Calmodulin and calbindin localization in retina from six vertebrate species

Calmodulin is abundant in the central nervous system, including the retina. However, the localization of calmodulin in the retina has not been described in detail. We therefore decided to investigate calmodulin localization in retinae from six vertebrate species, by using immunohistochemical labelin...

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Veröffentlicht in:Journal of comparative neurology (1911) 1991-12, Vol.314 (4), p.750-762
Hauptverfasser: Pochet, Roland, Pasteels, Brigitte, Seto-ohshima, Akiko, Bastianelli, Enrico, Kitajima, Satoko, Van Eldik, Linda J.
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container_issue 4
container_start_page 750
container_title Journal of comparative neurology (1911)
container_volume 314
creator Pochet, Roland
Pasteels, Brigitte
Seto-ohshima, Akiko
Bastianelli, Enrico
Kitajima, Satoko
Van Eldik, Linda J.
description Calmodulin is abundant in the central nervous system, including the retina. However, the localization of calmodulin in the retina has not been described in detail. We therefore decided to investigate calmodulin localization in retinae from six vertebrate species, by using immunohistochemical labeling with four different rabbit polyclonal antibodies against calmodulin. The localization of calbindin‐D28k, another calcium‐binding protein already well described in retina, was compared. We found that calmodulin distribution is more highly conserved among species, contrasting with calbindin variability. The most striking result emerging is that calmodulin could not be detected in photoreceptors although other layers are intensely calmodulin‐immunoreactive, casting doubt about a direct role of calmodulin in phototransduction. Horizontal cells are weakly calmodulin‐immunoreactive, bipolar cells are calmodulin‐immunoreactive except in turtle retina, numerous amacrine and ganglion cells are labeled in all species, and the fiber layer is always labeled. These data demonstrate that, while the calmodulin distribution in retina is similar among vertebrate species, selective differences in localization can be detected not only among the same cell types in different species but also among different cell types in the same species. The results showing differences in calmodulin immunoreactivity among cell types also provide further evidence that calmodulin expression in eukaryotes is not constitutive, in the sense that not every cell expresses similar levels of calmodulin.
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However, the localization of calmodulin in the retina has not been described in detail. We therefore decided to investigate calmodulin localization in retinae from six vertebrate species, by using immunohistochemical labeling with four different rabbit polyclonal antibodies against calmodulin. The localization of calbindin‐D28k, another calcium‐binding protein already well described in retina, was compared. We found that calmodulin distribution is more highly conserved among species, contrasting with calbindin variability. The most striking result emerging is that calmodulin could not be detected in photoreceptors although other layers are intensely calmodulin‐immunoreactive, casting doubt about a direct role of calmodulin in phototransduction. Horizontal cells are weakly calmodulin‐immunoreactive, bipolar cells are calmodulin‐immunoreactive except in turtle retina, numerous amacrine and ganglion cells are labeled in all species, and the fiber layer is always labeled. These data demonstrate that, while the calmodulin distribution in retina is similar among vertebrate species, selective differences in localization can be detected not only among the same cell types in different species but also among different cell types in the same species. The results showing differences in calmodulin immunoreactivity among cell types also provide further evidence that calmodulin expression in eukaryotes is not constitutive, in the sense that not every cell expresses similar levels of calmodulin.</description><identifier>ISSN: 0021-9967</identifier><identifier>EISSN: 1096-9861</identifier><identifier>DOI: 10.1002/cne.903140408</identifier><identifier>PMID: 1816273</identifier><identifier>CODEN: JCNEAM</identifier><language>eng</language><publisher>Hoboken: Wiley Subscription Services, Inc., A Wiley Company</publisher><subject>Animals ; Biological and medical sciences ; Calbindin 1 ; Calbindins ; calcium-binding proteins ; Calmodulin - analysis ; Cercopithecus aethiops - metabolism ; Columbidae - metabolism ; Eye and associated structures. Visual pathways and centers. Vision ; Fundamental and applied biological sciences. Psychology ; Gene Expression ; Goldfish - metabolism ; Immunoenzyme Techniques ; immunohistochemistry ; Mice - metabolism ; Photoreceptor Cells - chemistry ; photoreceptors ; Rana esculenta - metabolism ; Retina - chemistry ; S100 Calcium Binding Protein G - analysis ; Species Specificity ; Turtles - metabolism ; Vertebrata ; Vertebrates - metabolism ; Vertebrates: nervous system and sense organs</subject><ispartof>Journal of comparative neurology (1911), 1991-12, Vol.314 (4), p.750-762</ispartof><rights>Copyright © 1991 Wiley‐Liss, Inc.</rights><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4448-c115facbb677ff8c76d3459e0203e9af70e6927da674482c7d41291628748e5e3</citedby><cites>FETCH-LOGICAL-c4448-c115facbb677ff8c76d3459e0203e9af70e6927da674482c7d41291628748e5e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fcne.903140408$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fcne.903140408$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>315,781,785,1418,27926,27927,45576,45577</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&amp;idt=5194009$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1816273$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Pochet, Roland</creatorcontrib><creatorcontrib>Pasteels, Brigitte</creatorcontrib><creatorcontrib>Seto-ohshima, Akiko</creatorcontrib><creatorcontrib>Bastianelli, Enrico</creatorcontrib><creatorcontrib>Kitajima, Satoko</creatorcontrib><creatorcontrib>Van Eldik, Linda J.</creatorcontrib><title>Calmodulin and calbindin localization in retina from six vertebrate species</title><title>Journal of comparative neurology (1911)</title><addtitle>J. Comp. Neurol</addtitle><description>Calmodulin is abundant in the central nervous system, including the retina. However, the localization of calmodulin in the retina has not been described in detail. We therefore decided to investigate calmodulin localization in retinae from six vertebrate species, by using immunohistochemical labeling with four different rabbit polyclonal antibodies against calmodulin. The localization of calbindin‐D28k, another calcium‐binding protein already well described in retina, was compared. We found that calmodulin distribution is more highly conserved among species, contrasting with calbindin variability. The most striking result emerging is that calmodulin could not be detected in photoreceptors although other layers are intensely calmodulin‐immunoreactive, casting doubt about a direct role of calmodulin in phototransduction. Horizontal cells are weakly calmodulin‐immunoreactive, bipolar cells are calmodulin‐immunoreactive except in turtle retina, numerous amacrine and ganglion cells are labeled in all species, and the fiber layer is always labeled. These data demonstrate that, while the calmodulin distribution in retina is similar among vertebrate species, selective differences in localization can be detected not only among the same cell types in different species but also among different cell types in the same species. The results showing differences in calmodulin immunoreactivity among cell types also provide further evidence that calmodulin expression in eukaryotes is not constitutive, in the sense that not every cell expresses similar levels of calmodulin.</description><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Calbindin 1</subject><subject>Calbindins</subject><subject>calcium-binding proteins</subject><subject>Calmodulin - analysis</subject><subject>Cercopithecus aethiops - metabolism</subject><subject>Columbidae - metabolism</subject><subject>Eye and associated structures. Visual pathways and centers. Vision</subject><subject>Fundamental and applied biological sciences. 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Visual pathways and centers. Vision</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Expression</topic><topic>Goldfish - metabolism</topic><topic>Immunoenzyme Techniques</topic><topic>immunohistochemistry</topic><topic>Mice - metabolism</topic><topic>Photoreceptor Cells - chemistry</topic><topic>photoreceptors</topic><topic>Rana esculenta - metabolism</topic><topic>Retina - chemistry</topic><topic>S100 Calcium Binding Protein G - analysis</topic><topic>Species Specificity</topic><topic>Turtles - metabolism</topic><topic>Vertebrata</topic><topic>Vertebrates - metabolism</topic><topic>Vertebrates: nervous system and sense organs</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Pochet, Roland</creatorcontrib><creatorcontrib>Pasteels, Brigitte</creatorcontrib><creatorcontrib>Seto-ohshima, Akiko</creatorcontrib><creatorcontrib>Bastianelli, Enrico</creatorcontrib><creatorcontrib>Kitajima, Satoko</creatorcontrib><creatorcontrib>Van Eldik, Linda J.</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Calcium &amp; Calcified Tissue Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of comparative neurology (1911)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Pochet, Roland</au><au>Pasteels, Brigitte</au><au>Seto-ohshima, Akiko</au><au>Bastianelli, Enrico</au><au>Kitajima, Satoko</au><au>Van Eldik, Linda J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Calmodulin and calbindin localization in retina from six vertebrate species</atitle><jtitle>Journal of comparative neurology (1911)</jtitle><addtitle>J. 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subjects Animals
Biological and medical sciences
Calbindin 1
Calbindins
calcium-binding proteins
Calmodulin - analysis
Cercopithecus aethiops - metabolism
Columbidae - metabolism
Eye and associated structures. Visual pathways and centers. Vision
Fundamental and applied biological sciences. Psychology
Gene Expression
Goldfish - metabolism
Immunoenzyme Techniques
immunohistochemistry
Mice - metabolism
Photoreceptor Cells - chemistry
photoreceptors
Rana esculenta - metabolism
Retina - chemistry
S100 Calcium Binding Protein G - analysis
Species Specificity
Turtles - metabolism
Vertebrata
Vertebrates - metabolism
Vertebrates: nervous system and sense organs
title Calmodulin and calbindin localization in retina from six vertebrate species
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