Renewal of opsin in the photoreceptor cells of the mosquito.

Stein, Peter J.; Brammer, J. D.; Ostroy, Sanford E.

doi:10.1085/jgp.74.5.565

Cited by 30 publications

(13 citation statements)

References 26 publications

(26 reference statements)

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“…Although it cannot at present be disproved, this alternative appears unlikely because membrane breakdown and synthesis have rather been found to increase after illumination (Eguchi and Waterman 1967;Itaya 1976;Blest and Maples 1979;N/issel and Waterman 1979;Stein et al 1979;Hafner and Tokarski 1988). Processes leading to the renewal of rhodopsin and to the removal of metarhodopsin have come to a standstill for this period.…”

Section: Discussionmentioning

confidence: 99%

Visual pigment, dark adaptation and rhodopsin renewal in the eye of Pontoporeia affinis (Crustacea, Amphipoda)

et al. 1994

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The benthic amphipod Pontoporeia affinis lives in the Baltic sea and in northern European lakes in an environment where very little light is available for vision. The eyes, consisting of 40-50 ommatidia, are correspondingly modified. Microspectrophotometric recordings on isolated eyes show the presence of at least two kinds of screening pigments in the ommatidia with maxima at 540-580 nm and 460-500 nm. Difference spectra obtained from the rhabdoms after exposure to red and blue light, respectively, give evidence of a single rhodopsin with its maximum at 548nm and a 500-nm metarhodopsin. In ERG recordings sensitivity in the dark-adapted state, after saturating exposures to blue and to red light, stabilizes at levels determined by the rhodopsin concentration. No change is observed during 10-14 h after the beginning of dark adaptation. However, using animals pre-exposed with a strong red light and then kept in darkness, it is found that after a delay of 20-40 h sensitivity of the dark-adapted eye begins to increase and finally, after 5-6 days reaches a level corresponding to 100% rhodopsin. Thus, a slow renewal of rhodopsin appears to occur in darkness, where a photoisomerization of metarhodopsin is excluded.

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Section: Discussionmentioning

confidence: 99%

Visual pigment, dark adaptation and rhodopsin renewal in the eye of Pontoporeia affinis (Crustacea, Amphipoda)

et al. 1994

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“…Evidence from other sources also suggests that in arthropods rhodopsin is commonly either photoregenerated from metarhodopsin (e.g., Hamdorf et al, 1971;Hamdorf and Schwemer, 1975) or synthesized de novo (Stein et al, 1979;Paulsen and Schwemer, 1983). Chromophore exchange appears to be much less frequent than in the vertebrate eye.…”

Section: Discussionmentioning

confidence: 99%

“…There are currently no measurements of opsin synthesis in the bee, however. Other evidence indicates that opsin synthesis and membrane renewal are probably closely associated in many other arthropods (moth [Goldman et al, 1975], mosquito [Stein et al, 1979], crayfish [Cronin and Goldsmith, 1984]; see also reviews by Waterman, 1982 andSchwemer, 1986).…”

Section: Comparison Of Bee and Flymentioning

confidence: 98%

The role of retinal photoisomerase in the visual cycle of the honeybee.

Smith

Goldsmith

1991

The Journal of General Physiology

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The compound eye of the honeybee has previously been shown to contain a soluble retinal photoisomerase which, in vitro, is able to catalyze stereospecifically the photoconversion of all-trans retinal to 11-cis retinal. In this study we combine in vivo and in vitro techniques to demonstrate how the retinal photoisomerase is involved in the visual cycle, creating 11-cis retinal for the generation of visual pigment. Honeybees have approximately 2.5 pmol/eye of retinal associated with visual pigments, but larger amounts (4-12 pmol/eye) of both retinal and retinol bound to soluble proteins. When bees are dark adapted for 24 h or longer, greater than 80% of the endogenous retinal, mostly in the all-trans configuration, is associated with the retinal photoisomerase. On exposure to blue light the retinal is isomerized to 11-cis, which makes it available to an alcohol dehydrogenase. Most of it is then reduced to 11-cis retinol. The retinol is not esterified and remains associated with a soluble protein, serving as a reservoir of 11-cis retinoid available for renewal of visual pigment. Alternatively, 11-cis retinal can be transferred directly to opsin to regenerate rhodopsin, as shown by synthesis of rhodopsin in bleached frog rod outer segments. This retinaldehyde cycle from the honeybee is the third to be described. It appears very similar to the system in another group of arthropods, flies, and differs from the isomerization processes in vertebrates and cephalopod mollusks.

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“…It is no longer clear what proportion ofproteins in rhabdomeral membrane fractions actually consist of rhodopsin, for published estimates may have been prejudiced by contamination of the integral membrane proteins by actin (for example, see references 2 and 36). Proteins labeled in autoradiographic experiments on photoreceptor membrane turnover (33,42,57,64) have been assumed to be rhodopsin without positive evidence . Whether actin turns over with the membrane remains to be determined .…”

Section: Possible Roles For Membrane-bound Rhabdomeral Actinmentioning

confidence: 99%

Membrane-associated actin in the rhabdomeral microvilli of crayfish photoreceptors.

Couet¹,

Stowe²,

Blest³

1984

The Journal of Cell Biology

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Infiltration of compound eyes of crayfish, Cherax destructor, with the thiol protease inhibitor Ep-475 or with trifluoperazine prior to fixation for electron microscopy was found to stabilize an axial filament of 6-12 nm diam within each rhabdomeral microvillus of the photoreceptors . Rhabdoms isolated from retinal homogenates by sucrose gradient centrifugation under conditions that stabilize cytoskeletal material contained large amounts of a 42-kd polypeptide that co-migrated with insect flight muscle actin in one-and two-dimensional PAGE, inhibited pancreatic DNase I, and bound to vertebrate myosin . Vertebrate skeletal muscle actin added to retinal homogenates did not co-purify with rhabdoms, implying that actin was not a contaminant from nonmembranous structures. DNase I inhibition assays of detergent-lysed rhabdoms indicated the presence of large amounts of filamentous actin provided ATP was present . Monomeric actin in such preparations was completely polymerizable only after 90 min incubation with equimolar phalloidin . More than half of the actin present could be liberated from the membrane by sonication, indicating a loose association with the membrane . However, a large proportion of the actin was tightly bound to the rhabdomeral membrane, and washing sonicated membrane fractions with solutions of a range of ionic strengths and nonionic detergents failed to remove it. Antibodies to scallop actin only bound to frozen sections of rhabdoms after gentle permeabilization and very long incubation periods, probably because of steric hindrance and the hydrophobicity of the structure . The F-actin probe nitrobenzoxadiazol phallacidin bound to rhabdoms and labeled F-actin aggregates in other retinal components, but rhabdom fluorescence was not abolished by preincubation with phalloidin. The biochemical data indicate the existence of two distinct actin-based cytoskeletal systems, one being closely membrane associated. The other may possibly constitute the axial filament, although the evidence for this is equivocal .The rhabdomeres of arthropod and cephalopod photoreceptors are composed of numerous microvilli which in a given cell-type are remarkably uniform in diameter and ordered in arrays ofalmost crystalline regularity . Successive authors have implied or suggested that a cytoskeleton is likely to underlie this organization (6,31,37,59,60,65), and some have speculated that it will prove to be actin based. Actin is a component of rhabdoms of squid (59, 60), and the organization ofother microvillar types provides well known precedents (50,54,68).Conventional techniques of electron microscopy have not revealed a cytoskeletal organization within rhabdomeral microvilli with any consistency, and an early demonstration of an axial filament in microvilli of bee photoreceptors (70) has been largely overlooked in the literature. Recently, three studies have demonstrated an axial filament linked to the plasma membrane by side-arms in photoreceptor microvilli offlies (7, 8) and squid (60). Although these filament...

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Renewal of opsin in the photoreceptor cells of the mosquito.

Cited by 30 publications

References 26 publications

Visual pigment, dark adaptation and rhodopsin renewal in the eye of Pontoporeia affinis (Crustacea, Amphipoda)

Visual pigment, dark adaptation and rhodopsin renewal in the eye of Pontoporeia affinis (Crustacea, Amphipoda)

The role of retinal photoisomerase in the visual cycle of the honeybee.

Membrane-associated actin in the rhabdomeral microvilli of crayfish photoreceptors.

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