Linked Life Data

2168890

Source:http://linkedlifedata.com/resource/pubmed/id/2168890

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
27
pubmed:dateCreated
1990-10-18
pubmed:abstractText
Acidic fibroblast growth factor (aFGF) receptor was purified from plasma membranes of bovine liver using Triton X-100 extraction, wheat germ lectin-Sepharose 4B gel affinity chromatography, and DEAE-cellulose anion-exchange chromatography. As previously reported for the aFGF receptor in murine fibroblasts (Huang, S. S., and Huang, J. S. (1986) J. Biol. Chem. 261, 9568-9571), the purified aFGF receptor was also found to be a 135-kDa glycoprotein which showed an intrinsic and ligand-stimulated autophosphorylation activity. The 32P-labeled aFGF receptor was specifically immunoprecipitated by anti-FGF receptor (anti-flg/bek/cek gene product) antiserum. In contrast to other growth factor receptors/protein tyrosine kinases, the protein tyrosine kinase activity (autophosphorylation) of the aFGF receptor was stimulated (approximately 1.5-fold) by low concentrations of Mn2+, Mg2+, and Ca2+ (optimal concentrations of approximately 0.1, approximately 0.1, and 1 microM, respectively) but inhibited by higher concentrations of Mn2+, Mg2+, Ca2+, and pyrophosphate (greater than or equal to 20, greater than or equal to 50, greater than or equal to 10, and greater than or equal to 100 microM, respectively). However, addition of Mn2+ and pyrophosphate at a ratio of 1:1 not only reversed the inhibitory effect but also enhanced the kinase activity about 3-4-fold. The apparent Km of ATP for intrinsic and ligand-stimulated protein kinase activity of the aFGF receptor was estimated to be 25 microM. The preferred exogenous substrates for the protein tyrosine kinase activity of the aFGF receptor were found to be myelin basic protein and histone. Poly-L-arginine, an inhibitor for aFGF binding to the receptor, appeared to stimulate the mitogenesis or cell growth of responsive cells by mimicking aFGF activity.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
265
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
16455-63
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:2168890-Amino Acid Sequence, pubmed-meshheading:2168890-Animals, pubmed-meshheading:2168890-Cattle, pubmed-meshheading:2168890-Cell Membrane, pubmed-meshheading:2168890-Chromatography, Affinity, pubmed-meshheading:2168890-Chromatography, Ion Exchange, pubmed-meshheading:2168890-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:2168890-Fibroblast Growth Factors, pubmed-meshheading:2168890-Kinetics, pubmed-meshheading:2168890-Ligands, pubmed-meshheading:2168890-Liver, pubmed-meshheading:2168890-Membrane Glycoproteins, pubmed-meshheading:2168890-Molecular Sequence Data, pubmed-meshheading:2168890-Molecular Weight, pubmed-meshheading:2168890-Protein-Tyrosine Kinases, pubmed-meshheading:2168890-Receptors, Cell Surface, pubmed-meshheading:2168890-Receptors, Fibroblast Growth Factor
pubmed:year
1990
pubmed:articleTitle
Acidic fibroblast growth factor receptor purified from bovine liver is a novel protein tyrosine kinase.
pubmed:affiliation
Department of Biochemistry and Molecular Biology, St. Louis University School of Medicine, Missouri 63104.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't