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Heparin-Binding Property of Human Prolactin: A Novel Aspect of Prolactin Biology

Department of Cell Biology, University of Cincinnati Medical School, Cincinnati, Ohio 45267

Address all correspondence and requests for reprints to: Nira Ben-Jonathan, Ph.D., University of Cincinnati, Department of Anatomy and Cell Biology, 231 Bethesda Avenue (ML 521), Cincinnati, Ohio 45267.

	Abstract

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Prolactin (PRL) shares several characteristics with growth factors and cytokines, many of which are known to bind to heparan sulfate proteoglycans. In this study we examined the heparin-binding properties of selected members of the PRL/GH family, using heparin affinity columns followed by gel electrophoresis/Western blotting. Purified human PRL and its cleaved 16K fragment, but not human GH or placental lactogen, were retained on the heparin column and were displaced by 0.5 M NaCl. Native PRL in human pituitary extracts and amniotic fluid showed a similar binding affinity to heparin as the purified hormone. None of the other hormones tested, e.g., rat, ovine and bovine PRL, glycosylated ovine PRL or rat GH, bound to heparin. Two consensus heparin-binding sequences are present in human PRL but not in the other hormones included in this study. We postulate that the heparin-binding capability of PRL affects its biological activity as a growth factor and the angiostatic actions of its 16K fragment.

Received October 6, 1998.

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This Article Abstract Full Text (PDF) Purchase Article View Shopping Cart Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Copyright Permission Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Khurana, S. Articles by Ben-Jonathan, N. Search for Related Content PubMed PubMed Citation Articles by Khurana, S. Articles by Ben-Jonathan, N.