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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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