Localization of caveolin-1 and c-src in mature and differentiating photoreceptors: raft proteins co-distribute with rhodopsin during development |
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Authors: | Ágnes I Berta Kathleen Boesze-Battaglia Attila Magyar Ágoston Szél Anna L Kiss |
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Institution: | 1.Department of Human Morphology and Developmental Biology,Semmelweis University Budapest,Budapest,Hungary;2.Department of Biochemistry, School of Dental Medicine,University of Pennsylvania,Philadelphia,USA |
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Abstract: | Numerous biochemical and morphological studies have provided insight into the distribution pattern of caveolin-1 and the presence
of membrane rafts in the vertebrate retina. To date however, studies have not addressed the localization profile of raft specific
proteins during development. Therefore the purpose of our studies was to follow the localization pattern of caveolin-1, phospho-caveolin-1
and c-src in the developing retina and compare it to that observed in adults. Specific antibodies were used to visualize the
distribution of caveolin-1, c-src, a kinase phosphorylating caveolin-1, and phospho-caveolin-1. The labeling pattern of this
scaffolded complex was compared to those of rhodopsin and rhodopsin kinase. Samples were analyzed at various time points during
postnatal development and compared to adult retinas. The immunocytochemical studies were complemented with immunoblots and
immunoprecipitation studies. In the mature retina caveolin-1 and c-src localized mainly to the cell body and IS of photoreceptors,
with only very weakly labeled OS. In contrast, phospho-caveolin-1 was only detectable in the OS of photoreceptors. During
development we followed the expression and distribution profile of these proteins in a temporal sequence with special attention
to the period when OS formation is most robust. Double labeling immunocytochemistry and immunoprecipitation showed rhodopsin
to colocalize and co-immunoprecipitate with caveolin-1 and c-src. Individual punctate structures between the outer limiting
membrane and the outer plexiform layer were seen at P10 to be labeled by both rhodopsin and caveolin-1 as well as by rhodopsin
and c-src, respectively. These studies suggest that membrane raft specific proteins are co-distributed during development,
thereby pointing to a role for such complexes in OS formation. In addition, the presence of small punctate structures containing
caveolin-1, c-src and rhodopsin raise the possibility that these proteins may transport together to OS during development
and that caveolin-1 exists predominantly in a phosphorylated form in the OS. |
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