Abstract
Receptors for Insulin, Epidermal Growth Factor, Platelet-Derived Growth Factor and Insulin-like Growth Factor type 1 are tyrosine-specific protein kinases. This enzymatic activity may play a role in mediating the biological actions of these peptides. It has recently been identified a Mr 120 KDa glycoprotein in rat liver plasma membranes which can be phosphorylated by the insulin receptor and by the EGF receptor in a cell-free system and by the insulin receptor in intact cultured H-35 hepatoma cells. In the present report it is shown that the solubilized Insulin-like Growth Factor type 1 receptor can phosphorylate tyrosine residues in the same 120 KDa glycoprotein from the AS-30D rat hepatoma cells.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Female
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Immunosorbent Techniques
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Insulin / pharmacology
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Insulin-Like Growth Factor I / pharmacology
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Liver Neoplasms, Experimental / enzymology*
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Membrane Glycoproteins / metabolism*
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Microsomes, Liver / analysis
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Molecular Weight
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Phosphorylation
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Phosphotyrosine
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Protein-Tyrosine Kinases / metabolism*
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Rats
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Rats, Inbred Strains
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Receptor, Insulin / metabolism*
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Receptors, Cell Surface / metabolism*
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Receptors, Somatomedin
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Tumor Cells, Cultured
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Tyrosine / analogs & derivatives
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Tyrosine / metabolism
Substances
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Insulin
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Membrane Glycoproteins
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Receptors, Cell Surface
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Receptors, Somatomedin
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Phosphotyrosine
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Tyrosine
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Insulin-Like Growth Factor I
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Protein-Tyrosine Kinases
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Receptor, Insulin