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Calbindin D-28K immunoreactivity of human cone cells varies with retinal position

Published online by Cambridge University Press:  02 June 2009

Tammie L. Haley ,
Roland Pochet ,
Larry Baizer ,
Miriam D. Burton ,
John W. Crabb ,
Marc Parmentier  and
Arthur S. Polans
Tammie L. Haley
Affiliation:
R.S. Dow Neurological Sciences Institute and the Department of Ophthalmology, Good Samaritan Hospital and Medical Center, Portland
Roland Pochet
Affiliation:
Laboratoire d'Histologie, Faculte de Medecine, Universite Libre de Bruxelles, Belgium
Larry Baizer
Affiliation:
R.S. Dow Neurological Sciences Institute and the Department of Ophthalmology, Good Samaritan Hospital and Medical Center, Portland
Miriam D. Burton
Affiliation:
R.S. Dow Neurological Sciences Institute and the Department of Ophthalmology, Good Samaritan Hospital and Medical Center, Portland
John W. Crabb
Affiliation:
W. Alton Jones Cell Science Center, Lake Placid
Marc Parmentier
Affiliation:
Institut de Recherche, Interdisciplinaire en Biologie Humaine et Nucleaire, Universite Libre de Bruxelles, Belgium
Arthur S. Polans
Affiliation:
R.S. Dow Neurological Sciences Institute and the Department of Ophthalmology, Good Samaritan Hospital and Medical Center, Portland
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Abstract

Calbindin D-28K is a calcium-binding protein found in the cone but not rod photoreceptor cells in the retinas of a variety of species. Recent studies of the monkey retina indicated that calbindin D-28K may be expressed preferentially in non-foveal regions of the retina. In the current studies of human retinas, immunohistochemical experiments demonstrated that calbindin D-28K is reduced or absent in the fovea and parafovea, but prevalent in the perifovea and periphery. These findings were supported by the quantification of calbindin D-28K in 1-mm trephine punches obtained from different regions of the human retina. The specificity of the anti-calbindin D-28K antibodies used in these studies was confirmed by Western blot analysis using purified calbindin D-28K. The protein was purified from retinal tissue and its identity confirmed by partial amino-acid sequence analysis. The expression of calbindin D-28K did not correlate with the spectral properties of the cones, rather to their position in the retina. The study of spatially expressed genes, like the one encoding calbindin D-28K, may help explain the patterns of retinal degeneration seen in some human cone-rod dystrophies.

Keywords

Calbindin D-28KCalcium-binding proteinRetinaCone photoreceptor cellsRetinal degeneration
Type
Research Articles
Information
Visual Neuroscience , Volume 12 , Issue 2 , March 1995 , pp. 301 - 307
Copyright
Copyright © Cambridge University Press 1995

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References

Crabb, J.W., Johnson, C.M., Carr, S.A., Armes, L.G. & Saari, J.C. (1988). The complete primary structure of the cellular retinaldehyde-binding protein from bovine retina. Journal of Biological Chemistry 263, 18678–18687.CrossRefGoogle ScholarPubMed
Dizhoor, A., Ray, S., Kumar, S., Niemi, G., Spencer, M., Brolley, D., Walsh, K., Philipov, P., Hurley, J. & Stryer, L. (1991). Recoverin: A calcium sensitive activator of retinal rod guanylate cyclase. Science 251, 915–918.CrossRefGoogle ScholarPubMed
Fullmer, C.S. & Wasserman, R.H. (1980). In Calcium Binding Proteins: Structure and function, ed. Sieger, F.L., Carafoli, E., Kretsinoer, R.H., Maclennan, D.H. & Wasserman, R.H., pp. 363–370. New York: Eisevier.Google Scholar
Gorczyca, W.A., Gray-Keller, M.P., Detwiler, P. & Palczewski, K. (1994). Purification and physiological evaluation of guanylate cyclase activating protein from retinal rods. Proceedings of the National Academy of Sciences of the U.S.A. 91, 4014–4018.CrossRefGoogle ScholarPubMed
Gray-Keller, M.P., Polans, A.S., Palczewski, K. & Detwiler, P. (1993). The effect of recoverin-like calcium-binding proteins on the photoresponse of retinal rods. Neuron 10, 523–531.CrossRefGoogle ScholarPubMed
Gross, M.D., Gosnell, M., Tsarbopoulos, A. & Hunziker, W. (1993). A functional and degenerate pair of EF hands contains the very high-affinity calcium-binding site of calbindin D28k. Journal of Biological Chemistry 268, 20917–20922.CrossRefGoogle ScholarPubMed
Hall, A.K. & Norman, A.W. (1991). Vitamin D-independent expression of chick brain calbindin-D28k. Molecular Brain Research 9, 9–14.CrossRefGoogle ScholarPubMed
Hogan, M.J., Alvarado, J.A. & Weddell, J.E. (1971). The retina. In Histology of the Human Eye, ed. Hogan, M.J., Alvarado, J.A. & Weddell, J.E., pp. 393–522. Philadelphia, Pennsylvania: W.B. Saunders Company.Google Scholar
Hunziker, W. (1986). The 28-kDa vitamin D-dependent calcium-binding protein has a six-domain structure. Proceedings of the National Academy of Sciences of the U.S.A. 83, 7578–7582.CrossRefGoogle Scholar
Jande, S.S., Maler, L. & Lawson, D.E.M. (1981). Immunohistochemical mapping of calcium-binding protein in brain. Nature 294, 765–767.CrossRefGoogle ScholarPubMed
Kawamura, S. & Murakami, M. (1991). Calcium-dependent regulation of cyclic GMP phosphodiesterase by a protein from frog retinal rods. Nature 349, 420–423.CrossRefGoogle ScholarPubMed
Maruyama, K., Ebisawa, K. & Nonomura, Y. (1985). Purification of vitamin D-dependent 28, 000-Mr calcium-binding protein from bovine cerebellum and kidney by calcium-dependent elution from DEAE-Cellulose DE-52 column chromatography. Analytical Biochemistry 151, 1–6.CrossRefGoogle ScholarPubMed
Miller, J.J. & Baimbridge, K.G. (1983). Biochemical and immuno-histochemical correlates of kindling-induced epilepsy: Role of calcium-binding protein. Brain Research 278, 322–326.CrossRefGoogle Scholar
Nagao, S., Yamazaki, A. & Bitensky, M. (1987). Calmodulin and calmodulin-binding proteins in amphibian rod outer segments. Biochemistry 26, 1659–1665.CrossRefGoogle ScholarPubMed
Nakano, A., Terasawa, M., Watanabe, M., Usuda, N., Morita, T. & Hidaka, H. (1992). Neurocalcin, a novel calcium-binding protein with three EF-hand domains, expressed in retinal amacrine cells and ganglion cells. Biochemical and Biophysical Research Communications 186, 1207–1211.CrossRefGoogle ScholarPubMed
Nakatani, K. & Yau, K.-W. (1989). Sodium-dependent calcium extrusion and sensitivity regulation in retinal cones of the salamander. Journal of Physiology 409, 525–548.CrossRefGoogle ScholarPubMed
Parmentier, M., Lawson, D.E.M. & Vassart, G. (1987). Human 27-kDa calbindin complementary DNA sequence: Evolutionary and functional implications. European Journal of Biochemistry 170, 207–215.CrossRefGoogle ScholarPubMed
Pasteels, B., Rogers, J., Blachier, F. & Pochet, R. (1990). Calbindin and calretinin localization in retina from different species. Visual Neuroscience 5, 1–16.CrossRefGoogle ScholarPubMed
Pochet, R., Pasteels, B., Seto-Ohshima, A., Bastianelli, E., Kitajima, S. & Van Eldik, L.J. (1991). Calmodulin and calbindin localization in retina from six vertebrate species. Journal of Comparative Neurology 314, 750–762.CrossRefGoogle ScholarPubMed
Polans, A.S. & Burton, M.D. (1988). Sialoglycoproteins of the frog rod outer segment plasma membrane, investigative Ophthalmology and Visual Science 29, 1523–1532.Google ScholarPubMed
Polans, A.S., Buczylko, J., Crabb, J. & Palczewski, K. (1991). A photoreceptor calcium-binding protein is recognized by autoantibodies obtained from patients with cancer-associated retinopathy. Journal of Cell Biology 112, 981–989.CrossRefGoogle ScholarPubMed
Polans, A.S., Burton, M.D., Haley, T.L., Crabb, J.W. & Palczewski, K. (1993 a). Recoverin, but not visinin, is an autoantigen in the human retina identified with a cancer-associated retinopathy. Investigative Ophthalmology and Visual Science 34, 81–90.Google Scholar
Polans, A.S., Crabb, J. & Palczewski, K. (1993 b). Calcium-binding proteins in the retina. In Methods in Neuroscience, Vol. 15: Photo-receptor Cells, ed. Hargrave, P., pp. 248–260. New York: Academic Press.CrossRefGoogle Scholar
Pugh, E.N. Jr., & Lamb, T.D. (1990). Cyclic GMP and calcium: The internal messengers of excitation and adaptation in vertebrate pho-toreceptors. Vision Research 30, 1923–1948.CrossRefGoogle Scholar
Röhrenbeck, J., Wässle, H. & Boycott, B.B. (1989). Horizontal cells in the monkey retina: Immunocytochemical staining with antibodies against calcium-binding proteins. European Journal of Neuroscience 1, 407–420.CrossRefGoogle ScholarPubMed
Sanna, P.P., Keyser, K.T., Battenberg, E. & Bloom, F.E. (1990). Parvalbumin immunoreactivity in the rat retina. Neuroscience Letters 118, 136–139.CrossRefGoogle ScholarPubMed
Szlyk, J.P., Fishman, G.A., Alexander, K.R., Peachey, N.S. & Derlacki, D.J. (1993). Clinical subtypes of cone-rod dystrophy. Archives of Ophthalmology 111, 781–788.CrossRefGoogle ScholarPubMed
Takamatsu, K. & Uyemura, K. (1992). Identification of recoverin-like immunoreactivity in mouse brain. Brain Research 571, 350–353.CrossRefGoogle ScholarPubMed
Taylor, A.N. (1974). Chick brain calcium-binding protein: Comparison with intestinal vitamin D-induced calcium-binding protein. Archives of Biochemistry and Biophysics 161, 100–108.CrossRefGoogle Scholar
Verstappen, A., Parmentier, M., Chirnoaga, M., Lawson, D.E.M., Pasteels, J.L. & Pochet, R. (1986). Vitamin D-dependent calcium-binding protein immunoreactivity in human retina. Ophthalmology Research 18, 209–214.CrossRefGoogle ScholarPubMed
Wasserman, R.H. & Taylor, A.N. (1966). Vitamin D-induced calcium-binding protein in chick intestinal mucosa. Science 152, 791–793.CrossRefGoogle Scholar
Yamagata, K., Goto, K., Kuo, C.H., Kondo, H. & Miki, N. (1990). Visinin: A novel calcium-binding protein expressed in retinal core cells. Neuron 2, 469–476.CrossRefGoogle Scholar