J. Biol. Chem., Vol. 263, Issue 27, 13615-13622, 09, 1988

Fatty acids covalently bound to erythrocyte proteins undergo a differential turnover in vivo

M Staufenbiel
Max-Planck-Institut fur Zellbiologie, Abteilung Traub, Ladenburg/Heidelberg, Federal Republic of Germany.

Recently, covalently bound fatty acids have been identified on a variety of proteins. Many of these acyl proteins are physiologically important, and the lipid modification often appears to be essential for their function. In this investigation mature erythrocytes have been used to study in detail the metabolic behavior of protein-bound fatty acids. Although deficient in protein synthesis, these cells are still able to covalently attach [3H]palmitic acid to proteins located at the plasma membrane and its associated cytoskeleton. Linkage analyses demonstrated that the labeled polypeptides contained ester- or thioester-bound fatty acids. The covalent binding of fatty acid was rapidly reversible. Half-lives of the protein-bound fatty acid molecules ranged from less than 30 min to more than 3 h. The deacylation reaction was not due to a chemically labile linkage of protein and fatty acid but appeared to be physiologically induced. Differences in the fatty acid turnover rates between the acyl proteins suggested an independent regulation of their lipid turnover. A number of proteins underwent dynamic fatty acid acylation, indicating that palmitylated proteins undergoing fatty acid turnover are not a rare exception.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				U. E. Petaja-Repo, M. Hogue, T. T. Leskela, P. M. H. Markkanen, J. T. Tuusa, and M. Bouvier Distinct Subcellular Localization for Constitutive and Agonist-modulated Palmitoylation of the Human {delta} Opioid Receptor J. Biol. Chem., June 9, 2006; 281(23): 15780 - 15789. [Abstract] [Full Text] [PDF]

				A. K. Das, B. Dasgupta, R. Bhattacharya, and J. Basu Purification and Biochemical Characterization of a Protein-palmitoyl Acyltransferase from Human Erythrocytes J. Biol. Chem., April 25, 1997; 272(17): 11021 - 11025. [Abstract] [Full Text] [PDF]

				J.-Y. Lu and J. Y. Lu Depalmitoylation of CAAX Motif Proteins J. Biol. Chem., March 31, 1995; 270(13): 7251 - 7256. [Abstract] [Full Text] [PDF]

				A Schweizer, J Rohrer, P Jeno, A DeMaio, T. Buchman, and H. Hauri A reversibly palmitoylated resident protein (p63) of an ER-Golgi intermediate compartment is related to a circulatory shock resuscitation protein J. Cell Sci., January 3, 1993; 104(3): 685 - 694. [Abstract] [PDF]