{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,4]],"date-time":"2026-07-04T16:05:59Z","timestamp":1783181159782,"version":"3.54.6"},"reference-count":37,"publisher":"Wiley","issue":"7","license":[{"start":{"date-parts":[[2010,10,28]],"date-time":"2010-10-28T00:00:00Z","timestamp":1288224000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["The Prostate"],"published-print":{"date-parts":[[2011,5,15]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:sec><jats:title>BACKGROUND<\/jats:title><jats:p>Prostasomes are exosome\u2010like vesicles that are secreted by the prostate and incorporated into semen during ejaculation. Human prostasomes are proposed to function in regulation of sperm function, immunosuppression, and prostate cancer progression. Previously, we identified galectin\u20103 on the surface of prostasomes. Galectin\u20103 is a \u03b2\u2010galactoside binding protein involved in immunomodulation, cell interactions, and cancer progression, including prostate cancer. Functional characterization of galectin\u20103 in a given biological environment includes identification of its target glycoprotein ligands.<\/jats:p><\/jats:sec><jats:sec><jats:title>METHODS<\/jats:title><jats:p>Candidate galectin\u20103 ligands in prostasomes were identified by tandem mass spectrometry of proteins that co\u2010purified with galectin\u20103 during lactose affinity chromatography. Immunochemical and biochemical methods were used to investigate the association of Mac\u20102 binding protein (M2BP) with prostasomes.<\/jats:p><\/jats:sec><jats:sec><jats:title>RESULTS<\/jats:title><jats:p>Proteins identified by tandem mass spectrometry included M2BP, CD26\/dipeptidyl peptidase IV, prolactin\u2010inducible protein (PIP), olfactomedin\u20104 (OLFM4), and semenogelins I and II (SgI and SgII). M2BP is a known galectin\u20103 ligand that was not previously described in prostasomes. M2BP protein bands were detected in the testis, epididymis, vas deferens, prostate, seminal vesicle, and sperm extracts. In seminal plasma, M2BP was identified in the soluble fraction and in purified prostasomes. Surface biotinylation and immunofluorescence studies indicated that M2BP is present on the prostasome surface and on sperm, respectively.<\/jats:p><\/jats:sec><jats:sec><jats:title>CONCLUSIONS<\/jats:title><jats:p>M2BP, CD26, PIP, OLFM4, and SgI and SgII are candidate glycoprotein ligands for galectin\u20103 in prostasomes. Given their overlap in functional significance with prostasomes and galectin\u20103, the identification of these glycoproteins as galectin\u20103 ligands in prostasomes lays the groundwork for future studies of prostasomes in reproduction and prostate cancer. Prostate 71:711\u2013721, 2011. \u00a9 2010 Wiley\u2010Liss, Inc.<\/jats:p><\/jats:sec>","DOI":"10.1002\/pros.21287","type":"journal-article","created":{"date-parts":[[2010,10,29]],"date-time":"2010-10-29T11:32:52Z","timestamp":1288351972000},"page":"711-721","source":"Crossref","is-referenced-by-count":33,"title":["Co\u2010purification of Mac\u20102 binding protein with galectin\u20103 and association with prostasomes in human semen"],"prefix":"10.1002","volume":"71","author":[{"given":"Ashley S.","family":"Block","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sarika","family":"Saraswati","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Cheryl 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