Heparin-binding property of human prolactin: a novel aspect of prolactin biology.

Abstract:

: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.

journal_name

Endocrinology

journal_title

Endocrinology

authors

Khurana S,Kuns R,Ben-Jonathan N

doi

10.1210/endo.140.2.6677

subject

Has Abstract

pub_date

1999-02-01 00:00:00

pages

1026-9

issue

2

eissn

0013-7227

issn

1945-7170

journal_volume

140

pub_type

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