to control fatty acid oxidation by means of the ability of malonyl-CoA to inhibit carnitine palmitoyltransferase I, ...
Carnitine-acylcarnitine translocase. *Carnitine palmitoyltransferase II. Beta oxidation. General. *Acyl CoA dehydrogenase ( ...
Carnitine palmitoyltransferase I. *Long-chain-fatty-acid-CoA ligase. tryptophan metabolism. *Kynureninase ...
carnitine palmitoyltransferase I deficiency. *Charcot-Marie-Tooth disease. *Charcot-Marie-Tooth disease, type 4 ...
palmitoyltransferases: Carnitine O-palmitoyltransferase *CPT1. *CPT2. *Serine C-palmitoyltransferase *SPTLC1. *SPTLC2. *other: ...
Carnitine palmitoyltransferase I. *Long-chain-fatty-acid-CoA ligase. tryptophan metabolism. *Kynureninase ...
Carnitine-acylcarnitine translocase. *Carnitine palmitoyltransferase II. Beta oxidation. General. *Acyl CoA dehydrogenase ( ... block for new fatty acids and can inhibit the transfer of the fatty acyl group from acyl CoA to carnitine with carnitine ...
Carnitine-acylcarnitine translocase. *Carnitine palmitoyltransferase II. Beta oxidation. General. *Acyl CoA dehydrogenase ( ...
Carnitine palmitoyltransferase I. *Long-chain-fatty-acid-CoA ligase. tryptophan metabolism. *Kynureninase ...
Carnitine palmitoyltransferase I. *Long-chain-fatty-acid-CoA ligase. tryptophan metabolism. *Kynureninase ...
Carnitine-acylcarnitine translocase. *Carnitine palmitoyltransferase II. Beta oxidation. General. *Acyl CoA dehydrogenase ( ... carnitine biosynthetic process. • medium-chain fatty acid catabolic process. • carnitine metabolic process, CoA-linked. • fatty ...
Carnitine palmitoyltransferase I. *Long-chain-fatty-acid-CoA ligase. tryptophan metabolism. *Kynureninase ...
Carnitine palmitoyltransferase II deficiency. *Charcot-Marie-Tooth disease, types 1 and 2 ...
palmitoyltransferases: Carnitine O-palmitoyltransferase *CPT1. *CPT2. *Serine C-palmitoyltransferase *SPTLC1. *SPTLC2. *other: ...
Carnitine palmitoyltransferase II deficiency. *Myokymia. ReferencesEdit. *^ Blexrud MD, Windebank AJ, Daube JR (1993). "Long- ...
CPT2: carnitine palmitoyltransferase II. *DBT: dihydrolipoamide branched chain transacylase E2. *DIRAS3: DIRAS family, GTP- ...
Carnitine-acylcarnitine translocase. *Carnitine palmitoyltransferase II. Beta oxidation. General. *Acyl CoA dehydrogenase ( ...
Carnitine palmitoyltransferase I. *Long-chain-fatty-acid-CoA ligase. tryptophan metabolism. *Kynureninase ...
... 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, ...
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 ...
... 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 ...
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 ...
Carnitine O-palmitoyltransferase (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 ...
Carnitine palmitoyltransferase II (CPT II) deficiency is a condition that prevents the body from using certain fats for energy ... CARNITINE PALMITOYLTRANSFERASE II DEFICIENCY, LETHAL NEONATAL. *CARNITINE PALMITOYLTRANSFERASE II DEFICIENCY, MYOPATHIC, STRESS ... Carnitine palmitoyltransferase II deficiency *Genetic Testing Registry: Carnitine palmitoyltransferase II deficiency, infantile ... medlineplus.gov/genetics/condition/carnitine-palmitoyltransferase-ii-deficiency/ Carnitine palmitoyltransferase II deficiency. ...
Carnitine palmitoyltransferase II deficiency, hepatocardiomuscular. Carnitine palmitoyltransferase II deficiency with ...
... Review. In: GeneReviews® [Internet]. Seattle (WA): University of Washington, ... Clinical characteristics: Carnitine palmitoyltransferase 1A (CPT1A) deficiency is a disorder of long-chain fatty acid oxidation ... detection of biallelic pathogenic variants in CPT1A on molecular genetic testing or diminished carnitine palmitoyltransferase 1 ... C6-C10 fatty acids do not require the carnitine shuttle for entry into the mitochondrion). Prevention of secondary ...
... improve beta-oxidation of fatty acids and to reduce episodes of rhabdomyolysis in patients with carnitine palmitoyltransferase ... Fenofibrate Therapy in Carnitine Palmitoyl Transferase Type 2 Deficiency. I. Hamilton-Craig. ,1 M. Yudi. ,2 L. Johnson. ,3 and ... Carnitine palmitoyl transferase type 2 (CPT2) deficiency is a rare autosomal recessive disorder of mitochondrial fatty acid ... E. Sigauke, D. Rakheja, K. Kitson, and M. J. Bennett, "Carnitine palmitoyltransferase II deficiency: a clinical, biochemical, ...
Carnitine palmitoyltransferase 1B isoform a variantImported. ,p>Information which has been imported from another database using ... tr,Q53FV7,Q53FV7_HUMAN Carnitine palmitoyltransferase 1B isoform a variant (Fragment) OS=Homo sapiens OX=9606 PE=2 SV=1 ... Belongs to the carnitine/choline acetyltransferase family.UniRule annotation. ,p>Information which has been generated by the ...
J:79496 Price N, et al., A novel brain-expressed protein related to carnitine palmitoyltransferase I. Genomics. 2002 Oct;80(4): ...
... the carnitine palmitoyltransferase (CPT) system has since come to be recognized as a pivotal component of fuel homeostasis. ... The mitochondrial carnitine palmitoyltransferase system. From concept to molecular analysis Eur J Biochem. 1997 Feb 15;244(1):1 ... the carnitine palmitoyltransferase (CPT) system has since come to be recognized as a pivotal component of fuel homeostasis. ...
Learn more about Carnitine Palmitoyltransferase Ii Deficiency from related diseases, pathways, genes and PTMs with the Novus ... Carnitine Palmitoyltransferase Ii Deficiency: Disease Bioinformatics. Research of Carnitine Palmitoyltransferase Ii Deficiency ... Carnitine Palmitoyltransferase Ii Deficiency is also known as Carnitine Palmitoyl Transferase 2 Deficiency. ... Explore more on Carnitine Palmitoyltransferase Ii Deficiency below! For more information on how to use Laverne, please read the ...
Carnitine O-palmitoyltransferase 2, mitochondrial. A. 653. Rattus norvegicus. Mutation(s): 0 Gene Names: Cpt2, Cpt-2. EC: 2.3. ... Carnitine palmitoyl transferase 2 (CPT-2) is a key enzyme in the mitochondrial fatty acid metabolism. The active site is ... Carnitine palmitoyl transferase 2 (CPT-2) is a key enzyme in the mitochondrial fatty acid metabolism. The active site is ... CRYSTAL STRUCTURE OF RAT CARNITINE PALMITOYLTRANSFERASE 2 IN COMPLEX WITH CoA-site inhibitor. *DOI: 10.2210/pdb4EP9/pdb ...
Carrier screening in cases where there is a family history of carnitine palmitoyltransferase II deficiency, but disease-causing ... Confirmation of diagnosis of carnitine palmitoyltransferase II deficiency ... Carrier screening in cases where there is a family history of carnitine palmitoyltransferase II deficiency, but disease-causing ...
Carnitine palmitoyltransferase-1 (CPT1) is a rate-limiting step of mitochondrial β-oxidation by controlling the mitochondrial ... Carnitine palmitoyltransferase-1b deficiency aggravates pressure overload-induced cardiac hypertrophy caused by lipotoxicity.. ... Carnitine Palmitoyltransferase-1b (CPT1b) Deficiency Aggravates Pressure-Overload-Induced Cardiac Hypertrophy due to ... Carnitine Palmitoyltransferase-1b (CPT1b) Deficiency Aggravates Pressure-Overload-Induced Cardiac Hypertrophy due to ...
Inhibitory activity against rat-liver mitochondrial Carnitine palmitoyl transferase II. ...
CARNITINE PALMITOYLTRANSFERASE II DEFICIENCY, LATE-ONSET. Carnitine Palmitoyltransferase II. Carnitine palmitoyl transferase 1A ... Carnitine palmitoyltransferase 2/Citrate synthase:CRto:Pt:RBC:Qn. Carnitine palmitoyltransferase 2:CCnt:Pt:Amnio fld cells:Qn. ... Carnitine O-Palmitoyltransferase. Known as: Palmitoyltransferase, Carnitine, Acyltransferase, Palmitylcarnitine, O- ... Palmitoyltransferase, Carnitine Expand. An enzyme that catalyzes reversibly the conversion of palmitoyl-CoA to ...
... carnitine palmitoyltransferase (hexadecanoyl-CoA:carnitine O-hexadecanoyltransferase, EC 2.3.1.23), and its role in the... ... Carnitine and carnitine palmitoyltransferase in metabolic studies, in:Carnitine Biosynthesis, Metabolism, and Functions ( R. A ... Carnitine palmitoyltransferase II deficiency with normal carnitine palmitoyltransferase I in skeletal muscle and leukocytes, J ... Comparison of properties of carnitine palmitoyltransferase I with those of carnitine palmitoyltransferase II, and preparation ...
CPT, carnitine palmitoyltransferase; EMCL, extramyocellular lipid; FFA, free fatty acid; HMRS, 1H magnetic resonance ... Lopaschuk GD, Wall SR, Olley PM, Davies NJ: Etomoxir, a carnitine palmitoyltransferase I inhibitor, protects hearts from fatty ... Prolonged Inhibition of Muscle Carnitine Palmitoyltransferase-1 Promotes Intramyocellular Lipid Accumulation and Insulin ... Prolonged Inhibition of Muscle Carnitine Palmitoyltransferase-1 Promotes Intramyocellular Lipid Accumulation and Insulin ...
Carnitine palmitoyltransferase-2 (CPT2) is a mitochondrial enzyme involved in long-chain fatty acid entry into mitochondria for ... Carnitine palmitoyltransferase-2 (CPT2) is a mitochondrial enzyme involved in long-chain fatty acid entry into mitochondria for ... Resveratrol-Induced Changes in MicroRNA Expression in Primary Human Fibroblasts Harboring Carnitine-Palmitoyl Transferase-2 ... "Resveratrol-Induced Changes in MicroRNA Expression in Primary Human Fibroblasts Harboring Carnitine-Palmitoyl Transferase-2 ...
Carnitine O-palmitoyltransferase 2, mitochondrial. A, B. 634. Rattus norvegicus. Mutation(s): 0 Gene Names: Cpt2, Cpt-2. EC: ... Carnitine palmitoyl transferase 2 (CPT-2) is a key enzyme in the mitochondrial fatty acid metabolism. The active site is ... Carnitine palmitoyl transferase 2 (CPT-2) is a key enzyme in the mitochondrial fatty acid metabolism. The active site is ... Crystal structure of rat carnitine palmitoyltransferase 2 in complex with 1-[(R)-2-(3,4-Dihydro-1H-isoquinoline-2-carbonyl)- ...
... disorders are caused by defects in one of the FAO enzymes that regulates cellular uptake of fatty acids and free carnitine. An ... However, the diagnosis of primary carnitine deficiency (PCD) or carnitine palmitoyltransferase-1 (CPT1) deficiency using the ... Extracellular acylcarnitine (AC) profiling detects carnitine palmitoyltransferase-2, carnitine acylcarnitine translocase, and ... in vitro probe acylcarnitine assay for identifying deficiencies of carnitine transporter and carnitine palmitoyltransferase-1. ...
Structural model of carnitine palmitoyltransferase I based on the carnitine acetyltransferase crystal. Biochem J. 2004 May 1; ... Showing Protein Carnitine O-palmitoyltransferase 1, liver isoform (HMDBP00309). IdentificationBiological propertiesGene ... IJlst L, Mandel H, Oostheim W, Ruiter JP, Gutman A, Wanders RJ: Molecular basis of hepatic carnitine palmitoyltransferase I ... Stoler JM, Sabry MA, Hanley C, Hoppel CL, Shih VE: Successful long-term treatment of hepatic carnitine palmitoyltransferase I ...
Carnitine palmitoyltransferase 1 (CPT1) is a mitochondrial transmembrane enzyme thought to be rate limiting for long-chain ... Overexpression of Carnitine Palmitoyltransferase-1 in Skeletal Muscle Is Sufficient to Enhance Fatty Acid Oxidation and Improve ... Overexpression of Carnitine Palmitoyltransferase-1 in Skeletal Muscle Is Sufficient to Enhance Fatty Acid Oxidation and Improve ... Overexpression of Carnitine Palmitoyltransferase-1 in Skeletal Muscle Is Sufficient to Enhance Fatty Acid Oxidation and Improve ...
Combined partial deficiency of muscle carnitine palmitoyltransferase and carnitine with autosomal dominant inheritance. ... Combined partial deficiency of muscle carnitine palmitoyltransferase and carnitine with autosomal dominant inheritance. ... glycolysis and normal glycogen content but combined partial deficiency of muscle carnitine palmitoyltransferase and carnitine ... Plasma concentration of ketone bodies and acid soluble acyl-carnitine increased normally with prolonged fasting. The ...
Carnitine palmitoyltransferase-I (CPT-I) plays a crucial role in regulating cardiac fatty acid oxidation which provides the ... Differential regulation in the heart of mitochondrial carnitine palmitoyltransferase-I muscle and liver isoforms. ...
... carnitine palmitoyl transferase (CPT)-1.. Acetylcholine-induced endothelium-dependent relaxation in mouse thoracic aortic (MTA ... ß ACTIVATION ON LIPID-INDUCED ENDOTHELIAL DYSFUNCTION via CARNITINE PALMITOYL TRANSFERASE-1 UPREGULATION ... ß ACTIVATION ON LIPID-INDUCED ENDOTHELIAL DYSFUNCTION via CARNITINE PALMITOYL TRANSFERASE-1 UPREGULATION ...
Her doctor said that she had SCOT deficiency OR carnitine palmitoyl transferase 1 deficiency. Now she is normal. Will this ... Will medical crises due to either carnitine palmitoyl transferase 1 deficiency or SCOT deficiency happen again? ... Will medical crises due to either carnitine palmitoyl transferase 1 deficiency or SCOT deficiency happen again? ...
What is carnitine palmitoyltransferase? Meaning of carnitine palmitoyltransferase medical term. What does carnitine ... Looking for online definition of carnitine palmitoyltransferase in the Medical Dictionary? carnitine palmitoyltransferase ... and carnitine palmitoyltransferase (CPT II) in the inner mitochondrial membrane (carnitine O-palmitoyltransferase EC 2.. ... Acetyl-L-Carnitine supplementation reverses the age-related decline in carnitine palmitoyltransferase 1 (cpt1) activity in ...
Carnitine palmitoyltransferase (CPT) II deficiency results in two different clinical forms, one with systemic and the other ... CARNITINE PALMITOYLTRANSFERASE II / GENE ANALYSIS / MISSENSE MUTATION / TRANSFECTION / GENE POLYMORPHISM / 遺伝子導入. ... form of carnitine palmitoyltransferase II deficiency Human Genetics. 98. 116-118 (1996). *. Description. 「研究成果報告書概要(欧文)」より ... hepaticform of carnitine palmitoyltransferase II deficiency Human Genetics. 98. 116-118 (1996). *. Description. 「研究成果報
Etomoxir sodium salt is an irreversible inhibitor of carnitine palmitoyltransferase-1 (CPT-1) on the outer face of the inner ... Here we show that when FAO was reduced approximately 90% by pharmacological inhibition of carnitine palmitoyltransferase I ( ... Identifying off-target effects of etomoxir reveals that carnitine palmitoyltransferase I is essential for cancer cell ... Identifying off-target effects of etomoxir reveals that carnitine palmitoyltransferase I is essential for cancer cell ...
... oxidation is thought to be transport of FAs across the mitochondrial membrane by carnitine palmitoyltransferase I (CPT I). To ... oxidation is thought to be transport of FAs across the mitochondrial membrane by carnitine palmitoyltransferase I (CPT I). To ... Overexpression of carnitine palmitoyltransferase I in skeletal muscle in vivo increases fatty acid oxidation and reduces ... Overexpression of carnitine palmitoyltransferase I in skeletal muscle in vivo increases fatty acid oxidation and reduces ...
  • Palmitoylcarnitine Palmitoyl CoA There are four different forms of CPT in humans: CPT1A - associated with Carnitine palmitoyltransferase I deficiency CPT1B CPT1C CPT2 - associated with carnitine palmitoyltransferase II deficiency Fatty acid degradation § Transport into the mitochondrial matrix Jogl G, Tong L (January 2003). (wikipedia.org)
  • Carnitine palmitoyltransferase 1A (CPT1A) deficiency is a disorder of long-chain fatty acid oxidation. (nih.gov)
  • The diagnosis of CPT1A is established in a proband by the detection of biallelic pathogenic variants in CPT1A on molecular genetic testing or diminished carnitine palmitoyltransferase 1 (CPT 1) enzyme activity on cultured skin fibroblasts when molecular genetic testing is not definitive. (nih.gov)
  • These pathways complement our catalog of research reagents for the study of Carnitine Palmitoyltransferase Ii Deficiency including antibodies and ELISA kits against CPT2, CPT1A, ETFDH, CHPT1, CHKA. (novusbio.com)
  • Here, we show that carnitine palmitoyltransferase 1A (CPT1A) has lysine succinyltransferase (LSTase) activity in vivo and in vitro. (elsevier.com)
  • Importantly, mutation of CPT1A Gly710 (G710E) selectively inactivated carnitine palmitoyltransferase (CPTase) activity but not the LSTase activity that decreased enolase activity in cells and promoted cell proliferation under glutamine depletion. (elsevier.com)
  • Mutation of CPT1A Gly710 (G710E) selectively inactivates canonical carnitine palmitoyltransferase (CPTase) activity but not LSTase activity. (elsevier.com)
  • The "CPT1A" form is associated with carnitine palmitoyltransferase I deficiency. (colegiomontpellier.net)
  • Carnitine Palmitoyltransferase 1A Deficiency Bennett MJ - 2016 PMID: 20301700: Organization of the human liver carnitine palmitoyltransferase 1 gene ( CPT1A) and identification of novel mutations in hypoketotic hypoglycaemia. (colegiomontpellier.net)
  • Diseases associated with CPT1A include Carnitine Palmitoyltransferase I Deficiency and Carnitine Palmitoyltransferase Ii Deficiency, Infantile . (genecards.org)
  • T) variant of carnitine palmitoyltransferase 1 (CPT1A) is frequent in some aboriginal populations and may be associated with increased infant deaths. (cdc.gov)
  • CPT1A sequencing is a molecular test used to identify variants in the gene associated with Carnitine Palmitoyltransferase IA Deficiency. (ggc.org)
  • Prevalence of carnitine palmitoyltransferase 1A (CPT1A). (ubc.ca)
  • carnitine palmitoyltransferase 1A , or CPT1A for short. (adn.com)
  • Specifically, oxidation of fatty acids (FAO) was reduced in these cells, which linked to reduced carnitine palmitoyltransferase 1a (Cpt1a), an essential enzyme for carnitine shuttle. (frontiersin.org)
  • L-Carnitine treatment augmented FAO but attenuated CSE-induced apoptosis by upregulating Cpt1a. (frontiersin.org)
  • Carnitine palmitoyltransferase-1 (CPT1) is a rate-limiting step of mitochondrial β-oxidation by controlling the mitochondrial uptake of long-chain acyl-CoAs. (nih.gov)
  • However, the diagnosis of primary carnitine deficiency (PCD) or carnitine palmitoyltransferase-1 (CPT1) deficiency using the conventional IVP assay has been hampered by the presence of a large amount of free carnitine (C0), a key molecule deregulated by these deficiencies. (biomedsearch.com)
  • We hypothesized that skeletal muscle-specific overexpression of the muscle isoform of carnitine palmitoyltransferase 1 (CPT1), the enzyme that controls the entry of long-chain fatty acyl CoA into mitochondria, would enhance rates of fatty acid oxidation and improve insulin action in muscle in high-fat diet insulin-resistant rats. (diabetesjournals.org)
  • We investigated whether the age-related impairment of cardiac fatty acid catabolism occurs, at least partially, through diminished levels of L-carnitine, which would adversely affect carnitine palmitoyltransferase 1 (CPT1), the rate-limiting enzyme for fatty acyl-CoA uptake into mitochondria for beta]-oxidation. (thefreedictionary.com)
  • PubMed:14711372 ] Mitochondrial carnitine palmitoyltransferase‐1 (CPT1) is a target for oxidative inactivation in human cells. (colegiomontpellier.net)
  • Fatty acid β-oxidation is the major metabolic pathway for generating adenosine triphosphate (ATP) in the kidneys, which is governed by carnitine palmitoyltransferase 1 (CPT1). (elsevier.com)
  • Carnitine palmitoyltransferase I (CPT1) is the main rate-limiting step in β-oxidation and represents a key regulatory site controlling flux through this pathway by virtue of its inhibition by the fatty acid synthesis precursor malonyl-CoA ( McGarry and Mannaerts, 1977 ). (frontiersin.org)
  • Dysregulated lipid metabolism and mitochondrial dysfunction are hypothesized to play a key role in MS. Carnitine Palmitoyl Transferase 1 (CPT1) is a rate-limiting enzyme for beta-oxidation of fatty acids in mitochondria. (au.dk)
  • 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)
  • CPT2 together with carnitine palmitoyltransferase I oxidizes long-chain fatty acids in the mitochondria. (wikipedia.org)
  • Carnitine palmitoyltransferase-2 ( CPT2 ) is a mitochondrial enzyme involved in long-chain fatty acid entry into mitochondria for their β-oxidation and energy production. (mdpi.com)
  • This enzyme attaches long chain fatty acids to carnitine so they can be moved into the mitochondria. (diseaseinfosearch.org)
  • Fatty acids are then moved into the mitochondria (the part of cell where energy is made) using carnitine. (diseaseinfosearch.org)
  • Once inside the mitochondria, CPII takes the carnitine off, so the fatty acids can then be used for energy. (diseaseinfosearch.org)
  • Diagram of long-chain fatty acid (LCFA) import into the mitochondria by the carnitine shuttle. (colegiomontpellier.net)
  • The protein encoded by this gene, a member of the carnitine/choline acetyltransferase family, is the rate-controlling enzyme of the long-chain fatty acid beta-oxidation pathway in muscle mitochondria. (nih.gov)
  • Transport of fatty acids into the mitochondria for β-oxidation is mediated by a carnitine carrier system. (frontiersin.org)
  • Without enough of this enzyme, carnitine is not removed from long-chain fatty acids. (medlineplus.gov)
  • First conceptualized as a mechanism for the mitochondrial transport of long-chain fatty acids in the early 1960s, the carnitine palmitoyltransferase (CPT) system has since come to be recognized as a pivotal component of fuel homeostasis. (nih.gov)
  • This chapter will review the data describing the mitochondrial enzyme, carnitine palmitoyltransferase (hexadecanoyl-CoA:carnitine O -hexadecanoyltransferase, EC 2.3.1.23), and its role in the transport and metabolism of long-chain fatty acids. (springer.com)
  • Catalyzes the transfer of the acyl group of long-chain fatty acid-CoA conjugates onto carnitine, an essential step for the mitochondrial uptake of long-chain fatty acids and their subsequent beta-oxidation in the mitochondrion. (hmdb.ca)
  • an enzyme that catalyzes the transfer between coenzyme A and carnitine of long-chain fatty acids. (thefreedictionary.com)
  • Carnitine palmitoyltransferase II (CPT II) deficiency is an autosomal inherited metabolic disorder in which the β-oxidation of the long chain fatty acids is defective. (elitmed.hu)
  • Long-chain fatty acids in all tissues and medium-chain fatty acids in most tissues (an important exception is the liver) are esterified to coenzyme A in the cytosol and cannot enter the mitochondrial matrix to undergo beta oxidation without the action of carnitine and 3 proteins (carnitine palmitoyltransferase 1, carnitine acylcarnitine translocase, and carnitine palmitoyltransferase 2). (colegiomontpellier.net)
  • Carnitine palmitoyltransferase II deficiency is a condition that prevents the body from converting certain fats called long-chain fatty acids into energy, particularly during periods without food (fasting). (unt.edu)
  • Together with carnitine, this enzyme helps release long-chain fatty acids from a particular transport enzyme. (unt.edu)
  • If carnitine palmitoyltransferase II is defective, long-chain fatty acids from food and fats stored in the body cannot be broken down and processed. (unt.edu)
  • The mitochondrial oxidation of long-chain fatty acids is initiated by the sequential action of carnitine palmitoyltransferase I (which is located in the outer membrane and is detergent-labile) and carnitine palmitoyltransferase II (which is located in the inner membrane and is detergent-stable), together with a carnitine-acylcarnitine translocase. (genecards.org)
  • considering the fact that basically the smallest fraction of data facing Carnitine palmitoyltransferase I deficiency is listed in se's, equivalent to www.google.com or others, a non-systematic method of net study should be not just time eating, but in addition incomplete. (manuel-monroy.com)
  • Bezafibrate therapy resulted in 60-284% improvement in skeletal muscle palmitoyl L-carnitine oxidation levels, 20-93% increase in skeletal muscle CPT2 mRNA, and full correction of the initial defective fatty acid oxidation in myoblasts in vitro . (hindawi.com)
  • Two additional groups (low-fat + etoxomir and lard + etoxomir) consumed diets containing 0.01% of the carnitine palmitoyltransferase-1 inhibitor, R-etomoxir, which produced chronic blockade of enzyme activity in liver and skeletal muscle. (diabetesjournals.org)
  • Yeung, Oscar W.H. Carnitine palmitoyltransferase and carnitine octanoyltransferase activities in liver, kidney cortex, adipocyte, lactating mamary gland, skeletal muscle and heart. (colegiomontpellier.net)
  • Extracellular acylcarnitine (AC) profiling detects carnitine palmitoyltransferase-2, carnitine acylcarnitine translocase, and other FAO deficiencies. (biomedsearch.com)
  • carnitine/acylcarnitine translocase (CACT) within the inner mitochondrial membrane, and carnitine palmitoyltransferase (CPT II) in the inner mitochondrial membrane (carnitine O-palmitoyltransferase EC 2. (thefreedictionary.com)
  • Severe rhabdomyolysis with hypoglycemia in an adult patient with carnitine palmitoyltransferase II deficiency. (colegiomontpellier.net)
  • What genes are related to carnitine palmitoyltransferase II deficiency? (unt.edu)
  • This gene provides instructions for making an enzyme called carnitine palmitoyltransferase 2. (medlineplus.gov)
  • Mutations in the CPT2 gene reduce the activity of carnitine palmitoyltransferase 2. (medlineplus.gov)
  • Carnitine O-palmitoyltransferase 2, mitochondrial is an enzyme that in humans is encoded by the CPT2 gene. (wikipedia.org)
  • Defects in this gene are associated with mitochondrial long-chain fatty-acid (LCFA) oxidation disorders and carnitine palmitoyltransferase II deficiency. (wikipedia.org)
  • Aires V, Delmas D, Djouadi F, Bastin J, Cherkaoui-Malki M, Latruffe N. Resveratrol-Induced Changes in MicroRNA Expression in Primary Human Fibroblasts Harboring Carnitine-Palmitoyl Transferase-2 Gene Mutation, Leading to Fatty Acid Oxidation Deficiency. (mdpi.com)
  • Two novel gene mutations(Glu174→Lys,Phe383→Tyr)causing the 'hepatic'form of carnitine palmitoyltransferase II deficiency' Human Genetics. (nii.ac.jp)
  • This gene provides the code to make the protein, carnitine palmitoyltransferase II (CPII). (diseaseinfosearch.org)
  • If there is a mutation to the CPT2 gene, there is not enough CPII made to remove the carnitine. (diseaseinfosearch.org)
  • Identification of 16 new disease-causing mutations in the CPT2 gene resulting in carnitine palmitoyltransferase II deficiency. (colegiomontpellier.net)
  • Mutations in the CPT2 gene cause carnitine palmitoyltransferase II deficiency. (unt.edu)
  • Mutations in the CPT2 gene lead to the production of a defective version of an enzyme called carnitine palmitoyltransferase II. (unt.edu)
  • CPT1B (Carnitine Palmitoyltransferase 1B) is a Protein Coding gene. (genecards.org)
  • GO annotations related to this gene include transferase activity, transferring acyl groups and carnitine O-palmitoyltransferase activity . (genecards.org)
  • Gene Ontology (GO) annotations related to this gene include identical protein binding and carnitine O-palmitoyltransferase activity . (genecards.org)
  • Transgenic mice carrying the human heart muscle carnitine palmitoyltransferase I (M-CPTI) gene fused to a CAT reporter gene were generated to study the regulation of M-CPTI gene expression. (elsevier.com)
  • Etomoxir sodium salt is an irreversible inhibitor of carnitine palmitoyltransferase-1 (CPT-1) on the outer face of the inner mitochondrial membrane. (selleckchem.com)
  • Using a real time confocal microscopy assay, it was found that the carnitine palmitoyltransferase I (CPTI) inhibitor, etomoxir, reduced mitochondrial fusion dynamics in a time-dependent manner. (frontiersin.org)
  • Carnitine palmitoyltransferase II precursor (CPT2) is a mitochondrial membrane protein which is transported to the mitochondrial inner membrane. (wikipedia.org)
  • Tandem mass spectrometry identified protein abundance differences per mitochondrial mass in insulin resistance, including lower abundance of complex I subunits and enzymes involved in the oxidation of branched-chain amino acids (BCAA) and fatty acids (e.g., carnitine palmitoyltransferase 1B). (forskningsdatabasen.dk)
  • These and other studies on the effects of detergents on the mitochondrial [3H]TG-CoA binding protein provide further support for the model of carnitine palmitoyltransferase proposed in the preceding paper. (elsevier.com)
  • While carnitine palmitoyltransferase I is a different protein in liver and muscle, it seems likely that both tissues share the same transferase II. (elsevier.com)
  • A related transferase is carnitine acyltransferase. (wikipedia.org)
  • A primary biochemical action of malonyl-CoA is the inhibition of the acyltransferase activity of carnitine palmitoyltransferase-1 (CPT-1). (physiology.org)
  • It is known that malonyl-CoA inhibits the acyltransferase activity of carnitine palmitoyltransferase-1 (CPT-1) that converts long-chain fatty acyl-CoA (LCFA-CoA) to long-chain acylcarnitine ( 9 , 23 ). (physiology.org)
  • Novel mutations associated with carnitine palmitoyltransferase II deficiency. (colegiomontpellier.net)
  • Genetic mutations causative for McArdle disease, carnitine palmitoyl transferase deficiency 2, myoadenylate deaminase deficiency, and malignant hyperthermia have all been associated with Exertional rhabdomyolysis. (nih.gov)
  • Characterization of hepatic carnitine palmitoyltransferase. (elsevier.com)
  • Fingerprint Dive into the research topics of 'Characterization of hepatic carnitine palmitoyltransferase. (elsevier.com)
  • Intracellular in vitro probe acylcarnitine assay for identifying deficiencies of carnitine transporter and carnitine palmitoyltransferase-1. (biomedsearch.com)
  • The body can convert L-carnitine to other amino acids called acetyl-L-carnitine and propionyl-L-carnitine. (rxlist.com)
  • Should the Human Carnitine Palmitoyltransferase 2, Mitochondrial (CPT2) ELISA Kit is proven to show malperformance, you will receive a refund or a free replacement. (orbitalbiosciences.com)
  • Description: A sandwich quantitative ELISA assay kit for detection of Human Carnitine Palmitoyltransferase 2, Mitochondrial (CPT2) in samples from tissue homogenates, cell lysates or other biological fluids. (orbitalbiosciences.com)
  • The mitochondrial carnitine palmitoyltransferase system. (nih.gov)
  • Because we had found whole testis from adult rats to be much richer in the messenger RNA for the muscle (M) than for the liver (L) form of mitochondrial carnitine palmitoyltransferase I (CPT I), we sought to determine which cell type(s) accounts for this expression pattern and how it might relate to reproductive function. (elsevier.com)
  • 3) association of carnitine palmitoyltransferase I with a membrane component(s) is necessary for catalytic activity. (elsevier.com)
  • 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)
  • Her doctor said that she had SCOT deficiency OR carnitine palmitoyl transferase 1 deficiency. (nih.gov)
  • Will medical crises due to either carnitine palmitoyl transferase 1 deficiency or SCOT deficiency happen again? (nih.gov)
  • Following organizations serve the condition "Carnitine Palmitoyl Transferase 1 Deficiency" for support, advocacy or research. (diseaseinfosearch.org)
  • Carnitine O-palmitoyltransferase (also called carnitine palmitoyltransferase) is a mitochondrial transferase enzyme (EC 2.3.1.21) involved in the metabolism of palmitoylcarnitine into palmitoyl-CoA. (wikipedia.org)
  • Research of Carnitine Palmitoyltransferase Ii Deficiency has been linked to Inborn Errors Of Metabolism, Myalgia, Rhabdomyolysis, Hypoglycemia, Weakness. (novusbio.com)
  • Carnitine palmitoyl transferase 2 (CPT-2) is a key enzyme in the mitochondrial fatty acid metabolism. (rcsb.org)
  • Carnitine--metabolism and functions. (semanticscholar.org)
  • A key regulatory point in the control of fatty acid (FA) oxidation is thought to be transport of FAs across the mitochondrial membrane by carnitine palmitoyltransferase I (CPT I). To investigate the role of CPT I in FA metabolism, we used in vivo electrotransfer (IVE) to locally overexpress CPT I in muscle of rodents. (garvan.org.au)
  • abstract = "Carnitine palmitoyltransferase (CPT) is a mitochondrial-inner-membrane enzyme, with activities located on both the outer and inner sides of the membrane. (elsevier.com)
  • abstract = "Carnitine palmitoyl-transferase has been extracted with 0.5% Tween-20 from human liver homogenatc and purified to homogeneity. (elsevier.com)
  • abstract = "Exposure of rat liver mitochondrial membranes to octyl glucoside, Triton X-100, or Tween 20 solubilized an active and tetradecylglycidyl-CoA (TG-CoA)-insensitive carnitine palmitoyltransferase (presumed to be carnitine palmitoyltransferase II). (elsevier.com)
  • Fingerprint Dive into the research topics of 'Are there two forms of carnitine palmitoyltransferase in muscle? (elsevier.com)
  • Pharmacological inhibition of carnitine palmitoyl transfe. (au.dk)
  • Carnitine palmitoyl transferase type 2 (CPT2) deficiency is a rare autosomal recessive disorder of mitochondrial fatty acid oxidation [ 1 ]. (hindawi.com)
  • Researched pathways related to Carnitine Palmitoyltransferase Ii Deficiency include Fatty Acid Oxidation, Lipid Storage, Transport, Lipid Oxidation, Reverse Transcription. (novusbio.com)
  • Mitochondrial fatty acid oxidation (FAO) disorders are caused by defects in one of the FAO enzymes that regulates cellular uptake of fatty acids and free carnitine. (biomedsearch.com)
  • Carnitine palmitoyltransferase-I (CPT-I) plays a crucial role in regulating cardiac fatty acid oxidation which provides the primary source of energy for cardiac muscle contraction. (ovid.com)
  • For example, preliminary evidence suggests that carnitine palmitoyltransferase type 1A deficiency, a fatty acid disorder highly prevalent in AN and other indigenous circumpolar populations, might contribute to infant mortality (8). (thefreedictionary.com)
  • Carnitine palmitoyltransferase (CPT) deficiencies are common disorders of mitochondrial fatty acid oxidation. (colegiomontpellier.net)
  • CPT I is the key enzyme in the carnitine-dependent transport across the mitochondrial inner membrane and its deficiency results in a decreased rate of fatty acid beta-oxidation. (genecards.org)
  • 19 Inactivation of ACC reduces the synthesis of malonyl-CoA, which in turn activates carnitine palmitoyltransferase-1A (CPT-1A) and increases fatty acid oxidation. (rsc.org)
  • https://en.wikipedia.org/wiki/Lipogenesis Fat build-up is determined by the balance between lipogenesis and lipolysis/fatty acid oxidation. (natap.org)
  • The predicted amino acid sequence showed the highest homology (62.6%) with that of carnitine palmitoyltransferase I (CPTI) from rat liver. (tokushima-u.ac.jp)
  • We investigated whether PPARβ activation can prevent palmitate-induced endothelial dysfunction using ex vivo and in vitro models, focusing on the rate-limiting enzyme for beta-oxidation, carnitine palmitoyl transferase (CPT)-1. (bmj.com)
  • Combined partial deficiency of muscle carnitine palmitoyltransferase and carnitine with autosomal dominant inheritance. (bmj.com)
  • The biochemical evaluation of the muscle tissue revealed intact anaerobic glycolysis and normal glycogen content but combined partial deficiency of muscle carnitine palmitoyltransferase and carnitine in both cases. (bmj.com)
  • Carnitine palmitoyl transferase (CPT) deficiency is a rare condition that causes muscle weakness and other symptoms. (umassmemorial.org)
  • Are there two forms of carnitine palmitoyltransferase in muscle? (elsevier.com)
  • But L-carnitine does not seem to improve quality of life , muscle cramping, low blood pressure , breathing function, or exercise performance. (rxlist.com)
  • Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Rat Carnitine Palmitoyltransferase 2, Mitochondrial (CPT2) in Tissue homogenates, cell lysates and other biological fluids. (orbitalbiosciences.com)
  • Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Rat Carnitine Palmitoyltransferase 2, Mitochondrial (CPT2) in samples from Tissue homogenates, cell lysates and other biological fluids with no significant corss-reactivity with analogues from other species. (orbitalbiosciences.com)
  • Serum samples collected on 7th, 15th and 22nd days and carnitine palmitoyl transferase assay done. (jyoungpharm.org)
  • Bezafibrate therapy has been shown to improve beta-oxidation of fatty acids and to reduce episodes of rhabdomyolysis in patients with carnitine palmitoyltransferase type-2 (CPT2) deficiency. (hindawi.com)
  • Carnitine palmitoyl transferase I and the control of myocardial beta-oxidation flux. (semanticscholar.org)
  • article{Eaton2001CarnitinePT, title={Carnitine palmitoyl transferase I and the control of myocardial beta-oxidation flux. (semanticscholar.org)
  • Carnitine palmitoyltransferase I is assumed to be rate limiting for beta-oxidation in all tissues. (semanticscholar.org)
  • CPT1B heterozygous variants of G320D and S427C among control subjects showed significantly higher levels of total and free carnitine in the blood compared to acute myocardial infarction patients. (nih.gov)
  • Belongs to the carnitine/choline acetyltransferase family. (abcam.com)
  • The FDA has approved the use of L-carnitine, either taken by mouth or given intravenously (by IV), for treating L-carnitine deficiency caused by certain genetic diseases or other disorders. (rxlist.com)
  • There is mixed evidence about the effects of L-carnitine in treating disorders caused by low carnitine levels in people with serious kidney disease undergoing hemodialysis. (rxlist.com)
  • Plasma concentration of ketone bodies and acid soluble acyl-carnitine increased normally with prolonged fasting. (bmj.com)
  • Taking a specific product containing L-carnitine and coenzyme Q10 (Carni Q-Gel, Tishcon Corporation, Westbury, NY) also appears to improve symptoms of heart failure. (rxlist.com)
  • Pharmacological use of l-carnitine in uremic anemia : has its full potential been exploited? (warwick.ac.uk)
  • Carnitine Palmitoyltransferase II (CPT2) deficiency (myopathic form) is a rare, progressive adult metabolic myopathy caused by a genetic insufficiency in CPT2 enzyme production. (thefreedictionary.com)
  • Carnitine palmitoyltransferase I deficiency (CPT-IA) is a rare genetic condition. (diseaseinfosearch.org)
  • Carnitine palmitoyltransferase II deficiency (CPTII), lethal neonatal form is a rare genetic condition. (diseaseinfosearch.org)
  • 42 Carnitine Palmitoyltransferase I Deficiency How Is Genetic Testing Done? (manuel-monroy.com)
  • L-carnitine supplements are taken by mouth to increase L-carnitine levels in people whose natural level of L-carnitine is too low because they have a genetic disorder, are taking certain drugs (such as valproic acid for seizures or certain antibiotics for tuberculosis ), or because they are undergoing a medical procedure ( hemodialysis for kidney disease ) that uses up the body's L-carnitine. (rxlist.com)
  • The term 'prevalence' of Carnitine palmitoyl transferase II deficiency, lethal neonatal form usually refers to the estimated population of people who are managing Carnitine palmitoyl transferase II deficiency, lethal neonatal form at any given time. (rightdiagnosis.com)
  • The term 'incidence' of Carnitine palmitoyl transferase II deficiency, lethal neonatal form refers to the annual diagnosis rate, or the number of new cases of Carnitine palmitoyl transferase II deficiency, lethal neonatal form diagnosed each year. (rightdiagnosis.com)