Letter | Published:

Vanadate inhibits the red cell (Na+, K+) ATPase from the cytoplasmic side

Nature volume 272, pages 552554 (06 April 1978) | Download Citation

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Abstract

THE enzyme (Na+, K+)ATPase exists in the plasma membrane of animal cells and maintains a high intracellular K+-to-Na+ ratio by coupling movement of these ions to the hydrolysis of ATP. This enzyme spans the plasma membrane1 and is asymmetrically positioned with the ATP hydrolysing site on the cytoplasmic side2. Cardiac glycosides inhibit the (Na+, K+)-ATPase by binding to the part of the enzyme facing the extracellular fluid3. Although there is considerable evidence that hormonal regulation of (Na+, K+)ATPase occurs in certain tissues4–8, no endogenous regulatory agents of the purified enzyme have been identified. Recently we discovered that vanadate (vanadium in the +5 oxidation state) inhibits purified (Na+, K+)ATPase from several tissues at concentrations of 10−7–10−8 M (refs 9,10). Vanadium has been established as a nutritional requirement in chickens and rats, and our estimates of the concentration of vanadium in muscle tissue (10−6–10−7 M) agree with concentrations measured in other tissues11. It is known that vanadate has properties similar to those of the phosphate ion12, and it therefore seemed likely that it might inhibit the enzyme by binding to the hydrolysis site which is on the cytoplasmic surface of the enzyme. We demonstrate here that vanadate is transported into the red cell and inhibits the (Na+, K +)ATPase from the cytoplasmic side.

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References

  1. 1.

    J. biol. Chem. 250, 7443–7449 (1975).

  2. 2.

    & J. biol. Chem 239, 345–352 (1964).

  3. 3.

    & Biochim. biophys. Acta 291, 680–689 (1973).

  4. 4.

    & J. Physiol., Lond. 265, 19–42 (1977).

  5. 5.

    & J. Physiol., Lond. 270, 383–414 (1977).

  6. 6.

    & J. Physiol., Lond. 270, 415–430 (1977).

  7. 7.

    , & Nature 260, 546–547 (1976).

  8. 8.

    , & Biochem. biophys. Res. Commun. 71, 136–143 (1976).

  9. 9.

    & Biochemistry 16, 4572–4578 (1977).

  10. 10.

    et al. J. biol. Chem. 252, 7421–7423 (1977).

  11. 11.

    in Truce Elements in Human and Animal Nutrition 354 (Academic, London, 1962).

  12. 12.

    , & J. Am. chem. Soc. 95, 8762–8768 (1973).

  13. 13.

    & J. Membr. Biol. 10, 311–330 (1972).

  14. 14.

    & Biochemistry 12, 4900–4904 (1973).

  15. 15.

    , & Archs Biochem. Biophys 100, 119–130 (1973).

  16. 16.

    & Nature 000, 000–000 (1978).

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Author information

Affiliations

  1. Department of Biochemistry and Molecular Biology, Harvard University, The Biological Laboratories, 16 Divinity Ave., Cambridge, Massachusetts 02138

    • LEWIS C. CANTLEY JR
    • , MARILYN D. RESH
    •  & GUIDO GUIDOTTI

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DOI

https://doi.org/10.1038/272552a0

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