RGD Reference Report - Characterization of a natural inhibitor of the insulin receptor tyrosine kinase: cDNA cloning, purification, and anti-mitogenic activity. - Rat Genome Database

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

Authors: Auberger, P  Falquerho, L  Contreres, JO  Pages, G  Le Cam, G  Rossi, B  Le Cam, A 
Citation: Auberger P, etal., Cell 1989 Aug 25;58(4):631-40.
RGD ID: 632173
Pubmed: PMID:2766355   (View Abstract at PubMed)

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.



Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
AhsgRatnegative regulation of cell growth  IDA  RGD 
AhsgRatnegative regulation of insulin receptor signaling pathway  IDA  RGD 

Molecular Function

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
AhsgRatreceptor signaling protein tyrosine kinase inhibitor activity  IDA  RGD 

Objects Annotated

Genes (Rattus norvegicus)
Ahsg  (alpha-2-HS-glycoprotein)


Additional Information