Immunocytochemical localization of opsin, visual arrestin, myosin III, and calmodulin in Limulus lateral eye retinular cells and ventral photoreceptors
| Autor: | W. Clay Smith, Chelsi Cacciatore, Richard Payne, Michael A. Malone, Bruce G. Calman, Barbara-Anne Battelle, Alain Dabdoub, A. W. Andrews |
|---|---|
| Rok vydání: | 2001 |
| Předmět: |
Male
Opsin genetic structures Calmodulin Myosins Eye Horseshoe Crabs Arrestin Animals Protein Isoforms Tissue Distribution biology General Neuroscience Rod Opsins Photoreceptor protein biology.organism_classification Immunohistochemistry eye diseases Horseshoe crab Cell biology Rhodopsin Limulus biology.protein Female Photoreceptor Cells Invertebrate sense organs Visual phototransduction |
| Zdroj: | The Journal of comparative neurology. 435(2) |
| ISSN: | 0021-9967 |
| Popis: | The photoreceptors of the horseshoe crab Limuluspolyphemus are classical preparations for studies of the photoresponse and its modulation by circadian clocks. An extensive literature details their physiology and ultrastructure, but relatively little is known about their biochemical organization largely because of a lack of antibodies specific for Limulus photoreceptor proteins. We developed antibodies directed against Limulus opsin, visual arrestin, and myosin III, and we have used them to examine the distributions of these proteins in the Limulus visual system. We also used a commercial antibody to examine the distribution of calmodulin in Limulus photoreceptors. Fixed frozen sections of lateral eye were examined with conventional fluorescence microscopy; ventral photoreceptors were studied with confocal microscopy. Opsin, visual arrestin, myosin III, and calmodulin are all concentrated at the photosensitive rhabdomeral membrane, which is consistent with their participation in the photoresponse. Opsin and visual arrestin, but not myosin III or calmodulin, are also concentrated in extra-rhabdomeral vesicles thought to contain internalized rhabdomeral membrane. In addition, visual arrestin and myosin III were found widely distributed in the cytosol of photoreceptors, suggesting that they have functions in addition to their roles in phototransduction. Our results both clarify and raise new questions about the functions of opsin, visual arrestin, myosin III, and calmodulin in photoreceptors and set the stage for future studies of the impact of light and clock signals on the structure and function of photoreceptors. J. Comp. Neurol. 435:211–225, 2001. © 2001 Wiley-Liss, Inc. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Plný text