{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T12:39:11Z","timestamp":1791117551474,"version":"4.1.0"},"reference-count":19,"publisher":"Portland Press Ltd.","issue":"5","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2011,10,1]]},"abstract":"<jats:p>Our laboratory has characterized EPPIN [epididymal protease inhibitor; SPINLW1] as a novel gene on human chromosome 20q12-13.2, which encodes a cysteine-rich protein of 133 amino acids with a calculated molecular mass of 15.283\u00a0kDa, containing both Kunitz-type and WAP (whey acidic protein)-type four-disulfide core consensus sequences. Eppin is secreted by Sertoli cells in the testis and epididymal epithelial cells; it is predominantly a dimer, although multimers often exist, and in its native form eppin is found on the human sperm surface complexed with LTF (lactotransferrin) and clusterin. During ejaculation SEMG (semenogelin) from the seminal vesicles binds to the eppin protein complex, initiating a series of events that define eppin's function. Eppin's functions include (i) modulating PSA (prostate-specific antigen) enzyme activity, (ii) providing antimicrobial protection and (iii) binding SEMG thereby inhibiting sperm motility. As PSA hydrolyses SEMG in the ejaculate coagulum, spermatozoa gain progressive motility. We have demonstrated that eppin is essential for fertility because immunization of male monkeys with recombinant eppin results in complete, but reversible, contraception. To exploit our understanding of eppin's function, we are developing compounds that inhibit eppin\u2013SEMG interaction and mimic anti-eppin, inhibiting sperm motility. These compounds should have potential as a male contraceptive.<\/jats:p>","DOI":"10.1042\/bst0391447","type":"journal-article","created":{"date-parts":[[2012,5,3]],"date-time":"2012-05-03T12:32:44Z","timestamp":1336048364000},"page":"1447-1449","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":25,"title":["Functional studies of eppin"],"prefix":"10.1042","volume":"39","author":[{"given":"Michael\u00a0G.","family":"O'Rand","sequence":"first","affiliation":[{"name":"Department of Cell and Developmental Biology and Laboratories for Reproductive Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, U.S.A."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Esther\u00a0E.","family":"Widgren","sequence":"additional","affiliation":[{"name":"Department of Cell and Developmental Biology and Laboratories for Reproductive Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, U.S.A."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Katherine\u00a0G.","family":"Hamil","sequence":"additional","affiliation":[{"name":"Department of Cell and Developmental Biology and Laboratories for Reproductive Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, U.S.A."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Erick\u00a0J.","family":"Silva","sequence":"additional","affiliation":[{"name":"Department of Cell and Developmental Biology and Laboratories for Reproductive Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, U.S.A."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Richard\u00a0T.","family":"Richardson","sequence":"additional","affiliation":[{"name":"Department of Cell and Developmental Biology and Laboratories for Reproductive Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, U.S.A."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","published-online":{"date-parts":[[2011,9,21]]},"reference":[{"key":"2021111900491312000_B1","doi-asserted-by":"crossref","first-page":"1245","DOI":"10.1210\/endo.141.3.7389","article-title":"HE2b and HE2g, new members of an epididymis-specific family of androgen-regulated proteins in the human","volume":"141","author":"Hamil","year":"2000","journal-title":"Endocrinology"},{"key":"2021111900491312000_B2","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1016\/S0378-1119(01)00462-0","article-title":"Cloning and sequencing of human Eppin: a novel family of protease inhibitors expressed in the epididymis and testis","volume":"270","author":"Richardson","year":"2001","journal-title":"Gene"},{"key":"2021111900491312000_B3","doi-asserted-by":"crossref","first-page":"476","DOI":"10.1095\/biolreprod.107.060194","article-title":"Characterization of an eppin protein complex from human semen and spermatozoa","volume":"77","author":"Wang","year":"2007","journal-title":"Biol. 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