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Pinopsin is a chicken pineal photoreceptive molecule

Abstract

IN avian pinealocytes, an environmental light signal resets the phase of the endogenous circadian pacemaker that controls the rhythmic production of melatonin1–6. Investigation of the pineal phototransduction pathway should therefore reveal the molecular mechanism of the biological clock. The presence of rhodopsin-Iike photoreceptive pigment4,5 7–9, transducin-like immunoreaction10, and cyclic GMP-dependent cation-channel activity11 in the avian pinealocytes suggests that there is a similarity between retinal rod cells and pinealocytes in the phototransduction pathway. We have now cloned chicken pineal cDNA encoding the photoreceptive molecule, which is 43–48% identical in amino-acid sequence to vertebrate retinal opsins. Pineal opsin, produced by transfection of complementary DNA into cultured cells, was reconstituted with 11-cis-retinal, resulting in formation of a blue-sensitive pigment λmax ≈470 nm). In the light of this functional evidence and because the gene is specifically expressed only in the pineal gland, we con-clude that it is a pineal photosensor and name it pinopsin.

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References

  1. Binkley, S. A., Riebman, J. B. & Reilly, K. B. Science 202, 1198–1201 (1978).

    Article  ADS  CAS  PubMed  Google Scholar 

  2. Kasal, C. A., Menaker, M. & Prez-Polo, J. R. Science 203, 656–658 (1979).

    Article  ADS  CAS  PubMed  Google Scholar 

  3. Deguchi, T. Science 203, 1245–1247 (1979).

    Article  ADS  CAS  PubMed  Google Scholar 

  4. Deguchi, T. Nature 290, 706–707 (1981).

    Article  ADS  CAS  PubMed  Google Scholar 

  5. Wallingford, J. C. & Zats, M. Exp. Eye Res. 46, 909–918 (1988).

    Article  CAS  PubMed  Google Scholar 

  6. Takahashi, J. S., Murakami, N., Nikaido, S. S., Pratt, B. L. & Robertson, L. M. Rec. Progr. Horm. Res. 45, 279–352 (1989).

    CAS  PubMed  Google Scholar 

  7. Foster, R. G., Schalken, J. J., Timmers, A. M. & DeGrip, W. J. J. comp. Physiol. A 165, 553–563 (1989).

    Article  Google Scholar 

  8. Araki, M., Fukada, Y., Shichida, Y., Yoshizawa, T. & Tokunaga, F. Devl Brain Res. 65, 85–92 (1992).

    Article  CAS  Google Scholar 

  9. Masuda, H. et al. Tiss. Cell 26, 101–113 (1994).

    Article  CAS  Google Scholar 

  10. van Veen, T. et al. Proc. natn. Acad. Sci. U.S.A. 83, 912–916 (1986).

    Article  ADS  CAS  Google Scholar 

  11. Dryer, S. E. & Henderson, D. Nature 353, 756–758 (1991).

    Article  ADS  CAS  PubMed  Google Scholar 

  12. Kuwata, O. et al. FEBS Lett. 272, 128–132 (1990).

    Article  CAS  PubMed  Google Scholar 

  13. Okano, T., Kojima, D., Fukada, Y., Shichida, Y. & Yoshizawa, T. Proc. natn. Acad. Sci. U.S.A. 89, 5932–5936 (1992).

    Article  ADS  CAS  Google Scholar 

  14. Saitou, N. & Nei, M. Molec. Biol. Evol. 4, 406–425 (1987).

    CAS  PubMed  Google Scholar 

  15. Kojima, D. et al. Proc. natn. Acad. Sci. U.S.A. 89, 6941–6845 (1992).

    Article  Google Scholar 

  16. Sun, J.-H., Reiter, R. J., Mata, N. L. & Tsin, A. T. C. Neurosci. Lett. 133, 97–99 (1991).

    Article  CAS  PubMed  Google Scholar 

  17. Okano, T., Fukada, Y., Artamonov, I. D. & Yoshizawa, T. Biochemistry 28, 8848–8856 (1989).

    Article  CAS  PubMed  Google Scholar 

  18. Zats, M. & Mullen, D. A. Brain Res. 453, 63–71 (1988).

    Article  Google Scholar 

  19. Takao, M., Yasui, A. & Tokunaga, F. Vision Res. 28, 471–480 (1988).

    Article  CAS  PubMed  Google Scholar 

  20. Sambrook, J., Fritsch, E. F. & Maniatis, T. Molecular Cloning: A Laboratory Manual 2nd edn (Cold Spring Harbor Laboratory Press, New York, 1989).

    Google Scholar 

  21. Nathans, J. Biochemistry 29, 9746–9752 (1990).

    Article  CAS  PubMed  Google Scholar 

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Okano, T., Yoshizawa, T. & Fukada, Y. Pinopsin is a chicken pineal photoreceptive molecule. Nature 372, 94–97 (1994). https://doi.org/10.1038/372094a0

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