Insulin receptor autophosphorylation and kinase activity in streptozotocin diabetic rats. Effect of a short fast

Roberto Gherzi, Gabriella Andraghetti, Eleuterio Ferrannini, Renzo Cordera

Research output: Contribution to journalArticle

Abstract

Insulin receptor associated kinase activity and its relationships with the insulin resistance of streptozotocin-induced diabetes were investigated in rats, using solubilized, partially purified insulin receptors from liver membranes. Insulin receptor kinase activity was measured by means of both autophosphorylation and phosphorylation of the exogenous substrate Glu4: Tyr1. Diabetes was associated with a 45% reduction in kinase activity, in the same number of insulin receptors, with no change in insulin binding affinity. To investigate the independent roles of hyperglycemia and hypoinsulinemia on the observed impairment of receptor kinase activity, diabetic rats were fasted for 24 h in order to normalize blood glucose levels only. After this short fast, no change in kinase activity, from the values measured in fed diabetic animals, was observed. Our findings suggest that streptozotocin diabetes is associated with a reduction of insulin receptor kinase activity, which a short fast is not able to reverse.

Original languageEnglish
Pages (from-to)850-856
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume140
Issue number3
DOIs
Publication statusPublished - Nov 14 1986

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Fingerprint Dive into the research topics of 'Insulin receptor autophosphorylation and kinase activity in streptozotocin diabetic rats. Effect of a short fast'. Together they form a unique fingerprint.

  • Cite this