Chromium oligopeptide activates insulin receptor tyrosine kinase activity

Biochemistry. 1997 Apr 15;36(15):4382-5. doi: 10.1021/bi963154t.


A possible new mechanism for the amplification of insulin receptor tyrosine kinase activity in response to insulin has been identified. The chromium-containing oligopeptide low molecular weight chromium-binding substance (LMWCr) does not effect the tyrosine protein kinase activity of rat adipocytic membrane fragments in the absence of insulin; however, insulin-stimulated kinase activity in the membrane fragments is increased up to 8-fold by the oligopeptide. Using isolated rat insulin receptor, LMWCr has been shown to bind to insulin-activated insulin receptor with a dissociation constant of circa 250 pM, resulting in the increase of its tyrosine protein kinase activity. The ability of LMWCr to stimulate insulin receptor tyrosine kinase activity is dependent on its chromium content. The results appear to explain the previously poorly understood relationship between chromium and adult-onset diabetes and cardiovascular disease.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adipocytes / enzymology
  • Animals
  • Chromium Compounds / pharmacology*
  • Enzyme Activation / drug effects
  • Male
  • Molecular Weight
  • Oligopeptides / pharmacology*
  • Protein-Tyrosine Kinases / chemistry
  • Protein-Tyrosine Kinases / drug effects
  • Protein-Tyrosine Kinases / metabolism*
  • Rats
  • Rats, Sprague-Dawley
  • Receptor, Insulin / chemistry
  • Receptor, Insulin / metabolism*


  • Chromium Compounds
  • Oligopeptides
  • Protein-Tyrosine Kinases
  • Receptor, Insulin