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. 1995 Mar 15;306(Pt 3):793–799. doi: 10.1042/bj3060793

Detection of acyl-CoA-binding protein in human red blood cells and investigation of its role in membrane phospholipid renewal.

H Fyrst 1, J Knudsen 1, M A Schott 1, B H Lubin 1, F A Kuypers 1
PMCID: PMC1136591  PMID: 7702576

Abstract

Acyl-CoA-binding protein (ACBP) has been identified in a number of tissues and shown to affect the intracellular distribution and utilization of acyl-CoA. We have detected ACBP in the cytosol but not the membrane of human red blood cells and, using an e.l.i.s.a. with antibodies prepared against human liver ACBP, found that its concentration was 0.5 microM. To investigate the role of ACBP in human red blood cells, we added purified human liver ACBP and radiolabelled acyl-CoA to isolated membranes from these cells. ACBP prevented high concentrations of acyl-CoA from binding to the membrane but could not keep the acyl-CoA in the aqueous phase at low concentrations. This suggested the presence of a pool in the membrane with a binding affinity for acyl-CoA that was greater than that of ACBP for acyl-CoA. In the presence of lysophospholipid, this membrane-bound pool of acyl-CoA was rapidly used as a substrate by acyl-CoA:lysophospholipid acyltransferase (LAT) to generate phospholipid from lysophospholipid. We also found that ACBP-bound acyl-CoA was preferred over free acyl-CoA as a substrate by LAT. These results are the first documentation that human red blood cells contain ACBP and that this protein can affect the utilization of acyl-CoA in plasma membranes of these cells. The interactions between acyl-CoA, ACBP and the membrane suggest that there are several pools of acyl-CoA in the human red blood cell and that ACBP may have a role in regulating their distribution and fate.

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Selected References

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  1. BLIGH E. G., DYER W. J. A rapid method of total lipid extraction and purification. Can J Biochem Physiol. 1959 Aug;37(8):911–917. doi: 10.1139/o59-099. [DOI] [PubMed] [Google Scholar]
  2. Beutler E., West C., Blume K. G. The removal of leukocytes and platelets from whole blood. J Lab Clin Med. 1976 Aug;88(2):328–333. [PubMed] [Google Scholar]
  3. 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]
  4. Christensen H. N. Is PQQ a significant nutrient in addition to its role as a therapeutic agent in the higher animal? Nutr Rev. 1994 Jan;52(1):24–25. doi: 10.1111/j.1753-4887.1994.tb01351.x. [DOI] [PubMed] [Google Scholar]
  5. DODGE J. T., MITCHELL C., HANAHAN D. J. The preparation and chemical characteristics of hemoglobin-free ghosts of human erythrocytes. Arch Biochem Biophys. 1963 Jan;100:119–130. doi: 10.1016/0003-9861(63)90042-0. [DOI] [PubMed] [Google Scholar]
  6. Davidson B. C., Cantrill R. C. Erythrocyte membrane acyl:CoA synthetase activity. FEBS Lett. 1985 Nov 25;193(1):69–74. doi: 10.1016/0014-5793(85)80081-8. [DOI] [PubMed] [Google Scholar]
  7. Haunerland N., Jagschies G., Schulenberg H., Spener F. Fatty-acid-binding proteins. Occurrence of two fatty-acid-binding proteins in bovine liver cytosol and their binding of fatty acids, cholesterol, and other lipophilic ligands. Hoppe Seylers Z Physiol Chem. 1984 Mar;365(3):365–376. doi: 10.1515/bchm2.1984.365.1.365. [DOI] [PubMed] [Google Scholar]
  8. Hornberger W., Patscheke H. Primary stimuli of icosanoid release inhibit arachidonoyl-CoA synthetase and lysophospholipid acyltransferase. Mechanism of action of hydrogen peroxide and methyl mercury in platelets. Eur J Biochem. 1990 Jan 12;187(1):175–181. doi: 10.1111/j.1432-1033.1990.tb15292.x. [DOI] [PubMed] [Google Scholar]
  9. Knudsen J. Acyl-CoA-binding and transport, an alternative function for diazepam binding inhibitor (DBI), which is identical with acyl-CoA-binding protein. Neuropharmacology. 1991 Dec;30(12B):1405–1410. doi: 10.1016/s0028-3908(11)80009-2. [DOI] [PubMed] [Google Scholar]
  10. Knudsen J., Faergeman N. J., Skøtt H., Hummel R., Børsting C., Rose T. M., Andersen J. S., Højrup P., Roepstorff P., Kristiansen K. Yeast acyl-CoA-binding protein: acyl-CoA-binding affinity and effect on intracellular acyl-CoA pool size. Biochem J. 1994 Sep 1;302(Pt 2):479–485. doi: 10.1042/bj3020479. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Knudsen J., Højrup P., Hansen H. O., Hansen H. F., Roepstorff P. Acyl-CoA-binding protein in the rat. Purification, binding characteristics, tissue concentrations and amino acid sequence. Biochem J. 1989 Sep 1;262(2):513–519. doi: 10.1042/bj2620513. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. LANDS W. E. LIPID METABOLISM. Annu Rev Biochem. 1965;34:313–346. doi: 10.1146/annurev.bi.34.070165.001525. [DOI] [PubMed] [Google Scholar]
  13. LANDS W. E. Metabolism of glycerolipids. 2. The enzymatic acylation of lysolecithin. J Biol Chem. 1960 Aug;235:2233–2237. [PubMed] [Google Scholar]
  14. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  15. Lucas A. H., Granoff D. M. A major crossreactive idiotype associated with human antibodies to the Haemophilus influenzae b polysaccharide. Expression in relation to age and immunoglobulin G subclass. J Clin Invest. 1990 Apr;85(4):1158–1166. doi: 10.1172/JCI114548. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Mandrup S., Andreasen P. H., Knudsen J., Kristiansen K. Genome organization and expression of the rat ACBP gene family. Mol Cell Biochem. 1993 Jun 9;123(1-2):55–61. doi: 10.1007/BF01076475. [DOI] [PubMed] [Google Scholar]
  17. Mandrup S., Hummel R., Ravn S., Jensen G., Andreasen P. H., Gregersen N., Knudsen J., Kristiansen K. Acyl-CoA-binding protein/diazepam-binding inhibitor gene and pseudogenes. A typical housekeeping gene family. J Mol Biol. 1992 Dec 5;228(3):1011–1022. doi: 10.1016/0022-2836(92)90888-q. [DOI] [PubMed] [Google Scholar]
  18. Mandrup S., Jepsen R., Skøtt H., Rosendal J., Højrup P., Kristiansen K., Knudsen J. Effect of heterologous expression of acyl-CoA-binding protein on acyl-CoA level and composition in yeast. Biochem J. 1993 Mar 1;290(Pt 2):369–374. doi: 10.1042/bj2900369. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Mikkelsen J., Knudsen J. Acyl-CoA-binding protein from cow. Binding characteristics and cellular and tissue distribution. Biochem J. 1987 Dec 15;248(3):709–714. doi: 10.1042/bj2480709. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Mogensen I. B., Schulenberg H., Hansen H. O., Spener F., Knudsen J. A novel acyl-CoA-binding protein from bovine liver. Effect on fatty acid synthesis. Biochem J. 1987 Jan 1;241(1):189–192. doi: 10.1042/bj2410189. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Pawlak J., Smith S. Evaluation of thioesterase II as a serum marker for rat mammary cancer. Cancer Res. 1986 Sep;46(9):4712–4719. [PubMed] [Google Scholar]
  22. ROBERTSON A. F., LANDS W. E. METABOLISM OF PHOSPHOLIPIDS IN NORMAL AND SPHEROCYTIC HUMAN ERYTHROCYTES. J Lipid Res. 1964 Jan;5:88–93. [PubMed] [Google Scholar]
  23. Rasmussen J. T., Börchers T., Knudsen J. Comparison of the binding affinities of acyl-CoA-binding protein and fatty-acid-binding protein for long-chain acyl-CoA esters. Biochem J. 1990 Feb 1;265(3):849–855. doi: 10.1042/bj2650849. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Rasmussen J. T., Faergeman N. J., Kristiansen K., Knudsen J. Acyl-CoA-binding protein (ACBP) can mediate intermembrane acyl-CoA transport and donate acyl-CoA for beta-oxidation and glycerolipid synthesis. Biochem J. 1994 Apr 1;299(Pt 1):165–170. doi: 10.1042/bj2990165. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Rasmussen J. T., Rosendal J., Knudsen J. Interaction of acyl-CoA binding protein (ACBP) on processes for which acyl-CoA is a substrate, product or inhibitor. Biochem J. 1993 Jun 15;292(Pt 3):907–913. doi: 10.1042/bj2920907. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Rosendal J., Ertbjerg P., Knudsen J. Characterization of ligand binding to acyl-CoA-binding protein. Biochem J. 1993 Mar 1;290(Pt 2):321–326. doi: 10.1042/bj2900321. [DOI] [PMC free article] [PubMed] [Google Scholar]

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