Carnitine O-Palmitoyltransferase: An enzyme that catalyzes reversibly the conversion of palmitoyl-CoA to palmitoylcarnitine in the inner mitochondrial membrane. EC 2.3.1.21.Carnitine: A constituent of STRIATED MUSCLE and LIVER. It is an amino acid derivative and an essential cofactor for fatty acid metabolism.Carnitine O-Acetyltransferase: An enzyme that catalyzes the formation of O-acetylcarnitine from acetyl-CoA plus carnitine. EC 2.3.1.7.Carnitine Acyltransferases: 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.Acetylcarnitine: An acetic acid ester of CARNITINE that facilitates movement of ACETYL COA into the matrices of mammalian MITOCHONDRIA during the oxidation of FATTY ACIDS.gamma-Butyrobetaine Dioxygenase: 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.Malonyl Coenzyme A: A coenzyme A derivative which plays a key role in the fatty acid synthesis in the cytoplasmic and microsomal systems.Organic Cation Transport Proteins: 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.Palmitoylcarnitine: 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.Palmitoyl Coenzyme A: A fatty acid coenzyme derivative which plays a key role in fatty acid oxidation and biosynthesis.Acyltransferases: 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.Betaine: 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)Acyl Coenzyme A: 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.Pentanoic AcidsCoenzyme AMitochondria, Liver: 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)Vitamin B Deficiency: 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.Epoxy Compounds: 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.Fatty Acids: 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)Ketone Bodies: 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.Liver: A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.Ergothioneine: A naturally occurring metabolite of HISTIDINE that has antioxidant properties.Starvation: Lengthy and continuous deprivation of food. (Stedman, 25th ed)3-Hydroxybutyric Acid: BUTYRIC ACID substituted in the beta or 3 position. It is one of the ketone bodies produced in the liver.Lipid Metabolism, Inborn Errors: Errors in the metabolism of LIPIDS resulting from inborn genetic MUTATIONS that are heritable.

*  人CPT1B肽(ab23261)|Abcam中国

Carnitine palmitoyltransferase 1B (muscle). *Carnitine palmitoyltransferase I like protein. *Carnitine palmitoyltransferase I ... Carnitine O-palmitoyltransferase 1, muscle isoform. *Carnitine O-palmitoyltransferase I. *Carnitine palmitoyltransferase 1A ( ... Carnitine O palmitoyltransferase 1B. *Carnitine O palmitoyltransferase I mitochondrial muscle isoform. *Carnitine O ...
abcam.cn/human-cpt1b-peptide-ab23261.html

*  CPT1B Gene - GeneCards | CPT1B Protein | CPT1B Antibody

Carnitine Palmitoyltransferase 1B, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - ... Carnitine O-palmitoyltransferase 1, muscle isoform Protein Accession:. Q92523. Secondary Accessions: *B7Z4U4 ... CPT1B (Carnitine Palmitoyltransferase 1B) is a Protein Coding gene. Diseases associated with CPT1B include Cpt Deficiency, ... carnitine palmitoyl transferase of the outer mitochondrial membrane 1B,88kDa,malonyl CoA sensitive,muscle isoform,generating ...
genecards.org/cgi-bin/carddisp.pl?gene=CPT1B&rf=/home/genecards/current/website/carddisp.pl&origene_full_trans=7

*  RCSB PDB - Protein Feature View - Carnitine O-palmitoyltransferase 2, mitochondrial - P18886 (CPT2 RAT)

The PDB archive contains information about experimentally-determined structures of proteins, nucleic acids, and complex assemblies. As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
rcsb.org/pdb/protein/P18886

*  Carnitine Palmitoyltransferase 1b Deficient Mice Develop Severe Insulin Resistance After Prolonged High Fat Diet Feeding

... ... Background: Carnitine palmitoyltransferase 1 (CPT1) is the rate-limiting enzyme governing the entry of longchain acyl-CoAs into ... Carnitine Palmitoyltransferase 1b Deficient Mice Develop Severe Insulin Resistance After Prolonged High Fat Diet Feeding. ... Citation: Kim T, Moore JF, Sharer JD, Yang K, Wood PA, Yang Q (2014) Carnitine Palmitoyltransferase 1b Deficient Mice Develop ...
https://omicsonline.org/peer-reviewed/carnitine-palmitoyltransferase-1b-deficient-mice-develop-severe-insulin-resistance-after-prolonged-high-fat-diet-feeding-30201.html

*  Carnitine Palmitoyl Transferase 2 Deficiency

... Common Name(s). Carnitine Palmitoyl Transferase 2 Deficiency, Carnitine ... "Carnitine Palmitoyl Transferase 2 Deficiency" (open studies are recruiting volunteers) and 7 "Carnitine Palmitoyl Transferase 2 ... Once inside the carnitine needs to be taken off by the enzyme carnitine palmitoyltransferase II. If there is not enough of this ... Labour management of a woman with carnitine palmitoyl transferase type 2 deficiency. Author(s): P M Slater, R Grivell, A M Cyna ...
diseaseinfosearch.org/Carnitine Palmitoyltransferase Deficiency Type 2/1110

*  Etomoxir-induced partial carnitine palmitoyltransferase-I (CPT-I) inhibition in vivo does not alter cardiac long-chain fatty...

1979) Carnitine palmitoyltransferase II deficiency with normal carnitine palmitoyltransferase I in skeletal muscle and ... Etomoxir-induced partial carnitine palmitoyltransferase-I (CPT-I) inhibition in vivo does not alter cardiac long-chain fatty ... Etomoxir-induced partial carnitine palmitoyltransferase-I (CPT-I) inhibition in vivo does not alter cardiac long-chain fatty ... Etomoxir-induced partial carnitine palmitoyltransferase-I (CPT-I) inhibition in vivo does not alter cardiac long-chain fatty ...
biochemj.org/content/419/2/447

*  Anti-CPT1B antibody (ab15703) | Abcam

Carnitine O palmitoyltransferase I mitochondrial muscle isoform antibody. *Carnitine O palmitoyltransferase I muscle isoform ... Carnitine palmitoyltransferase I like protein antibody. *Carnitine palmitoyltransferase I muscle antibody. *Carnitine ... Carnitine palmitoyltransferase 1A (muscle) antibody. *Carnitine palmitoyltransferase 1B (muscle) antibody. *Carnitine ... Carnitine O-palmitoyltransferase 1, muscle isoform antibody. *Carnitine O-palmitoyltransferase I antibody ...
abcam.com/CPT1B-antibody-ab15703.html

*  Fat depot origin affects fatty acid handling in cultured rat and human preadipocytes.

Carnitine O-Palmitoyltransferase / metabolism. Carrier Proteins / metabolism. Cells, Cultured. Epididymis. Fatty Acid-Binding ... Carnitine palmitoyltransferase 1 activity increased during differentiation and was higher in perirenal than in epididymal ...
biomedsearch.com/nih/Fat-depot-origin-affects-fatty/11158926.html

*  Search for a Test by Disorder | Molecular Genetics Laboratory

Carnitine Palmitoyltransferase deficiency: CPT1A* , CPT2 , MetaboSeq , Test Requisition. *Carnitine-acylcarnitine translocase ( ... Primary carnitine deficiency: SLC22A5 , MetaboSeq , Test Requisition. *Short-chain 3-hydroxyacyl-CoA dehydrogenase (SCHAD) ...
https://cincinnatichildrens.org/service/d/diagnostic-labs/molecular-genetics/test-disorder

*  Rhabdomyolysis - American Family Physician

Carnitine palmitoyltransferase deficiency. Carnitine deficiency. Short-chain and long-chain acyl-coenzyme A dehydrogenase ...
aafp.org/afp/2002/0301/p907.html

*  VLDL and apolipoprotein CIII induce ER stress and inflammation and attenuate insulin signalling via Toll-like receptor 2 in...

Carnitine palmitoyltransferase 1. CHOP. CCAAT-enhancer-binding protein homologous protein. eIF2α. Εukaryotic initiation factor ...
https://link.springer.com/article/10.1007/s00125-017-4401-5

*  Carnitina O-palmitoiltransferasi - Wikipedia

Is overt carnitine palmitoyltransferase of liver peroxisomal carnitine octanoyltransferase?, in Biochem. J., vol. 249, 1988, pp ... Purification and properties of carnitine octanoyltransferase and carnitine palmitoyltransferase from rat liver, in J. Biochem ... Purification and properties of an easily solubilized L-carnitine palmitoyltransferase from beef-liver mitochondria, in Biochem ... La carnitina O-palmitoiltransferasi (numero EC 2.3.1.21) è un enzima appartenente alla classe delle transferasi, che catalizza ...
https://it.wikipedia.org/wiki/Carnitina_O-palmitoiltransferasi

*  The hidden roots of modern day Turkey | Veterans Today

Carnitine Palmitoyltransferase ll Deficiency. Congenital Amegakaryocytic Thrombocytopenia. Congenital Disorder of Glycosylation ...
https://veteranstoday.com/2015/07/30/the-hidden-roots-of-modern-day-turkey/

*  "hsa-mir-5095" related genes - GeneCards Search...

Carnitine Palmitoyltransferase 1A. Protein Coding. 66. GC11M068772. 0.08. 25. USP15 Ubiquitin Specific Peptidase 15. Protein ...
genecards.org/Search/Keyword/?queryString="hsa-mir-5095"

*  KEGG BRITE: KEGG Orthology (KO) - Camelus ferus (Wild Bactrian camel)

... carnitine palmitoyltransferase 1A 102524549 CPT1B; carnitine palmitoyltransferase 1B 102505825 CPT1C; carnitine ... carnitine palmitoyltransferase 1A 102524549 CPT1B; carnitine palmitoyltransferase 1B 102505825 CPT1C; carnitine ... carnitine O-palmitoyltransferase 1, liver isoform [EC:2.3.1.21] K19523 CPT1B; carnitine O-palmitoyltransferase 1, muscle ... carnitine O-palmitoyltransferase 1, liver isoform [EC:2.3.1.21] K19523 CPT1B; carnitine O-palmitoyltransferase 1, muscle ...
genome.jp/kegg-bin/get_htext?cfr00001 102511249

*  Regulation of metabolism by dietary carbohydrates in two lines of rainbow trout divergently selected for muscle fat content |...

Carnitine palmitoyl transferase isoforms a (CPT1a), b (CPT1b), c (CPT1c) and d (CPT1d) and 3-hydroxyacyl-CoA dehydrogenase ( ... and carnitine palmitoyl transferase 1 (CPT1; EC 2.3.1.21) and 3-hydroxyacyl-CoA dehydrogenase (HOAD; EC 1.1.1.35) for fatty ...
jeb.biologists.org/content/215/15/2567.full

*  Human Metabolome Database: Showing metabocard for TG(16:1(9Z)/18:1(9Z)/20:4(5Z,8Z,11Z,14Z)) (HMDB0005441)

Carnitine O-palmitoyltransferase 1, muscle isoform. General function:. Involved in acyltransferase activity. Specific function: ... Carnitine O-palmitoyltransferase 1, liver isoform. General function:. Involved in acyltransferase activity. Specific function: ... Carnitine O-palmitoyltransferase 2, mitochondrial. General function:. Involved in acyltransferase activity. Specific function: ... Catalyzes the transfer of the acyl group of long-chain fatty acid-CoA conjugates onto carnitine, an essential step for the ...
hmdb.ca/metabolites/HMDB05441

*  Human Metabolome Database: Showing metabocard for TG(16:0/16:1(9Z)/18:1(9Z)) (HMDB0005377)

Carnitine O-palmitoyltransferase 1, muscle isoform. General function:. Involved in acyltransferase activity. Specific function: ... Carnitine O-palmitoyltransferase 1, liver isoform. General function:. Involved in acyltransferase activity. Specific function: ... Carnitine O-palmitoyltransferase 2, mitochondrial. General function:. Involved in acyltransferase activity. Specific function: ... Catalyzes the transfer of the acyl group of long-chain fatty acid-CoA conjugates onto carnitine, an essential step for the ...
hmdb.ca/metabolites/HMDB05377

*  International Union of Pharmacology. LXXI. Free Fatty Acid Receptors FFA1, -2, and -3: Pharmacology and Pathophysiological...

2BrP is traditionally described as an inhibitor of carnitine palmitoyltransferase (CPT-1). CPT-1 inhibition leads to a build-up ... carnitine palmitoyltransferase; STZ, streptozotocin; GLP-1, glucagon-like peptide-1; GIP, glucose-dependent insulinotropic ...
pharmrev.aspetjournals.org/content/60/4/405.full

*  KAKEN - Research Projects | Brain type CPT II Deficiency ; CPT II analysis in the brain and its gene mutations. (KAKENHI...

Carnitine palmitoyltransferase II (CPT II) may have three different clinical forms, with 'muscular' and 'hepatic' and 'CNS ' ... Publications] Uemura O.: 'Secondary carnitine palmitoyltransferase deficiency in chronic renal failure and secondary ... Secondary carnitine palmitoyltransferase deficiency in chronic renal failure and secondary hyperparathyroidism.' Tohoku J.Exper ... Publications] Uemura O: 'Secondary cannitine palmitoyltransferase deficiency in chronic renal failure and secondary ...
https://kaken.nii.ac.jp/grant/KAKENHI-PROJECT-07670876/

*  MitoAction | Genetic and Rare Diseases Information Center (GARD) - an NCATS Program

Carnitine palmitoyltransferase 2 deficiency Synonyms: Carnitine palmitoyltransferase deficiency type 2, CPT2, Carnitine ... Carnitine palmitoyl transferase IA deficiency, Hepatic carnitine palmitoyl transferase 1 deficiency, Hepatic carnitine ... Carnitine palmitoyltransferase I deficiency , muscle Synonyms: CPT I, MUSCLE, MCCPT1, KIAA1670, Carnitine palmitoyl transferase ... Carnitine palmitoyl transferase 1 deficiency Synonyms: Carnitine palmitoyltransferase 1A deficiency, CPT1A deficiency, Hepatic ...
https://rarediseases.info.nih.gov/organizations/694

*  Effect of nonsurgical periodontal therapy on serum and gingival crevicular fluid cytokine levels during pregnancy and...

7165725 - Response to starvation of hepatic carnitine palmitoyltransferase activity and its regul.... 10227405 - Trisomy/ ...
biomedsearch.com/nih/Effect-nonsurgical-periodontal-therapy-serum/22835005.html

*  Lin Yang | Sichuan University

Carnitine Palmitoyltransferase 1b Deficiency Protects Mice from Diet-Induced Insulin Resistance. Teayoun Kim, Lan He, Maria S. ... Carnitine Palmitoyltransferase 1b Deficient Mice Develop Severe Insulin Resistance After Prolonged High Fat Diet Feeding. ...
https://omicsonline.org/editor-profile/Lin_Yang/

*  Carnitina palmitoiltransferase II - Wikipedia

Localization of the human gene for carnitine palmitoyltransferase to 1p13-p11 by nonradioactive in situ hybridization». ... A Carnitina O-palmitoiltransferase II, mitocondrial é uma enzima que nos seres humanos é codificada pelo gene CPT2. Minoletti F ...
https://pt.wikipedia.org/wiki/Carnitina_palmitoiltransferase_II

Inborn error of lipid metabolismSystemic primary carnitine deficiencyMiddle ChakavianCarnitine-acylcarnitine translocase deficiency: Carnitine-acylcarnitine translocase deficiency is a rare, autosomal recessive metabolic disorder that prevents the body from converting long-chain fatty acids into energy, particularly during periods without food. Carnitine, a natural substance acquired mostly through the diet, is used by cells to process fats and produce energy.AcetylMalonyl-CoA O-methyltransferase: Malonyl-CoA O-methyltransferase (, BioC) is an enzyme with system name S-adenosyl-L-methionine:malonyl-CoA O-methyltransferase. This enzyme catalyses the following chemical reactionGeoffrey Chang: Geoffrey Chang is a professor at the University of California, San Diego's Skaggs School of Pharmacy and Pharmaceutical Sciences and Department of Pharmacology, School of Medicine. His laboratory focuses on the structural biology of integral membrane proteins, particularly exploring X-ray crystallography techniques for solving the tertiary structures of membrane proteins that are notoriously resistant to crystallization.Palmitoyl-CoABetaine: A betaine (BEET-ah-een, ) in chemistry is any neutral chemical compound with a positively charged cationic functional group such as a quaternary ammonium or phosphonium cation (generally: onium ions) which bears no hydrogen atom and with a negatively charged functional group such as a carboxylate group which may not be adjacent to the cationic site. A betaine thus may be a specific type of zwitterion.Isovaleric acidemiaCubam: Cubam, is the term used to refer to a multi-ligand receptor located in the terminal ileum, specializing in absorption of vitamin B12. Cubam is essentially composed of amnionless (AMN), and cubilin.Epoxidized soybean oilHeptadecanoic acidKetogenesisLiver sinusoid: A liver sinusoid is a type of sinusoidal blood vessel (with fenestrated, discontinuous endothelium) that serves as a location for the oxygen-rich blood from the hepatic artery and the nutrient-rich blood from the portal vein.SIU SOM Histology GIErgothioneineIndian Famine Codes: The Indian Famine Codes, developed by the colonial British in the 1880s, were one of the earliest famine scales. The Famine Codes defined three levels of food insecurity: near-scarcity, scarcity, and famine.Neutral lipid storage disease: Neutral lipid storage disease (also known as Chanarin–Dorfman syndrome) is an autosomal recessive disorder characterized by accumulation of triglycerides in the cytoplasm of leukocytes, muscle, liver, fibroblasts, and other tissues.Freedberg, et al.

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

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)

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

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)

(3/672) 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.

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)

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

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)

(5/672) 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.

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)

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

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)

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

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)

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

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)



choline acetyltransferase family


  • Belongs to the carnitine/choline acetyltransferase family. (abcam.com)
  • 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. (genecards.org)

muscle isoform


  • Carnitine palmitoyltransferase 1 activity increased during differentiation and was higher in perirenal than in epididymal preadipocytes, particularly the muscle isoform. (biomedsearch.com)

rate-limiti


  • Carnitine palmitoyltransferase 1 (CPT1) is the rate-limiting enzyme governing the entry of longchain acyl-CoAs into mitochondria. (omicsonline.org)

Protein Coding


  • CPT1B (Carnitine Palmitoyltransferase 1B) is a Protein Coding gene. (genecards.org)

Deficiency


  • Carnitine palmitoyltransferase type II deficiency (CPT-II) is a rare genetic condition. (diseaseinfosearch.org)
  • Following organizations serve the condition "Carnitine Palmitoyl Transferase 2 Deficiency" for support, advocacy or research. (diseaseinfosearch.org)

enzyme


  • Once inside the carnitine needs to be taken off by the enzyme carnitine palmitoyltransferase II. (diseaseinfosearch.org)

activity


  • GO annotations related to this gene include transferase activity, transferring acyl groups and carnitine O-palmitoyltransferase activity . (genecards.org)