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Cpt1b  -  carnitine palmitoyltransferase 1b, muscle

Rattus norvegicus

Synonyms: CPT I, CPT-IB, CPT1-M, CPTI-M, Carnitine O-palmitoyltransferase 1, muscle isoform, ...
 
 
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Disease relevance of Cpt1b

  • CONCLUSION: The selective uptake of FOP by liver and the high sensitivity of hepatic FOP DV to changes of HMFAO with CPT-I inhibition and hypoxia suggests potential usefulness for the 3-oxa fatty acid analog in assessments of hepatic mitochondrial oxidation of exogenous fatty acids with PET [1].
  • As one of the strongest specific inhibitors of CPT-I, HPC is a potential therapeutic agent in myocardial ischemia and Type II diabetes [2].
  • These data suggest that ESP 55016-CoA favorably alters lipid metabolism in a model of diabetic dyslipidemia in part by initially inhibiting fatty acid and sterol synthesis plus enhancing the oxidation of fatty acids through the ACC/malonyl-CoA/CPT-I regulatory axis [3].
  • Thus, the high CPT-I activity displayed by hepatoma cells may be reached by hepatocytes upon challenge to okadaic acid [4].
  • It is concluded that CPT-I may play a role in the generation of the ethanol-induced fatty liver [5].
 

High impact information on Cpt1b

  • The mRNA contents for genes associated with transcriptional activation [c-fos, c-jun, JunB, nuclear respiratory factor 1 (NRF-1)], mitochondrial proliferation [cytochrome c (Cyt c), cytochrome oxidase], and mitochondrial differentiation [carnitine palmitoyltransferase I (CPT-I) isoforms] were measured [6].
  • Carnitine palmitoyltransferase I (CPT-I) catalyzes the transfer of long chain fatty acyl groups from CoA to carnitine for translocation across the mitochondrial inner membrane [7].
  • The mechanism of malonyl-CoA-independent acute control of hepatic carnitine palmitoyltransferase I (CPT-I) activity was investigated [8].
  • (i) Very mild treatment of permeabilized hepatocytes with trypsin produced around 50% stimulation of CPT-I activity [8].
  • (iii) CPT-I activity in isolated mitochondria was depressed in a dose-dependent fashion by the addition of a total cytoskeleton fraction and a cytokeratin-enriched cytoskeletal fraction, the latter being 3 times more potent than the former [8].
 

Chemical compound and disease context of Cpt1b

 

Biological context of Cpt1b

 

Anatomical context of Cpt1b

  • CPT-IA and CPT-IB are isoforms of carnitine palmitoyltransferase I, of which CPT-IA is expressed in liver, kidney, fibroblasts, and heart and CPT-IB is expressed in skeletal muscle, heart, brown and white adipocytes, and testes [11].
  • In a first series of experiments, the possible involvement of the cytoskeleton in the control of CPT-I activity was studied [8].
  • Myocyte contractile capacity is associated with increased expression of the muscle carnitine palmitoyltransferase (CPT-I) isoform as measured by Northern analysis, immunoblotting, and altered sensitivity of CPT-I activity to malonyl-CoA in the stimulated cells [12].
  • The data suggest that a switch from the liver isoform of CPT-I, prominent in the neonatal rat heart, to the muscle CPT-I which predominates in adult rat heart, takes place in the neonatal cardiac myocytes over the same time period as the hypertrophic-mediated changes in myofibrillar assembly and increased contractile activity [12].
  • (ii) Incubation of intact hepatocytes with 3, 3'-iminodipropionitrile, a disruptor of intermediate filaments, increased CPT-I activity in a non-additive manner with respect to OA [8].
 

Associations of Cpt1b with chemical compounds

 

Analytical, diagnostic and therapeutic context of Cpt1b

  • CPT-I from astrocytes was sensitive to malonyl-CoA (IC50 = 3.4 +/- 0.8 microM) and cross-reacted on western blots with an antibody raised against liver CPT-I [14].
  • The effects of prolonged ethanol feeding on the regulatory properties of both hepatic fatty acid oxidation and carnitine palmitoyltransferase I activity (CPT-I) were studied in rats fed a high-fat diet containing 36% of total calories as ethanol (ethanol group) or an isocaloric amount of carbohydrate (control group) [16].
  • These alterations in the properties of hepatic CPT-I may be involved in the appearance of hyperketonemia in the rat pup upon maternal administration of low-protein diets [17].
  • The mitochondrial CPT-I activity in the remnant liver decreased significantly 24 hr after partial hepatectomy [18].
  • Northern blotting did not reveal any change in the relative abundance of mRNA for the liver vs. the muscle CPT-I isoforms [19].

References

  1. Preliminary evaluation of 15-[18F]fluoro-3-oxa-pentadecanoate as a PET tracer of hepatic fatty acid oxidation. DeGrado, T.R., Wang, S., Rockey, D.C. J. Nucl. Med. (2000) [Pubmed]
  2. (+)-Hemipalmitoylcarnitinium strongly inhibits carnitine palmitoyltransferase-I in intact mitochondria. Gandour, R.D., Leung, O.T., Greway, A.T., Ramsay, R.R., Nic a'Bháird, N., Fronczek, F.R., Bellard, B.M., Kumaravel, G. J. Med. Chem. (1993) [Pubmed]
  3. Effects of a novel dual lipid synthesis inhibitor and its potential utility in treating dyslipidemia and metabolic syndrome. Cramer, C.T., Goetz, B., Hopson, K.L., Fici, G.J., Ackermann, R.M., Brown, S.C., Bisgaier, C.L., Rajeswaran, W.G., Oniciu, D.C., Pape, M.E. J. Lipid Res. (2004) [Pubmed]
  4. Loss of response of carnitine palmitoyltransferase I to okadaic acid in transformed hepatic cells. Velasco, G., Passilly, P., Guzmán, M., Latruffe, N. Biochem. Pharmacol. (1998) [Pubmed]
  5. Effects of ethanol feeding on the activity and regulation of hepatic carnitine palmitoyltransferase I. Guzmán, M., Geelen, M.J. Arch. Biochem. Biophys. (1988) [Pubmed]
  6. Electrical stimulation of neonatal cardiomyocytes results in the sequential activation of nuclear genes governing mitochondrial proliferation and differentiation. Xia, Y., Buja, L.M., Scarpulla, R.C., McMillin, J.B. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  7. Thyroid hormone regulates carnitine palmitoyltransferase Ialpha gene expression through elements in the promoter and first intron. Jansen, M.S., Cook, G.A., Song, S., Park, E.A. J. Biol. Chem. (2000) [Pubmed]
  8. Malonyl-CoA-independent acute control of hepatic carnitine palmitoyltransferase I activity. Role of Ca2+/calmodulin-dependent protein kinase II and cytoskeletal components. Velasco, G., Geelen, M.J., del Pulgar, T.G., Guzmán, M. J. Biol. Chem. (1998) [Pubmed]
  9. Beta-receptor blockade decreases carnitine palmitoyl transferase I activity in dogs with heart failure. Panchal, A.R., Stanley, W.C., Kerner, J., Sabbah, H.N. J. Card. Fail. (1998) [Pubmed]
  10. Acylcarnitine accumulation does not correlate with reperfusion recovery in palmitate-perfused rat hearts. Madden, M.C., Wołkowicz, P.E., Pohost, G.M., McMillin, J.B., Pike, M.M. Am. J. Physiol. (1995) [Pubmed]
  11. Genomic DNA sequence, promoter expression, and chromosomal mapping of rat muscle carnitine palmitoyltransferase I. Wang, D., Harrison, W., Buja, L.M., Elder, F.F., McMillin, J.B. Genomics (1998) [Pubmed]
  12. Change in expression of heart carnitine palmitoyltransferase I isoforms with electrical stimulation of cultured rat neonatal cardiac myocytes. Xia, Y., Buja, L.M., McMillin, J.B. J. Biol. Chem. (1996) [Pubmed]
  13. The stimulation of ketogenesis by cannabinoids in cultured astrocytes defines carnitine palmitoyltransferase I as a new ceramide-activated enzyme. Blázquez, C., Sánchez, C., Daza, A., Galve-Roperh, I., Guzmán, M. J. Neurochem. (1999) [Pubmed]
  14. Role of carnitine palmitoyltransferase I in the control of ketogenesis in primary cultures of rat astrocytes. Blázquez, C., Sánchez, C., Velasco, G., Guzmán, M. J. Neurochem. (1998) [Pubmed]
  15. Insulin regulates enzyme activity, malonyl-CoA sensitivity and mRNA abundance of hepatic carnitine palmitoyltransferase-I. Park, E.A., Mynatt, R.L., Cook, G.A., Kashfi, K. Biochem. J. (1995) [Pubmed]
  16. Alterations in the regulatory properties of hepatic fatty acid oxidation and carnitine palmitoyltransferase I activity after ethanol feeding and withdrawal. Guzmán, M., Castro, J. Alcohol. Clin. Exp. Res. (1990) [Pubmed]
  17. Pre- and postnatal protein undernutrition increases hepatic carnitine palmitoyltransferase I activity and decreases enzyme sensitivity to inhibitors in the suckling rat. Guzmán, M., Azzolin, I.R., Moulin, C.C., Perry, M.L. Horm. Metab. Res. (1992) [Pubmed]
  18. Alterations of remnant liver carnitine palmitoyltransferase I activity and serum carnitine concentration after partial hepatectomy in rats. Lai, H.S., Chen, W.J. J. Surg. Res. (1995) [Pubmed]
  19. The liver isoform of carnitine palmitoyltransferase I is activated in neonatal rat cardiac myocytes by hypoxia. Wang, D., Xia, Y., Buja, L.M., McMillin, J.B. Mol. Cell. Biochem. (1998) [Pubmed]
 
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