Abstract
Heparin-binding growth factors (HBGFs) bind to high-affinity cell surface receptors which possess intrinsic tyrosine kinase activity. A Mr 150,000 protein phosphorylated on tyrosine in response to class 1 HBGF (HBGF-1) was purified and partially sequenced. On the basis of this sequence, cDNA clones were isolated from a human endothelial cell library and identified as encoding phospholipase C-gamma. Phosphorylation of phospholipase C-gamma in intact cells treated with HBGF-1 was directly demonstrated by using antiphospholipase C-gamma antibodies. Thus, HBGF-1 joins epidermal growth factor and platelet-derived growth factor, whose receptor activation leads to tyrosine phosphorylation and probable activation of phospholipase C-gamma.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Animals
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Base Sequence
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Cells, Cultured
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Cloning, Molecular
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DNA / genetics*
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DNA / isolation & purification
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Enzyme Activation
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Fibroblast Growth Factors / pharmacology*
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Gene Library
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Humans
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Isoenzymes / genetics
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Isoenzymes / metabolism
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Mice
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Mice, Inbred Strains
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Molecular Sequence Data
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Oligonucleotide Probes
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Phosphorylation
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Protein-Tyrosine Kinases / metabolism*
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Receptors, Cell Surface / metabolism*
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Receptors, Fibroblast Growth Factor
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Substrate Specificity
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Type C Phospholipases / genetics*
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Type C Phospholipases / metabolism
Substances
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Isoenzymes
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Oligonucleotide Probes
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Receptors, Cell Surface
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Receptors, Fibroblast Growth Factor
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Fibroblast Growth Factors
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DNA
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Protein-Tyrosine Kinases
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Type C Phospholipases