Synthesis of androgen-dependent secretory proteins by rat seminal vesicles.
Androgenic steroids control the synthesis and secretion of several proteins by the seminal vesicles of the male rat. Prominent among them are 2 basic proteins, S and F, previously used as markers of androgen action. These proteins are not found among translation products of a wheat-germ protein-synthesising system supplied with mRNA from seminal vesicles of normal rats. Instead, higher molecular weight forms, S' and F', are formed which are nonetheless related antigenically to S and F respectively. Injected into Xenopus Laevis oocytes, seminal vesicle mRNA does direct synthesis and secretion of polypeptides S and F. Partial peptide analysis confirms that S' and F' have extensive amino acid sequence homology with S and F respectively. We conclude that S' and F' are precursor forms of the secreted proteins and thus at least 2 abundant proteins of this male accessory tissue are secreted by a mechanism common to a wide number of secreted proteins.
D000728:Androgens / Q000502:physiology*; D000818:Animals; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D008297:Male; D008970:Molecular Weight; D009865:Oocytes / Q000378:metabolism; D029584:Prostatic Secretory Proteins; D014176:Protein Biosynthesis; D012333:RNA, Messenger / Q000378:metabolism; D051381:Rats; D029589:Seminal Plasma Proteins; D012669:Seminal Vesicles / Q000378:metabolism*; D014982:Xenopus laevis
D000728:Androgens; D029584:Prostatic Secretory Proteins; D012333:RNA, Messenger; D029589:Seminal Plasma Proteins; C043076:beta-microseminoprotein