アブストラクト(20巻1号:The Bulletin of Kanagawa Dental College)

The Bulletin of Kanagawa Dental College

English

Title : The In Vitro Fatty Acylation of Human Spectrin
Subtitle : ORIGINAL ARTICLES
Authors : Yoshinori Jinbu
Authors(kana) :
Organization : Maxillo Facial Radiology, Kanagawa Dental College
Journal : The Bulletin of Kanagawa Dental College
Volume : 20
Number : 1
Page : 9-15
Year/Month : 1992 / 3
Article : Original article
Publisher : Kanagawa Odontological Society
Abstract : [Abstract] Spectrin is a major component of erythrocyte membrane skeleton and spectrin-like molecules are known to be distributed in different cell types. The in vitro fatty acylation of human erythrocyte membrane skeleton proteins was investigated. The β subunit of spectrin was found to be the major fatty acylated protein when the crude spectrin fraction was incubated with [14C] myristoyl CoA, [3H] myristoyl CoA, or [3H] palmitoyl CoA. Neither membrane ghosts nor spectrin depleted inside-out vesicles showed any major radiolabeled band. The radiolabeled protein was precipitated by anti-human spectrin antibodies. The incorporated [14C] myristoyl residue was not removed by repeated chloroform/methanol extractions but was sensitive to incubation with hydroxylamine. The reaction was strongly inhibited by in-side-out vesicles and hemolysates. The pH optimum of the reaction was approximately 8. Palmitoyl CoA was preferred over myristoyl CoA as substrate. These results indicate that the crude spectrin fraction contained a protein-acyltransferase and that the β subunit of spectrin can be fatty acylated through an ester linkage. In vivo, the fatty acylation of spectrin may play a role in the interaction of spectrin with membrane or other membrane skeleton proteins.
Practice : Dentistry
Keywords : Fatty Acylation, Cytoskeleton, Erythrocyte, Spectrin