Insulin-like actions of vanadate are mediated in an insulin-receptor-independent manner via non-receptor protein tyrosine kinases and protein phosphotyrosine phosphatases

Yoram Shechter, Jingping Li, Joseph Meyerovitch, Dov Gefel, Rafael Bruck, Gerard Elberg, David S. Miller, Assia Shisheva

Research output: Contribution to journalArticlepeer-review

Abstract

Most or all mammalian cells contain vanadium at a concentration of 0.1-1.0 μM. The bulk of the vanadium in cells is probably in the reduced vanadyl (IV) form. Although this element is essential and should be present in the diet in minute quantities, no known physiological role for vanadium has been found thus far. In the years 1975-1980 the vanadate ion was shown to act as an efficient inhibitor of Na+,K+-ATPase and of other related phosphohydrolyzes as well. In 1980 it was observed that vanadate vanadyl, when added to intact rat adipocytes, mimics the biological actions of insulin in stimulating hexose uptake and glucose oxidation. This initiated a long, currently active, field of research among basic scientists and diabetologists. Several of the aspects studied are reviewed here.

Original languageEnglish
Pages (from-to)39-47
Number of pages9
JournalMolecular and Cellular Biochemistry
Volume153
Issue number1-2
DOIs
StatePublished - Dec 1995
Externally publishedYes

Keywords

  • cytosolic protein tyrosine kinase
  • insulin action
  • molybdate-permolybdate
  • protein phosphotyrosine phosphatase
  • tungstate-pertungstate
  • vanadium salts

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