Skip to main content

Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

  • Letter
  • Published:

Calcitonin selectively stimulates 25-hydroxyvitamin D3-1α-hydroxylase in proximal straight tubule of rat kidney

Abstract

We have reported previously that the 25-hydroxyvitamin D3 (25(OH)D3)-1α-hydroxylase (1α(OH)ase) activity was localized exclusively in the proximal convoluted tubules (PCT) in mature vitamin D-deficient rats and that the enzyme activity was largely abolished by parathyroidectomy in the vitamin D-deficient rats with presumed secondary hyperparathyroidism1. However Akiba et al.2 found enzyme activity in both PCT and the proximal straight tubules (PST) of the fetal rabbit kidney. Parathyroid hormone and calcitonin, when given in vivo, can stimulate the production of 1α, 25(OH)2D3 from 25(OH)D3 in vitamin D-deficient rats3–6, and, moreover, their in vivo effects on the 1α(OH)ase in thyroparathyroidectomized vitamin D-deficient rats are additive6, a finding consistent with different sites of action of these two hormones. In addition, plasma calcitonin levels are elevated in the fetus of several mammalian species7–10, while they are likely to be low in hypocalcaemic vitamin D-deficient rats. From these observations, we hypothesized that calcitonin could be responsible for stimulating enzyme activity in the PST while parathyroid hormone primarily activates 1α(OH)ase in the PCT. To test this hypothesis, we examined the effect of calcitonin on the 1α(OH)ase activity in defined nephron segments of vitamin D-deficient rats. We report here that the hormone selectively stimulates 1α(OH)ase activity in the PST, whereas this enzyme activity is undetectable in control vitamin D-deficient animals.

This is a preview of subscription content, access via your institution

Access options

Buy this article

Prices may be subject to local taxes which are calculated during checkout

Similar content being viewed by others

References

  1. Kawashima, H., Torikai, S. & Kurokawa, K. Proc. natn. Acad. Sci. U. S. A 78, 1199–1203 (1981).

    Article  ADS  CAS  Google Scholar 

  2. Akiba, T., Endou, H., Koseki, C., Sakai, F., Horiuchi, N. & Suda, T. Biochem. Biophys. Res. Commun. 94, 313–318 (1980).

    Article  CAS  Google Scholar 

  3. Galante, L., Colston, K. W., MacAuley, S. J. & MacIntyre, I. Nature 238, 271–273 (1972).

    Article  ADS  CAS  Google Scholar 

  4. Lorenc, R., Tanaka, Y., DeLuca, H. F. & Jones, G. Endocrinology 100, 468–472 (1977).

    Article  CAS  Google Scholar 

  5. Horiuchi, N., Suda, T., Takahashi, H., Shimazawa, E. & Ogata, E. Endocrinology 101, 969–974 (1977).

    Article  CAS  Google Scholar 

  6. Horiuchi, N. et al. Biochem. J. 184, 269–275 (1979).

    Article  CAS  Google Scholar 

  7. Garel, J-M., Savajol, H. & Barlet, J.-P. Biol. Neonate 28, 207–218 (1976).

    Article  CAS  Google Scholar 

  8. Garel, J.-M, Martin-Rosset, W. & Barlet, J.-P. Horm. Metab. Res. 7, 429–432 (1975).

    Article  CAS  Google Scholar 

  9. Reynolds, W. A. et al. Metabolism 51, 595–598 (1980).

    CAS  Google Scholar 

  10. Samaan, N. A., Anderson, G. D. & Adam-Mayne, M. E. Am. J. Obstet. Gynecol. 121, 622–626 (1975).

    Article  CAS  Google Scholar 

  11. Bligh, E. G. & Dyer, W. J. Can. J. Biochem. Physiol. 37, 911–917 (1959).

    Article  CAS  Google Scholar 

  12. Chabardes, D., Imbert-Teboul, M., Montegut, M., Clique, A. & Morel, F. Proc. natn. Acad. Sci. U.S.A. 73, 3608–3612 (1976).

    Article  ADS  CAS  Google Scholar 

  13. Larkins, R. G. et al. Clin. Sci. molec. Med. 46, 569–582 (1974).

    CAS  Google Scholar 

  14. Imbert, M., Chabardes, D., Montegut, M., Clique, A. & Morel, F. Pflügers Arch. ges. Physiol. 354, 213–228 (1975).

    Article  CAS  Google Scholar 

  15. Torikai, S. & Imai, M. Tohoku J. exp. Med. 129, 91–99 (1979).

    Article  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Kawashima, H., Torikai, S. & Kurokawa, K. Calcitonin selectively stimulates 25-hydroxyvitamin D3-1α-hydroxylase in proximal straight tubule of rat kidney. Nature 291, 327–329 (1981). https://doi.org/10.1038/291327a0

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1038/291327a0

This article is cited by

Comments

By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.

Search

Quick links

Nature Briefing

Sign up for the Nature Briefing newsletter — what matters in science, free to your inbox daily.

Get the most important science stories of the day, free in your inbox. Sign up for Nature Briefing