Enhancement of UDPgalactose: glycoprotein galactosyltransferase in cultured human skin fibroblasts by cationic polypeptides.
Publication/Presentation Date
7-17-1978
Abstract
UDPgalactose : glycoprotein galactosyltransferase in normal human skin fibroblast homogenates has been assayed using ovalbumin as an acceptor. The activity in the homogenate fraction sedimenting between 51 300 X g and 105 000 X g was enhanced by the addition of a number of catonic polypeptides of L-configuration but not by those of D-configuration. In contrast to the enhancing effect of poly(L-lysine), poly(L-glutamic acid) inhibited the activity. Poly(D-glutamic acid) had no effect. Cationic or anionic amino acid derivatives, spermine or spermidine had no effect on activity. The enhancement of transferase activity by poly(L-arginine) is probably due to an increase in V for UDPgalactose and ovalbumin. The implication of these results for the regulation of glycoprotein synthesis in cultivated skin fibroblasts and for the pathogenesis of cystic fibrosis is discussed.
Volume
541
Issue
4
First Page
435
Last Page
442
ISSN
0006-3002
Published In/Presented At
Rao, G. J., Chyatte, D., & Nadler, H. L. (1978). Enhancement of UDPgalactose: glycoprotein galactosyltransferase in cultured human skin fibroblasts by cationic polypeptides. Biochimica et biophysica acta, 541(4), 435–442. https://doi.org/10.1016/0304-4165(78)90153-8
Disciplines
Medicine and Health Sciences
PubMedID
667130
Department(s)
Department of Surgery
Document Type
Article