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

Keith M Skubitz; Said A. Goueli

doi:10.1016/0006-291X(91)90483-N

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

Keith M Skubitz
, Said A. Goueli

Medicine - Hematology, Oncology, Transplant

Research output: Contribution to journal › Article › peer-review

20 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 language	English (US)
Pages (from-to)	49-55
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	174
Issue number	1
DOIs	https://doi.org/10.1016/0006-291X(91)90483-N
State	Published - 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.

Publisher link

10.1016/0006-291X(91)90483-N

Find It

Find It at U of M Libraries

Cite this

@article{7a90433dc9db496782c3d3d1ada88e66,

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

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.",

author = "Skubitz, \{Keith M\} and Goueli, \{Said A.\}",

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{\textquoteright} balanced salt solution, pH 7.4; NaCl-HEPES, 145 mM NaCl, 20 mM N-2-hydroxyethylpiperazine-N{\textquoteright}-2-ethanesulfonica cid, pH 7.4; PAGE, polyacrylamide gel electrophoresis;P VDF, Immobilon-P, PS, phosphoserine;P -T, phosphothreonine;P -Y, phosphotyrosine.",

year = "1991",

month = jan,

day = "15",

doi = "10.1016/0006-291X(91)90483-N",

language = "English (US)",

volume = "174",

pages = "49--55",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

publisher = "Elsevier B.V.",

number = "1",

}

TY - JOUR

T1 - Basic fibroblast growth factor is a substrate for phosphorylation by human neutrophil ecto-protein kinase activity

AU - Skubitz, Keith M

AU - Goueli, Said A.

N1 - 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.

PY - 1991/1/15

Y1 - 1991/1/15

N2 - 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.

AB - 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.

UR - https://www.scopus.com/pages/publications/0026078967

UR - https://www.scopus.com/pages/publications/0026078967#tab=citedBy

U2 - 10.1016/0006-291X(91)90483-N

DO - 10.1016/0006-291X(91)90483-N

M3 - Article

C2 - 1989619

AN - SCOPUS:0026078967

SN - 0006-291X

VL - 174

SP - 49

EP - 55

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 1

ER -

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

Abstract

Bibliographical note

Publisher link

Find It

Other files and links

Fingerprint

Cite this