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CPT1B  -  carnitine palmitoyltransferase 1B (muscle)

Homo sapiens

 
 
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Disease relevance of CPT1B

 

Psychiatry related information on CPT1B

  • If (1) is the case, the phenotypic effects of M-CPT1 deficiency have to be studied in order to generate criteria for clinical decision making and diagnosis [5].
 

High impact information on CPT1B

  • Structural and functional genomics of the CPT1B gene for muscle-type carnitine palmitoyltransferase I in mammals [6].
  • Muscle-type carnitine palmitoyltransferase I (M-CPT I) is a key enzyme in the control of beta-oxidation of long-chain fatty acids in the heart and skeletal muscle [6].
  • Therefore, the involvement of splice variation of M-CPT I in the modulation of malonyl-CoA inhibition of fatty acid oxidation may be less relevant than hitherto assumed [6].
  • Because knowledge of the mammalian genes encoding M-CPT I may aid in studies of disturbed energy metabolism, we obtained new genomic and cDNA data for M-CPT I for the human, mouse, rat, and sheep [6].
  • To explore the gene regulatory mechanisms involved in the metabolic control of cardiac fatty acid oxidative flux, the expression of muscle-type carnitine palmitoyltransferase I (M-CPT I) was characterized in primary cardiac myocytes in culture following exposure to the long-chain mono-unsaturated fatty acid, oleate [7].
 

Biological context of CPT1B

 

Anatomical context of CPT1B

  • In particular, ovine CPT1B mRNA was less tissue restricted, and the predominant transcript in the pancreas was CPT1B [8].
  • Quantitative real time PCR showed that levels of mRNA in blood cells correlated significantly (CPT1B: P< 0.001) with those in muscle tissue from the same donors [10].
  • Finally, CPT1-B mRNA was also stimulated after PPAR agonist treatment, and this likely takes part in drug-induced increase of FAO in control muscle cells [11].
  • In neonatal rat cardiac myocytes, expression of the FAO enzymes MCAD and M-CPT I was induced by treatment with the specific PPARalpha agonist WY-14643 [12].
  • In phenylephrine (PE)-precontracted rat aortic rings with intact endothelium, MCPT caused a concentration-dependent relaxation, which was inhibited by endothelium removed [13].
 

Associations of CPT1B with chemical compounds

  • Furthermore, on analysis of the 5'-flanking region, a putative gene encoding a 'choline kinase homologue' was found to be located only about 300 bp upstream from exon 1A of the human CPTI-M gene [14].
  • Oleate induced steady-state levels of M-CPT I mRNA 4.5-fold [7].
  • The vasorelaxant effects of MCPT together with IBMX (0.5 microM) had an additive action [13].
  • Endothelium-dependent and -independent vasorelaxation by a theophylline derivative MCPT: roles of cyclic nucleotides, potassium channel opening and phosphodiesterase inhibition [13].
  • The vasorelaxation activities of MCPT, a newly synthesized xanthine derivative, were investigated in this study [13].
 

Other interactions of CPT1B

  • Only from two of these genes (CPT1B and CPT2) have full genomic structures been described [15].
  • In the cases of KIAA1670 and KIAA1672, these single cDNA sequences covered two separately annotated transcribed regions [16].
  • For example, the sequence of a clone for KIAA1670 indicated that the CHKL and CPT1B genes were co-transcribed as a contiguous transcript without making both the protein-coding regions fused [16].
  • Western analysis showed a protein that was 6 kDa smaller than predicted, which is consistent with previous results for the native M-CPT I [17].

References

  1. Variants within the muscle and liver isoforms of the carnitine palmitoyltransferase I (CPT1) gene interact with fat intake to modulate indices of obesity in French-Canadians. Robitaille, J., Houde, A., Lemieux, S., Pérusse, L., Gaudet, D., Vohl, M.C. J. Mol. Med. (2007) [Pubmed]
  2. Localization and intron usage analysis of the human CPT1B gene for muscle type carnitine palmitoyltransferase I. van der Leij, F.R., Takens, J., van der Veen, A.Y., Terpstra, P., Kuipers, J.R. Biochim. Biophys. Acta (1997) [Pubmed]
  3. Clinical varieties of carnitine and carnitine palmitoyltransferase deficiency. Angelini, C., Trevisan, C., Isaya, G., Pegolo, G., Vergani, L. Clin. Biochem. (1987) [Pubmed]
  4. Further lowering of muscle lipid oxidative capacity in obese subjects after biliopancreatic diversion. Fabris, R., Mingrone, G., Milan, G., Manco, M., Granzotto, M., Dalla Pozza, A., Scarda, A., Serra, R., Greco, A.V., Federspil, G., Vettor, R. J. Clin. Endocrinol. Metab. (2004) [Pubmed]
  5. Rationale for a conditional knockout mouse model to study carnitine palmitoyltransferase I deficiencies. van der Leij, F.R., Drijfholt, A., Kuipers, J.R. Adv. Exp. Med. Biol. (1999) [Pubmed]
  6. Structural and functional genomics of the CPT1B gene for muscle-type carnitine palmitoyltransferase I in mammals. van der Leij, F.R., Cox, K.B., Jackson, V.N., Huijkman, N.C., Bartelds, B., Kuipers, J.R., Dijkhuizen, T., Terpstra, P., Wood, P.A., Zammit, V.A., Price, N.T. J. Biol. Chem. (2002) [Pubmed]
  7. Fatty acids activate transcription of the muscle carnitine palmitoyltransferase I gene in cardiac myocytes via the peroxisome proliferator-activated receptor alpha. Brandt, J.M., Djouadi, F., Kelly, D.P. J. Biol. Chem. (1998) [Pubmed]
  8. Cloning and expression of the liver and muscle isoforms of ovine carnitine palmitoyltransferase 1: residues within the N-terminus of the muscle isoform influence the kinetic properties of the enzyme. Price, N.T., Jackson, V.N., van der Leij, F.R., Cameron, J.M., Travers, M.T., Bartelds, B., Huijkman, N.C., Zammit, V.A. Biochem. J. (2003) [Pubmed]
  9. Fine chromosome mapping of the genes for human liver and muscle carnitine palmitoyltransferase I (CPT1A and CPT1B). Britton, C.H., Mackey, D.W., Esser, V., Foster, D.W., Burns, D.K., Yarnall, D.P., Froguel, P., McGarry, J.D. Genomics (1997) [Pubmed]
  10. Do blood cells mimic gene expression profile alterations known to occur in muscular adaptation to endurance training? Zeibig, J., Karlic, H., Lohninger, A., Damsgaard, R., Dumsgaard, R., Smekal, G. Eur. J. Appl. Physiol. (2005) [Pubmed]
  11. Peroxisome proliferator activated receptor delta (PPARdelta) agonist but not PPARalpha corrects carnitine palmitoyl transferase 2 deficiency in human muscle cells. Djouadi, F., Aubey, F., Schlemmer, D., Bastin, J. J. Clin. Endocrinol. Metab. (2005) [Pubmed]
  12. Effects of insulin-like growth factor-I on the maturation of metabolism in neonatal rat cardiomyocytes. Montessuit, C., Palma, T., Viglino, C., Pellieux, C., Lerch, R. Pflugers Arch. (2006) [Pubmed]
  13. Endothelium-dependent and -independent vasorelaxation by a theophylline derivative MCPT: roles of cyclic nucleotides, potassium channel opening and phosphodiesterase inhibition. Lo, Y.C., Tsou, H.H., Lin, R.J., Wu, D.C., Wu, B.N., Lin, Y.T., Chen, I.J. Life Sci. (2005) [Pubmed]
  14. Structural features of the gene encoding human muscle type carnitine palmitoyltransferase I. Yamazaki, N., Yamanaka, Y., Hashimoto, Y., Shinohara, Y., Shima, A., Terada, H. FEBS Lett. (1997) [Pubmed]
  15. Genomics of the human carnitine acyltransferase genes. van der Leij, F.R., Huijkman, N.C., Boomsma, C., Kuipers, J.R., Bartelds, B. Mol. Genet. Metab. (2000) [Pubmed]
  16. Identification of novel transcribed sequences on human chromosome 22 by expressed sequence tag mapping. Hirosawa, M., Nagase, T., Murahashi, Y., Kikuno, R., Ohara, O. DNA Res. (2001) [Pubmed]
  17. Cytological evidence that the C-terminus of carnitine palmitoyltransferase I is on the cytosolic face of the mitochondrial outer membrane. van der Leij, F.R., Kram, A.M., Bartelds, B., Roelofsen, H., Smid, G.B., Takens, J., Zammit, V.A., Kuipers, J.R. Biochem. J. (1999) [Pubmed]
 
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