Skip to main content
NCBI home page
Biochemical Journal logoLink to Biochemical Journal
. 1991 May 1;275(Pt 3):685–688. doi: 10.1042/bj2750685

Carnitine palmitoyltransferase in human erythrocyte membrane. Properties and malonyl-CoA sensitivity.

R R Ramsay 1, G Mancinelli 1, A Arduini 1
PMCID: PMC1150109  PMID: 2039446

Abstract

Carnitine palmitoyltransferase located in the erythrocyte plasma membrane is sensitive to inhibition by malonyl-CoA and 2-bromopalmitoyl-CoA plus carnitine. Although this inhibition and other properties suggest similarities to the intracellular enzymes in other tissues, no cross-reaction was observed with antisera to the peroxisomal or to the mitochondrial inner-membrane enzyme. The activity was solubilized by and was stable in Triton X-100, which destroys the enzymes found in microsomes and in the mitochondrial outer membrane. The substrate specificity is broader than for the intracellular enzymes, the activities with stearoyl-CoA (114%) and arachidonoyl-CoA (97%) being equal to that with palmitoyl-CoA, and the activities with linoleoyl-CoA (44%) and erucoyl-CoA (46%) about half that with palmitoyl-CoA. The function of this carnitine palmitoyltransferase is probably to buffer the acyl-CoA present in the erythrocyte for turnover of the fatty acyl groups of the membrane lipids.

Full text

PDF
685

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Arduini A., Mancinelli G., Ramsay R. R. Palmitoyl-L-carnitine, a metabolic intermediate of the fatty acid incorporation pathway in erythrocyte membrane phospholipids. Biochem Biophys Res Commun. 1990 Nov 30;173(1):212–217. doi: 10.1016/s0006-291x(05)81043-5. [DOI] [PubMed] [Google Scholar]
  2. Bieber L. L. Carnitine. Annu Rev Biochem. 1988;57:261–283. doi: 10.1146/annurev.bi.57.070188.001401. [DOI] [PubMed] [Google Scholar]
  3. Bird M. I., Saggerson E. D. Binding of malonyl-CoA to isolated mitochondria. Evidence for high- and low-affinity sites in liver and heart and relationship to inhibition of carnitine palmitoyltransferase activity. Biochem J. 1984 Sep 15;222(3):639–647. doi: 10.1042/bj2220639. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72:248–254. doi: 10.1016/0003-2697(76)90527-3. [DOI] [PubMed] [Google Scholar]
  5. Cooper M. B., Forte C. A., Jones D. A. Carnitine and acetylcarnitine in red blood cells. Biochim Biophys Acta. 1988 Mar 25;959(2):100–105. doi: 10.1016/0005-2760(88)90020-3. [DOI] [PubMed] [Google Scholar]
  6. Declercq P. E., Falck J. R., Kuwajima M., Tyminski H., Foster D. W., McGarry J. D. Characterization of the mitochondrial carnitine palmitoyltransferase enzyme system. I. Use of inhibitors. J Biol Chem. 1987 Jul 15;262(20):9812–9821. [PubMed] [Google Scholar]
  7. Derrick J. P., Ramsay R. R. L-carnitine acyltransferase in intact peroxisomes is inhibited by malonyl-CoA. Biochem J. 1989 Sep 15;262(3):801–806. doi: 10.1042/bj2620801. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. FRITZ I. B. CARNITINE AND ITS ROLE IN FATTY ACID METABOLISM. Adv Lipid Res. 1963;1:285–334. [PubMed] [Google Scholar]
  9. Lilly K., Bugaisky G. E., Umeda P. K., Bieber L. L. The medium-chain carnitine acyltransferase activity associated with rat liver microsomes is malonyl-CoA sensitive. Arch Biochem Biophys. 1990 Jul;280(1):167–174. doi: 10.1016/0003-9861(90)90532-4. [DOI] [PubMed] [Google Scholar]
  10. McGarry J. D., Foster D. W. Regulation of hepatic fatty acid oxidation and ketone body production. Annu Rev Biochem. 1980;49:395–420. doi: 10.1146/annurev.bi.49.070180.002143. [DOI] [PubMed] [Google Scholar]
  11. Murthy M. S., Pande S. V. Characterization of a solubilized malonyl-CoA-sensitive carnitine palmitoyltransferase from the mitochondrial outer membrane as a protein distinct from the malonyl-CoA-insensitive carnitine palmitoyltransferase of the inner membrane. Biochem J. 1990 Jun 15;268(3):599–604. doi: 10.1042/bj2680599. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Murthy M. S., Pande S. V. Some differences in the properties of carnitine palmitoyltransferase activities of the mitochondrial outer and inner membranes. Biochem J. 1987 Dec 15;248(3):727–733. doi: 10.1042/bj2480727. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Pande S. V. A mitochondrial carnitine acylcarnitine translocase system. Proc Natl Acad Sci U S A. 1975 Mar;72(3):883–887. doi: 10.1073/pnas.72.3.883. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Ramsay R. R., Derrick J. P., Friend A. S., Tubbs P. K. Purification and properties of the soluble carnitine palmitoyltransferase from bovine liver mitochondria. Biochem J. 1987 Jun 1;244(2):271–278. doi: 10.1042/bj2440271. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Ramsay R. R. The soluble carnitine palmitoyltransferase from bovine liver. A comparison with the enzymes from peroxisomes and from the mitochondrial inner membrane. Biochem J. 1988 Jan 1;249(1):239–245. doi: 10.1042/bj2490239. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Ramsay R. R., Tubbs P. K. The mechanism of fatty acid uptake by heart mitochondria: an acylcarnitine-carnitine exchange. FEBS Lett. 1975 Jun 1;54(1):21–25. doi: 10.1016/0014-5793(75)81059-3. [DOI] [PubMed] [Google Scholar]
  17. Singh R., Shepherd I. M., Derrick J. P., Ramsay R. R., Sherratt H. S., Turnbull D. M. A case of carnitine palmitoyltransferase II deficiency in human skeletal muscle. FEBS Lett. 1988 Dec 5;241(1-2):126–130. doi: 10.1016/0014-5793(88)81044-5. [DOI] [PubMed] [Google Scholar]
  18. Tyler J. M., Hargreaves W. R., Branton D. Purification of two spectrin-binding proteins: biochemical and electron microscopic evidence for site-specific reassociation between spectrin and bands 2.1 and 4.1. Proc Natl Acad Sci U S A. 1979 Oct;76(10):5192–5196. doi: 10.1073/pnas.76.10.5192. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. West D. W., Chase J. F., Tubbs P. K. The separation and properties of two forms of carnitine palmitoyltransferase from ox liver mitochondria. Biochem Biophys Res Commun. 1971 Mar 5;42(5):912–918. doi: 10.1016/0006-291x(71)90517-1. [DOI] [PubMed] [Google Scholar]
  20. Wittels B., Hochstein P. The identification of carnitine palmityltransferase in erythrocyte membranes. J Biol Chem. 1967 Jan 10;242(1):126–130. [PubMed] [Google Scholar]
  21. Woeltje K. F., Kuwajima M., Foster D. W., McGarry J. D. Characterization of the mitochondrial carnitine palmitoyltransferase enzyme system. II. Use of detergents and antibodies. J Biol Chem. 1987 Jul 15;262(20):9822–9827. [PubMed] [Google Scholar]
  22. Zammit V. A., Corstorphine C. G., Kolodziej M. P. Target size analysis by radiation inactivation of carnitine palmitoyltransferase activity and malonyl-CoA binding in outer membranes from rat liver mitochondria. Biochem J. 1989 Oct 1;263(1):89–95. doi: 10.1042/bj2630089. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES