{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T22:43:21Z","timestamp":1790894601001,"version":"4.1.0"},"reference-count":51,"publisher":"Portland Press Ltd.","issue":"1","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2005,11,15]]},"abstract":"<jats:p>We have shown previously that a \u2018soluble\u2019 form of PrP (prion protein), not associated with membranous vesicles, exists in the male reproductive fluid [Ecroyd, Sarradin, Dacheux and Gatti (2004) Biol. Reprod. 71, 993\u20131001]. Attempts to purify this \u2018soluble\u2019 PrP indicated that it behaves like a high-molecular-mass complex of more than 350\u00a0kDa and always co-purified with the same set of proteins. The main associated proteins were sequenced by MS and were found to match to clusterin (apolipoprotein J), BPI (bacterial permeability-increasing protein), carboxylesterase-like urinary excreted protein (cauxin), \u03b2-mannosidase and \u03b2-galactosidase. Immunoblotting and enzymatic assay confirmed the presence of clusterin and a cauxin-like protein and showed that a 17\u00a0kDa hydrophobic epididymal protein was also associated with this complex. These associated proteins were not separated by a high ionic strength treatment but were by 2-mercaptoethanol, probably due to its action on reducing disulphide bonds that maintain the interaction of components of the complex. Our results suggest that the associated PrP retains its GPI (glycosylphosphatidylinositol) anchor, in contrast with brain-derived PrP, and that it is resistant to cleavage by phosphatidylinositol-specific phospholipase C. Based on these results, the identity of the associated proteins and the overall biochemical properties of this protein ensemble, we suggest that \u2018soluble\u2019 PrP can form protein complexes that are maintained by hydrophobic interactions, in a similar manner to lipoprotein vesicles or micellar complexes.<\/jats:p>","DOI":"10.1042\/bj20050459","type":"journal-article","created":{"date-parts":[[2005,11,8]],"date-time":"2005-11-08T12:13:19Z","timestamp":1131451999000},"page":"211-219","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":28,"title":["The epididymal soluble prion protein forms a high-molecular-mass complex in association with hydrophobic proteins"],"prefix":"10.1042","volume":"392","author":[{"given":"Heath","family":"Ecroyd","sequence":"first","affiliation":[{"name":"Gam\u00e8te Male et Fertilit\u00e9, Institut National de la Recherche Agronomique, INRA-Nouzilly, 37380 Monnaie, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Maya","family":"Belghazi","sequence":"additional","affiliation":[{"name":"Service de Spectrom\u00e9trie de Masse pour la Prot\u00e9omique, UMR 6175, INRA-CNRS-Haras Nationaux-Universit\u00e9 de Tours, Station de Physiologie de la Reproduction et des Comportements, Institut National de la Recherche Agronomique, INRA-Nouzilly, 37380 Monnaie, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jean-Louis","family":"Dacheux","sequence":"additional","affiliation":[{"name":"Gam\u00e8te Male et Fertilit\u00e9, Institut National de la Recherche Agronomique, INRA-Nouzilly, 37380 Monnaie, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jean-Luc","family":"Gatti","sequence":"additional","affiliation":[{"name":"Gam\u00e8te Male et Fertilit\u00e9, Institut National de la Recherche Agronomique, INRA-Nouzilly, 37380 Monnaie, France"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","published-online":{"date-parts":[[2005,11,8]]},"reference":[{"key":"2021112214093930600_B1","doi-asserted-by":"crossref","first-page":"9097","DOI":"10.1073\/pnas.89.19.9097","article-title":"Molecular cloning of a candidate chicken prion protein","volume":"89","author":"Gabriel","year":"1992","journal-title":"Proc. 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