Abstract：
:Eppin (epididymal protease inhibitor) is a member of the whey acidic protein (WAP)-type four-disulfide core (WFDC) gene family. This study provides updated information on Eppin and the Eppin-like genes within the Eppin cluster on human chromosome 20. A virtual structural model of the Eppin protein demonstrates that the C-terminal half of Eppin is structurally homologous to the Kunitz-type trypsin inhibitor. The Eppin N-terminal may have structural similarities to defensin-type molecules, rather than to that of the WAP consensus sequence. Human spermatozoa have a receptor for Eppin. When recombinant semenogelin (Sg) is digested with PSA many low molecular weight fragments are produced. However, when Eppin is bound to Sg, digestion by PSA is modulated. Addition of antibodies to the C-terminal of Eppin resulted in blocking PSA activity modulation. We can hypothesize from our analysis of anti-Eppin epitopes on Eppin that when anti-Eppin antibodies are bound to Eppin on the sperm surface they block the binding site for semenogelin.
journal_name
Mol Cell Endocrinoljournal_title
Molecular and cellular endocrinologyauthors
O'Rand MG,Widgren EE,Wang Z,Richardson RTdoi
10.1016/j.mce.2005.12.039keywords:
subject
Has Abstractpub_date
2006-05-16 00:00:00pages
157-62issue
1-2eissn
0303-7207issn
1872-8057pii
S0303-7207(05)00485-5journal_volume
250pub_type
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