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In vitro synthesis and glycosylation of androgen‐dependent secretory proteins of rat dorsal prostate and coagulating gland
Author(s) -
Bartlett Richard J.,
French Frank S.,
Wilson Elizabeth M.
Publication year - 1984
Publication title -
the prostate
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.295
H-Index - 123
eISSN - 1097-0045
pISSN - 0270-4137
DOI - 10.1002/pros.2990050108
Subject(s) - glycosylation , tunicamycin , secretory protein , golgi apparatus , secretion , glycoprotein , protein biosynthesis , biochemistry , methionine , in vitro , biology , translation (biology) , endoplasmic reticulum , androgen , chemistry , microbiology and biotechnology , medicine , messenger rna , amino acid , hormone , unfolded protein response , gene
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 [ 35 S]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 [ 35 S]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 μg/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.