title: In vitro synthesis and glycosylation of androgen-dependent secretory proteins of rat dorsal prostate and coagulating gland.
abstract: The two major androgen-dependent secretory proteins of rat dorsal prostate and coagulating gland, DP I and DP II, were compared by in vitro translation of total poly(A)RNA and by pulse-chase techniques by means of [35S]methionine and tissue minces of coagulating gland. DP I is a major in vitro translation product of isolated poly(A)RNA, whereas DP II is undetectable in a mouse embryo fibroblast cell-free system where glycosylation does not occur. DP I is synthesized within 20 min in minces of coagulating gland incubated in the presence of [35S]methionine and is secreted in 40 min. DP II is detectable in the medium only after 8 hr of labeling. Inhibition of asparagine-linked protein glycosylation with tunicamycin (10 micrograms/ml) blocked the synthesis and secretion of DP II with an apparent increase in DP I secretion. Inhibition of DP II synthesis by monensin implicates the Golgi in the processing of DP II oligosaccharides. The data are consistent with the proposal that DP I enters a pathway of rapid secretion that is enhanced by the absence of core glycosylation, whereas DP II follows a slow pathway through the Golgi that involves extensive glycosylation.
mesh_terms: D000727:Androgen-Binding Protein / Q000032:analysis / Q000096:biosynthesis* / Q000378:metabolism; D000818:Animals; D002352:Carrier Proteins / Q000096:biosynthesis*; D002369:Castration; D004591:Electrophoresis, Polyacrylamide Gel; D066298:In Vitro Techniques; D008297:Male; D011061:Poly A / Q000378:metabolism; D011233:Precipitin Tests; D011467:Prostate / Q000187:drug effects / Q000378:metabolism*; D014176:Protein Biosynthesis / Q000187:drug effects; D012313:RNA / Q000378:metabolism; D012333:RNA, Messenger; D051381:Rats; D011919:Rats, Inbred Strains
chemical_list: D000727:Androgen-Binding Protein; D002352:Carrier Proteins; D012333:RNA, Messenger; C027519:probasin; D011061:Poly A; D012313:RNA