Immunocytochemical localization of photopigments in cephalopod retinae

Robles, Laura J.; Watanabe, Alan; Kremer, Norbert E.; Wong, Fulton; Bok, Dean

doi:10.1007/bf01611350

Cited by 22 publications

(24 citation statements)

References 41 publications

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“…10). This distribution was in agreement with the distribution we observed when using electron microscopy (Robles et al, 1987).…”

Section: Opsin Distributionsupporting

confidence: 94%

“…Immunocytochemical experiments have determined the precise location of opsin and aporetinochrome in cephalopod retinas (Fukushima et al, 1980;Ozaki et al, 1983;Robles et al, 1987). In our electron microscope immunocytochemical studies (Robles et al, 1987), we verified the presence of opsin in the rhabdoms and aporetinochrome in the myeloid bodies.…”

Section: Indexing Terms: Photopigments Rhodopsin Retinochrome Retisupporting

confidence: 69%

“…In our electron microscope immunocytochemical studies (Robles et al, 1987), we verified the presence of opsin in the rhabdoms and aporetinochrome in the myeloid bodies. In addition, we also localized retinochrome in the extracellular space between opposing rhabdomeres.…”

Section: Indexing Terms: Photopigments Rhodopsin Retinochrome Retimentioning

confidence: 67%

“…The antibodies were diluted to the appropriate concentrations with PBS containing 0.5% bovine serum albumin (BSA) and 0.1% Triton X-100 (PBS/BSA/Triton). The specificity and effective concentrations of these antibodies has been reported elsewhere (Robles et al, 1987;Molinaet al, 1992). After incubation in the primary antibody, sections were rinsed three times with PBSIBSAiTriton.…”

Section: Methodsmentioning

confidence: 87%

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Retinoid cycling proteins redistribute in light‐/dark‐adapted octopus retinas

Robles

Camacho

Torres

et al. 1995

J of Comparative Neurology

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In cephalopods, the complex rhodopsin-retinochrome system serves to regenerate metarhodopsin and metaretinochrome after illumination. In the dark, a soluble protein, retinal-binding protein (RALBP), shuttles 11-cis retinal released from metaretinochrome located in the photoreceptor inner segments to metarhodopsin present in the rhabdoms. While in the rhabdoms, RALBP delivers 11-cis retinal to regenerate rhodopsin and in turn binds the all-trans isomer released by metarhodopsin. RALBP then returns all-trans retinal to the inner segments to restore retinochrome. The conventional interpretation of retinoid cycling is contradicted by immunocytochemical studies showing that, in addition to rhodopsin, retinochrome is present in the rhabdomal compartment, making possible the direct exchange of chromophores between the metapigments with the potential exclusion of RALBP. By using immunofluorescence and laser scanning confocal microscopy, we have precisely located opsin, aporetinochrome, and RALBP in light-/dark-adapted octopus retinas. We found differences in the distribution of all three proteins throughout the retina. Most significantly, comparison of cross sections though light- and dark-adapted rhabdoms showed a dramatic shift in position of the proteins. In the dark, opsin and retinochrome colocalized at the base of the rhabdomal microvilli. In the light, opsin redistributed along the length of the microvillar membranes, and retinochrome retreated to a location that is perhaps extracellular. RALBP was present in the core cytoplasm of the photoreceptor outer segments in the dark, and RALBP moved to the periphery in the light. Because of the colocalization of opsin and retinochrome in the dark, we believe that the two metapigments participate directly in chromophore exchange. RALBP may serve to transport additional chromophore from the inner segments to the rhabdoms and may not be immediately involved in the exchange process.

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“…10). This distribution was in agreement with the distribution we observed when using electron microscopy (Robles et al, 1987).…”

Section: Opsin Distributionsupporting

confidence: 94%

Section: Indexing Terms: Photopigments Rhodopsin Retinochrome Retisupporting

confidence: 69%

Section: Indexing Terms: Photopigments Rhodopsin Retinochrome Retimentioning

confidence: 67%

Section: Methodsmentioning

confidence: 87%

See 2 more Smart Citations

Retinoid cycling proteins redistribute in light‐/dark‐adapted octopus retinas

Robles

Camacho

Torres

et al. 1995

J of Comparative Neurology

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“…These structures resemble the lipochondria that are found in the neurons of the abdom inal ganglia of Aplysia californica and that undergo mor phological changes in response to light (Brown et al 1975;Henkhart 1975); these lipochondria are also la belled by antibodies generated against squid opsin (Robles et al 1986). Preliminary studies with this squid opsin antibody have also shown labelling in the B. goul diana eye (Robles et al 1988).…”

Section: Site O F Photon Capturementioning

confidence: 88%

Opsin-like immunoreactivity in the circadian pacemaker neurons and photoreceptors of the eye of the opisthobranch mollusc Bulla gouldiana

Geusz

Foster

DeGrip

et al. 1996

Cell and Tissue Research

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Abstract. Circadian pacemaker cells in the eyes of the opisthobranch mollusc Bulla gouldiana generate a near 24-h rhythm in the frequency of optic nerve impulses. Previous electrophysiological studies suggest that these basal retinal neurons are intrinsically photosensitive and transduce light signals that shift the phase of their pace maker mechanism. To test whether the pacemaker neu rons contain opsin-like proteins, several polyclonal anti bodies that recognize opsins of vertebrate photoreceptors have been tested on histological sections of the eye and on the neurons in primary cell culture. The antibodies la bel both the pacemaker cells and the large distal photore ceptors that surround the lens. Immunoblot analyses of the proteins of the eye have identified a single band at 62±4 kDa. These opsin antibodies may label the photo pigment used in the entrainment of the circadian pace maker.

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Demonstration of a rhodopsin‐retinochrome system in the stalk eye of a marine gastropod, onchidium, by immunohistochemistry

Hamasaki-Katagiri

Terakita

Shichida

et al. 2001

J of Comparative Neurology

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The stalk eye of Onchidium sp. (Gastropoda, Mollusca) is the principal photoreceptor in a multiple photoreceptive system that consists of the stalk and dorsal eyes, dermal photoreceptor cells, and photosensitive neurons. To examine the localization of photopigments, the stalk eyes were immunostained with specific antibodies to rhodopsin, retinochrome, and retinal-binding protein (RALBP), which had been generated against squid retinal proteins. The retina of the stalk eye was divided into villous, pigmented, somatic, and neural layers. It was comprised mainly of two types of visual and pigmented supportive cells. The type 1 visual (VC1) cell was characterized by well-developed microvilli on its apical protrusion and photic vesicles in the cytoplasm. The photic vesicles were specifically blackened by prolonged osmification. The type 2 visual (VC2) cell had less numerous, shorter microvilli on its concave apical surface and lacked photic vesicles. The anti-squid rhodopsin antiserum was localized specifically to the villous layer that corresponded to the VC1 microvilli. With the anti-retinochrome peptide antibody, the somatic layer showed specific but patchy, positive staining that corresponded to the cytoplasm of the VC1 cells. Because the photic vesicles are known to contain retinochrome, these results indicate that this retinochrome is localized in the VC1 cytoplasm. Anti-RALBP antibody stained the supranuclear cytoplasm to the distal cytoplasm of VC1 cells. This is the first demonstration of the localization of RALBP in the Gastropoda Onchidium stalk eye. In squid retina that were immunostained as positive controls, the anti-rhodopsin antibody stained rhabdomeric microvilli, the anti-retinochrome antibody stained the inner segment and the basal region of the outer segment, and the anti-RALBP antibody stained the outer and inner segments, respectively. These results suggest that the rhodopsin-retinochrome system that has been established in cephalopod eyes is present in the Onchidium stalk eye.

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Immunocytochemical localization of photopigments in cephalopod retinae

Cited by 22 publications

References 41 publications

Retinoid cycling proteins redistribute in light‐/dark‐adapted octopus retinas

Retinoid cycling proteins redistribute in light‐/dark‐adapted octopus retinas

Opsin-like immunoreactivity in the circadian pacemaker neurons and photoreceptors of the eye of the opisthobranch mollusc Bulla gouldiana

Demonstration of a rhodopsin‐retinochrome system in the stalk eye of a marine gastropod, onchidium, by immunohistochemistry

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