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      Characterization of a natural inhibitor of the insulin receptor tyrosine kinase: cDNA cloning, purification, and anti-mitogenic activity.

      Cell

      Acute-Phase Proteins, Amino Acid Sequence, Amino Acids, metabolism, Animals, Base Sequence, Cell Division, drug effects, Cloning, Molecular, DNA, genetics, Glycoproteins, isolation & purification, Insulin Antagonists, pharmacology, Liver Neoplasms, Experimental, Molecular Sequence Data, Phosphoproteins, Phosphorylation, Protein-Tyrosine Kinases, antagonists & inhibitors, Rats, Receptor, Insulin

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          Abstract

          Amino acid sequence of the precursor of the phosphorylated N-glycoprotein (pp63) secreted by rat hepatocytes was deduced from the cDNA sequence. This polypeptide (Mr = 40,586) was rich in both cysteine and proline and contained three potential N-glycosylation sites. A single pp63 mRNA species (approximately 2000 bp), found in normal hepatocytes but not in FaO hepatoma cells, appeared to result from transcription of a single gene. pp63 purified by affinity chromatography inhibited insulin receptor tyrosine kinase and receptor autophosphorylation. Only the phosphorylated form of the protein was active. In additon, pp63 antagonized the growth-promoting action of insulin in FaO cells but did not affect hormone-mediated increase in amino acid transport capacity or tyrosine aminotransferase induction in these cells.

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          2766355

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