{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,20]],"date-time":"2026-07-20T14:19:06Z","timestamp":1784557146171,"version":"3.55.0"},"reference-count":39,"publisher":"Bioscientifica","issue":"1","content-domain":{"domain":["jme.bioscientifica.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2013,2]]},"abstract":"<jats:p>Prolactin is essential for normal mammary gland development and differentiation, and has been shown to promote tumor cell proliferation and chemotherapeutic resistance. Soluble isoforms of the prolactin receptor (PrlR) have been reported to regulate prolactin bioavailability by functioning as \u2018prolactin-binding proteins\u2019. Included in this category is \u03947\/11, a product of alternate splicing of the PrlR primary transcript. However, the direct interactions of prolactin with \u03947\/11, and the resulting effect on cell behavior, have not been investigated. Herein, we demonstrate the ability of \u03947\/11 to bind prolactin using a novel proximity ligation assay and traditional immunoprecipitation techniques. Biochemical analyses demonstrated that \u03947\/11 was heavily glycosylated, similar to the extracellular domain of the primary PrlR, and that glycosylation regulated the cellular localization and secretion of \u03947\/11. Low levels of \u03947\/11 were detected in serum samples of healthy volunteers, but were undetectable in human milk samples. Expression of \u03947\/11 was also detected in six of the 62 primary breast tumor biopsies analyzed; however, no correlation was found with \u03947\/11 expression and tumor histotype or other patient demographics. Functional analysis demonstrated the ability of \u03947\/11 to inhibit prolactin-induced cell proliferation as well as alter prolactin-induced rescue of cell cycle arrest\/early senescence events in breast epithelial cells. Collectively, these data demonstrate that \u03947\/11 is a novel regulatory mechanism of prolactin bioavailability and signaling.<\/jats:p>","DOI":"10.1530\/jme-12-0201","type":"journal-article","created":{"date-parts":[[2012,10,10]],"date-time":"2012-10-10T12:27:28Z","timestamp":1349872048000},"page":"79-90","update-policy":"https:\/\/doi.org\/10.1530\/crossmarkpolicy-1","source":"Crossref","is-referenced-by-count":8,"title":["Characterization of \u03947\/11, a functional prolactin-binding protein"],"prefix":"10.1530","volume":"50","author":[{"given":"J M","family":"Fleming","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"E","family":"Ginsburg","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"C W","family":"McAndrew","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"C D","family":"Heger","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"L","family":"Cheston","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"J","family":"Rodriguez-Canales","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"B K","family":"Vonderhaar","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"P","family":"Goldsmith","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"416","reference":[{"issue":"5","key":"1_14521005","doi-asserted-by":"crossref","first-page":"712","DOI":"10.1002\/ijc.2910550503","volume":"55","author":"Banerjee","year":"1993","journal-title":"International journal of cancer. 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