Regulation of insulin receptor-associated tyrosine kinase by a polyclonal IgG

Roberto Gherzi, Renzo Cordera, Gabriella Andraghetti, Roberto De Pirro, Gary R. Freidenberg, Renato Lauro, Luciano Adezati

Research output: Contribution to journalArticle

Abstract

The effect of a polyclonal anti-insulin receptor antibody (pIgG) on the insulin receptor tyrosine kinase (IRTK) activity toward poly-(Glu-Tyr) was examined using wheat germ agglutinin agarose-purified insulin receptors from rat liver membranes. The main effect of pIgG was a reduction of Vmax (from 60.8 to 31.8 pmol/min/mg), without changes of Km, when IRTK was activated by insulin. In contrast, when IRTK was activated by ATP preincubation, pIgG was unable to affect the reaction, suggesting that IRTK possesses at least two regulatory mechanisms, one of which can be affected by pIgG.

Original languageEnglish
Pages (from-to)9-14
Number of pages6
JournalMolecular and Cellular Endocrinology
Volume53
Issue number1-2
DOIs
Publication statusPublished - 1987

Keywords

  • Anti-insulin receptor antibody
  • Insulin receptor
  • Tyrosine kinase

ASJC Scopus subject areas

  • Endocrinology
  • Endocrinology, Diabetes and Metabolism

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    Gherzi, R., Cordera, R., Andraghetti, G., De Pirro, R., Freidenberg, G. R., Lauro, R., & Adezati, L. (1987). Regulation of insulin receptor-associated tyrosine kinase by a polyclonal IgG. Molecular and Cellular Endocrinology, 53(1-2), 9-14. https://doi.org/10.1016/0303-7207(87)90186-9