Removal of P12 (a Kazal-type Trypsin Inhibitor) on Mouse Sperm by Serine Protease in the Uterine Fluid
Date Issued
2008
Date
2008
Author(s)
Abstract
Trypsin inhibitor P12 consists of 57 amino acid residues in which six cysteines are crosslinked into three disulfide bonds. It is a protein of Mr 6126 Da with no glycoconjugate and belongs to Kazal-type trypsin inhibitor family. Among the reproductive tracts of male and female mice, P12 is only present in seminal vesicle, prostate and coagulating gland of adult male. P12 can specifically bind to sperm acrosome region to affect sperm activaty after ejaculation and it’s gene expression in these accessory sexual glands is androgen-dependent. It has verified that P12 can suppress a great extent of Ca2+-uptake by spermatozoa and has the ability to suppress capacitation, acrosome reaction, motility and hyperactivation of mouse spermatozoa. This work aims to study how to remove P12 on sperm acrosome before sperm-egg encounter. Results of Zymography and protease activity assay demonstrated a 33 kDa P12-inhibited protease in the mouse uterine fluid. It was a serine-type protease, because it could be inhibited by PMSF (phenylmethylsulphonyl fluoride). It was likely to be airway trypsin-like protease, as suggested by the partial peptide sequences determined by MS/MS analysis. Result of indirect immunofluorescence statining assay demonstrated the removal of P12 on sperm acrosome by the serine protease in uterine fluid.
Subjects
P12
sperm acrosome
protease
uterine fluid
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