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Is asparagine-linked protein glycosylation an obligatory requirement for angiogenesis?
Article in English | IMSEAR | ID: sea-27515
ABSTRACT
Dependence of protein N-glycosylation on capillary endothelial cell proliferation has been studied. Amphomycin, a potent N-glycosylation inhibitor, inhibited capillary endothelial cell proliferation in a dose-dependent manner. beta-Agonist isoproterenol as well as other intracellular cAMP enhancing agents, viz. cholera toxin, prostaglandin E1 and 8Br-cAMP, also enhanced capillary endothelial cell proliferation. In addition to cell proliferation, isoproterenol also enhanced protein glycosylation in these cells. Isoproterenol effect was mediated by beta-adrenoreceptors, as it got reduced on pre-treatment of cells with either atenolol or ICI 118, 551 or propranolol. Furthermore, isoproterenol stimulation of protein glycosylation by exogenous dolichyl monophosphate and its inhibition by tunicamycin (GlcNAc-1P transferase inhibitor) supported the concept that isoproterenol specifically stimulated protein N-glycosylation event(s) in the cell.
Subject(s)
Full text: Available Index: IMSEAR (South-East Asia) Main subject: Oligopeptides / Asparagine / Glycosylation / 8-Bromo Cyclic Adenosine Monophosphate / Cattle / Endothelium, Vascular / Alprostadil / Cell Division / Cells, Cultured / Protein Processing, Post-Translational Language: English Year: 1993 Type: Article

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Full text: Available Index: IMSEAR (South-East Asia) Main subject: Oligopeptides / Asparagine / Glycosylation / 8-Bromo Cyclic Adenosine Monophosphate / Cattle / Endothelium, Vascular / Alprostadil / Cell Division / Cells, Cultured / Protein Processing, Post-Translational Language: English Year: 1993 Type: Article