Relationship of the structure and biological activity of the natural homologues of tunicamycin.
The antibiotic tunicamycin was separated into 16 different components using reversed-phase high performance liquid chromatography. The effect of the eight major tunicamycin homologues on protein glycosylation and protein biosynthesis was examined. All homologues tested inhibited lipid-mediated protein glycosylation in chick or mouse fibroblasts. These homologues also inhibited the transfer of N-acetylglucosamine-1-phosphate from UDP-N-acetylglucosamine to dolichyl phosphate in chick liver microsome preparations, whereas the transfer of mannose from GDP-mannose to the lipid acceptor was hardly affected. The inhibition of protein glycosylation in fibroblasts or in microsomal preparations was concentration-dependent and maximum inhibition occurred at different concentrations for different homologues. The eight homologues differed in their ability to cause inhibition of protein synthesis.
D000818:Animals; D002478:Cells, Cultured; D002642:Chick Embryo; D002851:Chromatography, High Pressure Liquid; D004622:Embryo, Mammalian; D005347:Fibroblasts / Q000187:drug effects; D005944:Glucosamine / Q000031:analogs & derivatives*; D006023:Glycoproteins / Q000096:biosynthesis; D007700:Kinetics; D051379:Mice; D014176:Protein Biosynthesis / Q000187:drug effects; D013329:Structure-Activity Relationship; D013710:Tendons / Q000187:drug effects; D014415:Tunicamycin / Q000302:isolation & purification / Q000494:pharmacology*
D006023:Glycoproteins; D014415:Tunicamycin; D005944:Glucosamine