Direct modulation of insulin receptor protein tyrosine kinase by vanadate and anti-insulin receptor monoclonal antibodies

Roberto Gherzi, Cinzia Caratti, Gabriella Andraghetti, Stefano Bertolini, Antonio Montemurro, Giorgio Sesti, Renzo Cordera

Research output: Contribution to journalArticle


Sodium vanadate activates "in vitro" insulin receptor autophosphorylation and protein tyrosine kinase in a dose-dependent manner. Insulin receptor protein tyrosine kinase is directly activated also by the anti-insulin receptor beta subunit monoclonal antibody 18-44. We previously demonstrated that the anti-insulin receptor monoclonal antibody MA-10 decreases insulin-stimulated receptor protein tyrosine kinase activity "in vitro", without inhibiting insulin receptor binding. In this report we show that insulin receptor protein tyrosine kinase, activated by sodium vanadate or by monoclonal antibody 18-44, is inhibited by MA-10 antibody. These data suggest that insulin receptor protein tyrosine kinase activity can be either activated and inhibited through mechanisms different from insulin binding.

Original languageEnglish
Pages (from-to)1474-1480
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number3
Publication statusPublished - May 16 1988


ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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