Testosterone and 6-N,2'-O-dibutyryladenosine 3′:5′-cyclic monophosphate stimulate protein and lysosomal enzyme secretion in rat seminal vesicle

Abstract

Rat seminal-vesicle secretion was studied in vitro in a slice-incubation system. Seminalvesicle slices were preincubated with 32p, for 15 min, rinsed, and incubated in an isotopefree 'chase' medium for up to 4h. Gland slices spontaneously discharged protein, three lysosomal hydrolases and trichloroacetic acid-insoluble 32P into the medium in a time-and temperature-dependent manner. Testosterone (10puM) and dibutyryl cyclic AMP (1 mM) stimulated the discharge ofprotein, acid hydrolases and trichloroacetic acid-insoluble 32p, and also stimulated the incorporation of 32Pi into trichloroacetic acid-insoluble components. The acid phosphatase and J-N-acetylhexosaminidase isoenzymes were separated by isoelectric focusing. These hydrolases were secreted into the medium as acidic isoenzymes, presumably contained within primary lysosomes, whereas they occurred largely as less acidic and basic isoenzymes in the glandular tissue.