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

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Part of the book series: Developments in Molecular and Cellular Biochemistry ((DMCB,volume 16))

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.

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References

  1. Dubyak GR, Kleinzeller A: The insulin-mimetic effects of vanadate in isolated rat adipocytes. J Biol Chem 255: 5306–5312, 1980

    PubMed  CAS  Google Scholar 

  2. Shechter Y, Karlish SJD: Insulin-like stimulation of glucose oxidation in rat adipocytes by vanadyl ions (IV) ions. Nature 284: 556–558, 1980

    Article  PubMed  CAS  Google Scholar 

  3. Shechter Y, Ron A: Effect of depletion of phosphate and bicarbonate ions on insulin action in rat adipocytes. J Biol Chem 261: 14945–14950, 1986

    PubMed  CAS  Google Scholar 

  4. Degani H, Gochin M, Karlish SJD, Shechter Y: Electron paramagnetic studies and insulin-like effects of vanadium in rat adipocytes. Biochemistry 20: 5795–5799, 1981

    Article  PubMed  CAS  Google Scholar 

  5. Shechter Y: Insulin mimetic effects of vanadate; possible implications toward the future treatment of diabetes. Diabetes ‘Perspective in Diabetes’ 39: 1–5, 1990

    CAS  Google Scholar 

  6. Cantley LG, Aisen P: The.fate of cytoplasmic vanadium. Implication of (Na+, K+) ATPase inhibition. J Biol Chem 254: 1781–1784, 1979

    PubMed  CAS  Google Scholar 

  7. Simons TJB: Vanadate — a new tool for biologists. Nature 281: 337–338, 1979

    Article  PubMed  CAS  Google Scholar 

  8. Makara IG: Vanadium — an element in search of a role. Trends Biochem 5: 92–94, 1980

    Article  Google Scholar 

  9. Cantley LC, Resh MD, Guidotti G: Vanadate inhibits the red cell (Na+, K+)ATPase from the cytoplasmic side. Nature 272: 552–554, 1978

    Article  PubMed  CAS  Google Scholar 

  10. Mondon EC, Dolkas CB, Olefsky JM, Reaven GM: Insulin sensitivity of isolated perfused rat liver. Diabetes 24: 225–229, 1974

    Article  Google Scholar 

  11. Kahn RC, Shechter Y: In: A.G. Gilman, T.W. Rail, A.S. Nies, and P. Taylor (eds). Insulin, oral hypoglycemic agents, and the pharmacology of the endocrine pancreas. Goodman and Gilman Text Book of Pharmacology, Eighth edition, Chapter 61, Pergamon Press, 1990, pp 1463–1495

    Google Scholar 

  12. Bruck R, Prigozin H, Krepel Z, Rotenberg P, Shechter Y, Bar-Meir S: Vanadate inhibits glucose-output from isolated perfused rat liver. Hepatology 14: 540–544, 1991

    Article  PubMed  CAS  Google Scholar 

  13. Heyliger CE, Tahiliani AG, McNeill JH: Effect of vanadate on elevated blood glucose and depressed cardiac performance of diabetic rats. Science 227: 1474–1476, 1985

    Article  PubMed  CAS  Google Scholar 

  14. Hirsova D, Koldovsky O: On the question of the absorption of insulin from the gastrointestinal tract during postnatal development. Physiolog Bohemoslov 18: 281–284, 1969

    CAS  Google Scholar 

  15. Meyerovitch J, Farfel Z, Sack J, Shechter Y: Oral administration of vanadate normalizes blood glucose levels in streptozotocin-treated rats: Characterization and mode of action. J Biol Chem 262: 6658–6662, 1987

    PubMed  CAS  Google Scholar 

  16. Gil J, Miralpeix M, Carreras J, Bartrons R: Insulin-like effects of vanadate on glucokinase activity and fructose 2.6 bisphosphate levels in the liver of diabetic rats. J Biol Chem 263: 1868–1871, 1988

    PubMed  CAS  Google Scholar 

  17. Kobayashi M, Olefsky JM: Effects of streptozotocin-induced diabetes on insulin binding, glucose transport, and intracellular glucose metabolism in isolated rat adipocytes. Diabetes 28: 87–95, 1979

    PubMed  CAS  Google Scholar 

  18. Meyerovitch J, Rothenberg P, Shechter Y, Bonner-Weir SA, Kahn CR: Vanadate normalizes hyperglycemia in two mouse models of non-insulin-dependent diabetes mellitus. J Clin Invest 87: 1286–1294, 1991

    Article  PubMed  CAS  Google Scholar 

  19. Ramanadham S, Brownsey RW, Cross GH, Mongold JJ, McNeil, JH: Sustained prevention of myocardial metabolic abnormalities in diabetic rats following withdrawal from oral vanadyl treatment. Metabolism 38: 1022–1028, 1989

    Article  PubMed  CAS  Google Scholar 

  20. Brichard SM, Poltier AM, Henquin JC: Long term improvement of glucose homeostasis by vanadate in obese hyperinsulinemic fa/fa rats. Endocrinology 125: 2510–2516, 1989

    Article  PubMed  CAS  Google Scholar 

  21. Brichard SM, Assimacopoulos-Jeannet F, Jeanrenaud B: Vanadate treatment markedly increases glucose utilization in muscle of insulin-resistant fa/fa rats without modifying glucose transporter expression. Endocrinology 131: 311–317, 1992

    Article  PubMed  CAS  Google Scholar 

  22. Czech MP: The nature and regulation of the insulin receptor structure and function. Ann Rev Physiol 47: 357–381, 1985

    Article  CAS  Google Scholar 

  23. Ebina Y, Ellis L, Jarmagin K, Standring D, Beaudoin J, Roth RA, Rutter WJ: The human insulin receptor cDNA: The structural basis for hormone-activated transmembrane signalling. Cell 40: 7447–7458, 1985

    Article  Google Scholar 

  24. Kahn CR, White MF: The insulin receptor and the molecular mechanism of insulin action. J Clin Invest 82: 1151–1156, 1988

    Article  PubMed  CAS  Google Scholar 

  25. Shechter Y, Yaish P, Chorev M, Gilon C, Braun S, Levitzki A: Inhibition of insulin-dependent lipogenesis and anti-lipolysis by protein tyrosine kinase inhibitors. EMBO J 8: 1671–1676, 1989

    PubMed  CAS  Google Scholar 

  26. Shisheva A, Shechter Y: Quercetin selectively inhibits insulin receptor function in vitro and the bioresponses of insulin and insulinomimetic agents in rat adipocytes. Biochemistry 31: 8059–8063, 1992

    Article  PubMed  CAS  Google Scholar 

  27. Gottschalk WK: The pathway mediating insulin’s effects on pyruvate dehydrogenase bypasses the insulin receptor tyrosine kinase. J Biol Chem 266: 8814–8819, 1991

    PubMed  CAS  Google Scholar 

  28. Shoelson SE, Kahn CR: Phosphorylation, the insulin receptor, and insulin action. In: M. Draznin, S. Melmed and D. LeRoith, (eds). Molecular and Cellular Biology of Diabetes Mellitus. Alan R. Liss, New York, Vol. II, 1989, pp. 23–33.

    Google Scholar 

  29. Swarup G, Speeg KV Jr, Cohen S, Garbers DL: Phosphotyrosyl protein phosphatase of TCRC-2 cells. J Biol Chem 257: 7298–7301, 1982

    PubMed  CAS  Google Scholar 

  30. Hunter T, Sefton BM: Transforming gene product of rous sarcoma virus phosphorylates tyrosine. Proc Natl Acad Sci USA 77: 1311–1315, 1980

    Article  PubMed  CAS  Google Scholar 

  31. Srivastava A: Non-receptor protein tyrosine kinases of normal tissues. Intl J Biochem 11: 1229–1234, 1990

    Article  Google Scholar 

  32. Shisheva A, Shechter Y: A cytosolic protein tyrosine kinase in rat adipocytes. FEBS Lett 300: 93–96, 1991

    Article  Google Scholar 

  33. Shisheva A, Shechter Y: Role of cytosolic tyrosine kinase in mediating insulin-like actions of vanadate in rat adipocytes. J Biol Chem 268: 6463–3469, 1993

    PubMed  CAS  Google Scholar 

  34. Elberg G, Li J, Shechter Y: Vanadium activates or inhibits receptor and non-receptor protein tyrosine kinases in cell-free experiments, depending on its oxidation state. Possible role of endogenous vanadium in controlling celllular protein tyrosine kinase activity. J Biol Chem 269: 9521–9527, 1994

    PubMed  CAS  Google Scholar 

  35. Liochev S, Fridovich I: The oxidation of NADH by tetravalent vanadium. Arch Biochem Biophys 255: 274–278, 1987

    Article  PubMed  CAS  Google Scholar 

  36. Trudel S, Downey GP, Grienstein S, Paquet MC: Activation of permeabilized HL60 cells by vanadate. Evidence for diverged signal pathways. Biochem J 269: 127–131, 1990

    PubMed  CAS  Google Scholar 

  37. Grinstein S, Furuya W, Lu DJ, Mills BG: Vanadate stimulates oxygen consumption and tyrosine phosphorylation in electropermeabilized human neutrophils. J Biol Chem 265: 318–327, 1990

    PubMed  CAS  Google Scholar 

  38. Lau KHW, Farley JR, Baylink DJ: Review article: Phosphotyrosyl protein phosphatases. Biochem J 257: 23–36, 1989

    PubMed  CAS  Google Scholar 

  39. Fantus IG, Kadota S, Deragon G, Foster D, Posner BI: Pervanadate [peroxide(s) of vanadate] mimics insulin action in rat adipocytes via activation of the insulin-receptor tyrosine kinase. Biochemistry 28: 8864–8871, 1989

    Article  PubMed  CAS  Google Scholar 

  40. Carbonneau H, Tonks NK: 1002 Protein phosphatases? Annu Rev Cell Biol 8: 463–493, 1992

    Google Scholar 

  41. Walton KM, Dixon JE: Protein tyrosine phosphatases. Ann Rev Biochem 62: 101–120, 1993

    Article  PubMed  CAS  Google Scholar 

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© 1995 Kluwer Academic Publishers

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Shechter, Y. et al. (1995). Insulin-like actions of vanadate are mediated in an insulin-receptor-independent manner via non-receptor protein tyrosine kinases and protein phosphotyrosine phosphatases. In: Srivastava, A.K., Chiasson, JL. (eds) Vanadium Compounds: Biochemical and Therapeutic Applications. Developments in Molecular and Cellular Biochemistry, vol 16. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-1251-2_5

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  • DOI: https://doi.org/10.1007/978-1-4613-1251-2_5

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4612-8533-5

  • Online ISBN: 978-1-4613-1251-2

  • eBook Packages: Springer Book Archive

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