SERPINE2, a serine protease inhibitor extensively expressed in adult male mouse reproductive tissues, may serve as a murine sperm decapacitation factor.
Resource
Biology of Reproduction, 84(3), 514-525
Journal
Biology of Reproduction
Pages
522
Date Issued
2011
Date
2011
Author(s)
Lu, CH
Lee Robert, KK
Hwu, YM
Chu, SL
Chen, YJ
Chang, WC
Lin, S.P
Li, SH.
Abstract
SERPINE2, one of the potent serine protease inhibitor for modulating the activity of the plasminogen activator and thrombin, has been implicated in many biological processes. In the present study, we purified SERPINE2 from the mouse seminal vesicle secretion using liquid chromatography, identified by the liquid chromatography/tandem mass spectrometry, and showed a potent inhibitory activity to the urokinase-type plasminogen activator. SERPINE2 was expressed predominantly in seminal vesicles among murine male reproductive tissues. It was mainly detected in the mouse seminal vesicle secretion and mucosal epithelium of the seminal vesicle, epididymis, coagulating gland, and vas deferens. In the testis, SERPINE2 was found in spermatogonia, spermatocyte, spermatid, Leydig cell, and on spermatozoa. SERPINE2 was detected on the acrosomal cap of the testicular and epididymal sperm and suggested to be an intrinsic sperm surface protein. The purified SERPINE2 protein could bind onto the epididymal sperm. A prominent amount of SERPINE2 was detected on ejaculated and oviductal spermatozoa. Nevertheless, SERPINE2 was only detected on the uncapacitated sperm but not on the capacitated sperm, indicating that SERPINE2 is lost after the initiation of capacitation process. Moreover, SERPINE2 could inhibit BSA-induced sperm capacitation in vitro and prevent sperm binding to the egg thus block fertilization. It was through preventing the cholesterol efflux, one of the initiation events of capacitation, from the sperm. These findings suggest that the SERPINE2 protein may play a role as a sperm decapacitation factor. (poster)
Type
journal article
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