Phosphorylation of prolactin

W. S. Oetting, P. T. Tuazon, J. A. Traugh, A. M. Walker

Research output: Contribution to journalArticlepeer-review

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Abstract

Rat prolactin exhibits microheterogeneity when examined in electrophoretic systems, running as three isoforms having the same molecular weight but different net charges (prolactins 1, 2, and 3 with isoform 3 being the most acidic). As there is precedent for the phorphorylation of a pituitary hormone and phosphorylation is a common cause of microheterogeneity, we examined the possibility that rat prolactin existed in differentially phosphorylated forms. The investigation included examinations of rat prolactin phosphorylation both in vitro and in vivo. For the in vitro studies, purified rat prolactin was incubated with [γ-32P]ATP and low levels of each of five purified protein kinases. Phosphorylated rat prolactin was identified by autoradiography of silver-stained one- and two-dimensional gels. For the in vivo studies, rat anterior pituitary cells in primary culture were incubated in the presence of H3 32PO4 for 2 or 12 h, after which time the proteins were extracted from the cells, cold acetone-precipitated, or immunoprecipitated and run on two-dimensional gels. We report (a) the in vitro phosphorylation of rat prolactin by cAMP-dependent protein kinase, casein kinase I, protease-activated kinase I, and the calcium/phospholipid-dependent kinase, (b) that phosphorylation with these kinases results in phosphate incorporation only into isoforms 2 and 3, and (c) the phosphorylation of prolactin in rat pituitary cells in primary culture.

Original languageEnglish (US)
Pages (from-to)1649-1652
Number of pages4
JournalJournal of Biological Chemistry
Volume261
Issue number4
StatePublished - 1986

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