Molecular Human Reproduction, Vol. 8, No. 1, 32-36,
January 2002
© 2002 European Society of Human Reproduction and Embryology
Testis and spermatogenesis |
Matrix metalloproteinase (MMP)-2 and MMP-9 activities in human seminal plasma
1 Department of Functional Bioanalysis, 2 Department of Chemistry of Hygiene, Meiji Pharmaceutical University, 2–522–1 Noshio, Kiyose, Tokyo 204-8588, 3 Department of Obstetrics and Gynecology, Tachikawa Kyosai Hospital, Tokyo and 4 Department of Urology, Ichikawa General Hospital and Tokyo Dental College, Chiba, Japan
We report on the existence of two kinds of matrix metalloproteinases (MMPs), MMP-2 and MMP-9, in human seminal plasma. Partial purification of the proteinases was achieved by two steps, consisting of chromatography on a gel-filtration column and then on a gelatin affinity column. Proteinase activities in the chromatography extracts were shown to hydrolyse a fluorescent substrate specific to MMPs (Dnp-Pro-Leu-Gly-Leu-Trp-Ala-D-Arg-NH2). The proteinases were detected using gelatin-zymography, but were not detected using casein-zymography, and were also inhibited by EDTA, EGTA and o-phenanthroline. Molecular weights of the proteinases were determined by SDS–PAGE, gelatin-zymography and Western blot to be ~92, 84, 72, 67, 52 and 45 kDa. Gelatin-zymography showed three major bands of activity at 72, 67 and 52 kDa and minor bands at 92, 84 and 45 kDa. Apart from the two smallest bands, these proteinases were all recognized by the polyclonal antibodies for MMP-2 or MMP-9. These results indicate that two kinds of pro-form and active-form matrix metalloproteinases, MMP-2 and MMP-9, and their degradation products, are present in human seminal plasma.
human seminal plasma/matrix metalloproteinase/MMP/proteinase/zymography
5 To whom correspondence should be addressed. E-mail: kshimoka{at}my-pharm.ac.jp
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