LORENZ, C and STRAHLBOLSINGER, S and ERNST, JF (1992) SPECIFIC INVITRO O-GLYCOSYLATION OF HUMAN GRANULOCYTE-MACROPHAGE COLONY-STIMULATING-FACTOR-DERIVED PEPTIDES BY O-GLYCOSYLTRANSFERASES OF YEAST AND RAT-LIVER CELLS. EUROPEAN JOURNAL OF BIOCHEMISTRY, 205 (3). pp. 1163-1167. ISSN 0014-2956,
Full text not available from this repository.Abstract
Human granulocyte-macrophage colony-stimulating factor (hGM-CSF) is O-glycosylated at residues Ser9 and Thr10 during secretion by yeast and COS-1 cells [Ernst, J. F., Mermod, J.-J. and Richman, L. I. (1992) Eur. J. Biochem. 203, 663-667]. Two types of octapeptides encompassing residues 4-11 (peptide 4-11) and variants thereof, or residues 8-15 (peptide 8-15) of hGM-CSF were tested as substrates for in vitro O-glycosylation using dolichyl-phosphate-D-mannose: protein O-D-mannosyltransferase (Man-transferase) of the yeast Saccharomyces cerevisiae, or UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-transferase) of rat liver cells. Peptide 8-15 was found to be O-glycosylated at residues Ser9 and Thr10 by GalNAc-transferase and, with reduced efficiency, also by Man-transferase. Peptide 4-11 was a good substrate for yeast Man-transferase, leading to mannosylation of only Thr10, whereas it was very poorly O-glycosylated at positions Ser5 and Ser7 by GalNAc-transferase. The observed differences in peptide-acceptor activities indicate that the site of O-glycosylation depends on similar, but not identical protein structural features in yeast and mammalian cells.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | SACCHAROMYCES-CEREVISIAE; N-ACETYLGALACTOSAMINE; GM-CSF; |
| Depositing User: | Dr. Gernot Deinzer |
| Last Modified: | 19 Oct 2022 08:44 |
| URI: | https://pred.uni-regensburg.de/id/eprint/54548 |
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