Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P56851 (epididymal)
 11,273 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Guinea pig spermatozoa were found to contain a fully-latent cysteine proteinase that could be unmasked by incubating epididymal sperm for 2 hr at pH 3.5 and 37 degrees C. The proteinase was identified as cathepsin L (EC 3.4.22.15) on the basis of its optimal hydrolysis of benzyloxycarbonyl-Phe-Arg-7-(4-methyl)coumarylamide (Z-Phe-Arg-NMec) at pH 5.5; lack of action on Z-Arg-Arg-NMec and Arg-NMec; urea-enhanced digestion of azocasein; marked sensitivity to thiol reagents, leupeptin, Z-Phe-Phe-CHN2, and L-trans-epoxy-succinylleucylamido(3-methyl)butane (Ep-475 or E-64-c); and insensitivity to pepstatin and serine proteinase inhibitors. Gossypol, a male antifertility agent, was inhibitory. The unmasking phenomenon was reversibly inhibited by HgCl2 and mersalyl acid, and prevented by leupeptin and Ep-475, but not by pepstatin.
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PMID:Cathepsin L--a latent proteinase in guinea pig sperm. 334 13

Germinal angiotensin I-converting enzyme (gACE) is expressed only in the testis and is uniquely present in developing spermatids and sperm. We previously purified soluble gACE from porcine seminal plasma, and reported that gACE was secreted from residual body on spermatozoa by the other peptidase(s), namely Sheddase. Using Nma/DNP substrate, it was observed that the shedding activity in testicular fluid was stronger than in the sperm membrane and epididymal fluid. The shedding activity was inhibited by AEBSF and antipain, and not by EDTA and E-64. Accordingly, it is thought that Sheddase is an endo-type of serine peptidase.
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PMID:Shedding of gACE from residual body membrane of rat sperm. 1937 70