Basic fibroblast growth factor is a substrate for phosphorylation by human neutrophil ecto-protein kinase activity

Keith M Skubitz, Said A. Goueli

Research output: Contribution to journalArticlepeer-review

14 Scopus citations

Abstract

Basic fibroblast growth factor (FGF) has recently been shown to be a phosphoprotein and its receptor affinity is modified by phosphorylation. Since most studies of protein phosphorylation have focused on intracellular protein kinases, a physiologic mechanism of the regulation of basic FGF activity by phosphorylation has been unclear. Evidence for the existence of ecto-protein kinase activity on the surface of several types of cells including human neutrophils has been described. These ecto-protein kinase activities utilize exogenous ATP to phosphorylate exogenous as well as endogenous cell-surface proteins. This report demonstrates that human basic FGF is phosphorylated on serine by human neutrophil ecto-protein kinase activity and this phosphorylation is inhibited by heparin. Regulation of basic FGF activity by phosphorylation may be one of the functions of ecto-protein kinase activity.

Original languageEnglish (US)
Pages (from-to)49-55
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume174
Issue number1
DOIs
StatePublished - Jan 15 1991

Bibliographical note

Funding Information:
*Supported in part by National Institutes of Health Grant CA36248, the Leukemia Task Force, and the Masonic Memorial Hospital Fund, Inc. §To whom correspondences hould be addressed. Abbreviations: FGF, fibroblast growth factor; PKA, CAMP-dependent protein kinase; PKC, calcium-dependent and phospholipid-dependent protein kinase; HBSS, Hanks’ balanced salt solution, pH 7.4; NaCl-HEPES, 145 mM NaCl, 20 mM N-2-hydroxyethylpiperazine-N’-2-ethanesulfonica cid, pH 7.4; PAGE, polyacrylamide gel electrophoresis;P VDF, Immobilon-P, PS, phosphoserine;P -T, phosphothreonine;P -Y, phosphotyrosine.

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