TY - JOUR
T1 - Gelatinolytic proteinase activities in human seminal plasma
AU - Yin, H. Z.
AU - Vogel, M. M.
AU - Schneider, M.
AU - Ercole, C.
AU - Zhang, G.
AU - Sinha, A. A.
AU - Wilson, M. J.
PY - 1990
Y1 - 1990
N2 - Proteinase activities in human seminal plasma were detected using gelatin-containing sodium dodecyl sulphate-polyacrylamide gel electrophoresis zymography. Three prominent bands of activity of M(r) 60,000, 66,000 and 90,000 were observed as well as 9 other bands of less intensity (34,000-158,000). These proteinases were dependent upon calcium for optimal activity, did not hydrolyse casein, and were predominantly in the soluble portion of seminal plasma. Examination of seminal plasma of men with different sperm concentrations, split ejaculates, and prostatic secretions indicated that the prostate gland was a source of most of these activities. Proteinase activities of M(r) 34,000, 37,000, 82,000 and 120,000 were expressed more frequently in seminal plasma from normozoospermic men than from seminal plasma of oligo- and azoospermic men, indicating that they may also arise from spermatozoa in the semen sample. The proteinases of M(r) 60,000 and 66,000 were found in all seminal plasmas whereas there was variation in the expression of the other molecular forms of enzyme, even in the normozoospermic samples. There are multiple forms of gelatinolytic proteinase activities in human seminal plasma which appear to arise from multiple sources in the reproductive tract including the Cowper's/urethral glands, the prostate gland, seminal vesicle and/or spermatozoa. Their function(s) in semen remains to be established.
AB - Proteinase activities in human seminal plasma were detected using gelatin-containing sodium dodecyl sulphate-polyacrylamide gel electrophoresis zymography. Three prominent bands of activity of M(r) 60,000, 66,000 and 90,000 were observed as well as 9 other bands of less intensity (34,000-158,000). These proteinases were dependent upon calcium for optimal activity, did not hydrolyse casein, and were predominantly in the soluble portion of seminal plasma. Examination of seminal plasma of men with different sperm concentrations, split ejaculates, and prostatic secretions indicated that the prostate gland was a source of most of these activities. Proteinase activities of M(r) 34,000, 37,000, 82,000 and 120,000 were expressed more frequently in seminal plasma from normozoospermic men than from seminal plasma of oligo- and azoospermic men, indicating that they may also arise from spermatozoa in the semen sample. The proteinases of M(r) 60,000 and 66,000 were found in all seminal plasmas whereas there was variation in the expression of the other molecular forms of enzyme, even in the normozoospermic samples. There are multiple forms of gelatinolytic proteinase activities in human seminal plasma which appear to arise from multiple sources in the reproductive tract including the Cowper's/urethral glands, the prostate gland, seminal vesicle and/or spermatozoa. Their function(s) in semen remains to be established.
KW - human
KW - proteinase
KW - seminal plasma
UR - http://www.scopus.com/inward/record.url?scp=0025271441&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0025271441&partnerID=8YFLogxK
U2 - 10.1530/jrf.0.0880491
DO - 10.1530/jrf.0.0880491
M3 - Article
C2 - 2182842
AN - SCOPUS:0025271441
SN - 0022-4251
VL - 88
SP - 491
EP - 501
JO - Journal of reproduction and fertility
JF - Journal of reproduction and fertility
IS - 2
ER -