Stimulation of protein synthesis in pachytene primary spermatocytes from the human testis by pyruvate.
A sequential enzymatic incubation in collagenase and trypsin was carried out to yield a suspension of viable single cells from the seminiferous epithelium of adult human testis. The cell suspension predominantly consisted of pachytene primary spermatocytes (15%), round spermatids (32%), and condensing spermatids and residual bodies (21%). Human pachytene spermatocytes were isolated by unit gravity sedimentation using the methods originally developed for murine tissue. The spermatocyte-enriched fraction was 79% pure. When the effect of energy sources on protein synthesis by spermatocytes was examined, the highest rate of protein synthesis with pyruvate was found among four kinds of substrates added at a concentration of 10 mM. As shown with murine spermatocytes, the rate of protein synthesis by the human spermatocytes is probably regulated by pyruvate.
D000368:Aged; D004734:Energy Metabolism; D006801:Humans; D066298:In Vitro Techniques; D008297:Male; D008540:Meiosis; D014176:Protein Biosynthesis; D011773:Pyruvates / Q000494:pharmacology*; D013090:Spermatocytes / Q000187:drug effects / Q000378:metabolism*; D013737:Testis
D011773:Pyruvates