The Histochemical Journal

, Volume 22, Issue 1, pp 4–10 | Cite as

Expression of immunoreactivity for Ca-binding protein, spot 35 in the interstitial cell of the rat pineal organ

  • Miyuki Yamamoto
  • Hisatake Kondo
  • Tohru Yamakuni
  • Yasuo Takahashi
Papers
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Revised:

Summary

In the rat pineal organ numerous stellate cells exhibited intense immunoreactivity for calcium-binding spot 35 protein. Because of their peculiar shape and ultrastructure, identical to those of intrapineal S-100-immunoreactive cells, the spot 35-immunoreactive stellate cells were identified as the interstitial cells. The comparison of the morphology and population density of spot 35-, S-100-, and GFAP (glial fibrillar acidic protein)-immunoreactive cells, suggests that spot 35-immunoreactive cells represent a major subpopulation of the interstitial cells, all of which are S-100-immunoreactive and generally considered to be of glial nature, while GFAP-immunoreactive cells represent a minor subpopulation of the interstitial cells located in the proximal part close to the pineal stalk. This is the first report describing the occurrence of the calcium-binding protein in cells of glial nature.

Keywords

Population Density Acidic Protein Stellate Cell Proximal Part Interstitial Cell 
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References

  1. Baimbridge, K. G. &Miller, J. J. (1982) Immunohistochemical localization of calcium-binding protein in the cerebellum, hippocampus formation and olfactory bulb of the rat.Brain Res. 245, 223–9.CrossRefPubMedGoogle Scholar
  2. Bowie, E. P. &Herbert, D. C. (1976) Immunohistochemical evidence for the presence of arginine vasotocin in the rat pineal gland.Nature 261, 66.Google Scholar
  3. Carafoli, E. (1987) Intracellular calcium homeostasis.Annu. Rev. Biochem. 56, 395–433.PubMedGoogle Scholar
  4. Difiglia, M., Christakos, S. &Aromin, N. (1989) Ultrastructural localization of immunoreactive calbindin-D28k in the rat and monkey basal ganglia, including subcellular distribution with colloidal gold labelling.J. Comp. Neurol 279, 653–65.CrossRefPubMedGoogle Scholar
  5. Feldman, S. C. &Christakos, S. (1983) Vitamin D-dependent calcium-binding protein in rat brain: biochemical and immunocytochemical characterization.Endocrinol. 112, 290–302.Google Scholar
  6. Furness, J. B., Keast, J. R., Pompolo, S., Bornstein, J. C., Costa, M., Emson, P. C. &Lawson, D. e. M. (1988) Immunohistochemical evidence for the presence of calcium-binding proteins in the enteric neurons.Cell Tissue Res. 252, 79–87.CrossRefPubMedGoogle Scholar
  7. Heizmann, C. W. &Berchtold, M. W. (1987) Expression of parvalbumin and other Ca-binding proteins in normal and tumor cells: a topical review.Cell Calcium 8, 1–41.CrossRefPubMedGoogle Scholar
  8. Huang, S.-K., Nobiling, R., Schachner, M. &TaugnEr, R. (1984) Interstitial and parenchymal cells in the pineal gland of the golden hamster.Cell Tissue Res. 235, 327–37.PubMedGoogle Scholar
  9. Isobe, T., Ishioka, Masuda, T., Takahashi, Y., Ganno, S. &Okuyama, T. (1983) A rapid separation of S 100 subunits by high performance liquid chromatography: the subunit compositions of S 100 proteins.Biochem. Int. 6, 419–26.PubMedGoogle Scholar
  10. Kondo, H., Yamamoto, M., Yamakuni, T. &Takahashi, Y. (1988) An immunohistochemical study of the ontogeny of the horizontal cell in the rat retina using an antiserum against spot 35 protein, a novel Purkinje cell-specific protein, as a marker.Anat. Rec. 222, 103–9.CrossRefPubMedGoogle Scholar
  11. Legrand, Ch., Thomasset, M., Parkes, C. o., Clavel, M. C. &Rabie, A (1983) Calcium-binding protein in the developing rat cerebellum.Cell Tissue Res. 233, 389–402.CrossRefPubMedGoogle Scholar
  12. Luo, Z. R., Schultz, R. L., Whitter, E. F. &Vollrath, L. (1984) Ultrastructural characterization of glial cells in the rat pineal gland with special reference to the pineal stalk.Anat. Rec. 210, 663–74.CrossRefPubMedGoogle Scholar
  13. Møllers, M., Ingild, A. &Bock, E. (1978) Immunohistochemical demonstration of S-100 protein and GFA protein in interstitial cells of rat pineal gland.Brain Res. 140, 1–13.CrossRefPubMedGoogle Scholar
  14. Oksche, A. (1984) Evolution of the pineal complex: Correlation of structure and function.Ophthalmic Res. 16, 88–95.PubMedGoogle Scholar
  15. Philippe, E. &Droz, B. (1988) Calbindin D-28k-immunoreactive neurons in chick dorsal root ganglion: Ontogenesis and cytological characteristics of the immunoreactive sensory neurons.Neuroscience 26, 215–24.CrossRefPubMedGoogle Scholar
  16. Roman, A., Brisson, P., Pasteels, B., Demol, S., Pochet, R. &Collin, J. P. (1988) Pineal-retinal molecular relationships; immunocytochemical evidence of calbindin-27kDa in pineal transducers.Brain Res. 442, 33–42.CrossRefPubMedGoogle Scholar
  17. Schachner, M., Huang, S. K., Ziegelmüller, P., Bizzini, B. &Taugner, R. (1984) Glial cells in the pineal gland of mice and rats.Cell Tissue Res. 237, 245–52.CrossRefPubMedGoogle Scholar
  18. Sloviter, R. (1989) Calcium-binding protein (Calbindin-D28k) and parvalbumin immunocytochemistry: localization in the rat hippocampus with specific reference to the selective vulnerability of hippocampal neurons to seizure activity.J. Comp. Neurol. 280, 183–96.CrossRefPubMedGoogle Scholar
  19. Sternberger, L. A. (1974)Immunocytochemistry. Englewood Cliffs, New Jersey: Prentice Hall.Google Scholar
  20. Stichel, C. C., Kagi, U. &Heizmann, C. W. (1986) Palvalbumin in cat brain: isolation, characterization and localization.J. Neurochem. 47, 46–53.PubMedGoogle Scholar
  21. Vollrath, L. (1981) The pineal organ. InHandbuch der Mikroskopischen Anatomie des Menschen (edited byOkshe, A. &Vollrath, L.) (VI/7). Heidelberg: Springer-Verlag.Google Scholar
  22. Yamakuni, T., Usui, H., Iwanaga, T., Kondo, H., Odani, S. &Takahashi, Y. (1984) Isolation and immunohistochemical localization of a cerebellar protein.Neurosci. Lett. 45, 235–40.CrossRefPubMedGoogle Scholar
  23. Yamakuni, T., Arai, K. &Takahashi, Y. (1985) The developmental changes of mRNA levels for a cerebellar protein (spot 35 protein) in rat brain.FEBS Lett. 188, 127–30.CrossRefPubMedGoogle Scholar
  24. Yamakuni, T., Kuwano, R., Odani, S., Miki, N., Yamaguchi, K. &Takahashi, Y. (1987) Molecular cloning of cDNA to mRNA for a cerebellar spot 35 protein.Nucleic Acid Res. 16, 67–68.Google Scholar
  25. Yamakuni, T., Kuwano, R., Odani, S., Miki, N., Yamaguchi, K. &Takahashi, Y. (1987) Molecular cloning of cDNA to mRNA for a cerebellar spot 35 protein.J. Neurochem. 48, 1590–6.PubMedGoogle Scholar

Copyright information

© Chapman and Hall Ltd 1990

Authors and Affiliations

  • Miyuki Yamamoto
    • 1
  • Hisatake Kondo
    • 1
  • Tohru Yamakuni
    • 2
  • Yasuo Takahashi
    • 2
  1. 1.Department of Anatomy, School of MedicineKanazawa UniversityKanazawaJapan
  2. 2.Department of Neuropharmacology, Brain Research InstituteNiigata UniversityNiigataJapan

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