Photoregeneration and Sensitivity Control of Photoreceptors of Invertebrates

Hamdorf, Kurt; Paulsen, Reinhard; Schwemer, Joachim

doi:10.1007/978-3-642-85769-0_18

Cited by 93 publications

(52 citation statements)

References 10 publications

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“…The dorsal visual pigment of the male has an isosbestic point Aiso 513 nm; ventrally Ais o ~ 490 nm. Very similar values were obtained in blowfly and dronefly respectively (Hamdorf et al, 1973;Stavenga et al, 1973;Razmjoo and Hamdorf, 1976;Stavenga, 1976). Moreover the photo-equilibrium spectra were very similar as obtained in the respective cases (Fig.…”

Section: Visual Pigment Of the Hoverfly Syrphus Balteatussupporting

confidence: 83%

Visual pigment processes and prolonged pupillary responses in insect photoreceptor cells

Stavenga

1979

Biophys. Struct. Mechanism

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Abstract. The visual pigment in the peripheral retinular cells of the hoverflySyrphus balteatus was investigated by absorbance difference measurements.Different visual pigments were found in the dorsal versus the ventral part of the eye in the male, but not in the female. In the male in the dorsal part of the eye the visual pigment has an isosbestic point at 513 nm; in the ventral part this value is 490 nm. The latter value is found in the female in both parts of the eye.Prolonged pupiUary responses were studied in the male Syrphus and appeared to be most marked in the ventral part of the eye. In both hoverfly and blowfly prolonged pupillary responses are induced by short wavelength light only; i.e., by fight which excessively can convert rhodopsin into metarhodopsin. By contrast, in butterflies red light (and a long dark adaptation time) is necessary to evoke a prolonged pupillary response. It was demonstrated in both hoverfly and blowfly that long wavelength light, which reeonverts metarhodopsin into rhodopsin, inhibits a prolonged pupillary response; or, accelerates pupil opening.

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Section: Visual Pigment Of the Hoverfly Syrphus Balteatussupporting

confidence: 83%

Visual pigment processes and prolonged pupillary responses in insect photoreceptor cells

Stavenga

1979

Biophys. Struct. Mechanism

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“…The maximal content of Acid Metarhodopsin in photosteady state mixture depends on the wavelength of the actinic light (Hamdorf et al ., 1973). In case of Octopus defleini, the maximal content of Acid Metarhodopsin formed, about 70%, occurred when rhodopsin was illuminated with blue light (440 nm) (Tsuda, 1979).…”

Section: Purification Of T-acid Metarhodopsinmentioning

confidence: 99%

A Purified Agonist-Activated G-Protein Coupled Receptor: Truncated Octopus Acid Metarhodopsin

et al. 2004

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“…Briefly, under red light, more than 99% of the visual pigment is present in the P-state (Hamdorf et al, 1973 ; P-state membranes). Irradiation with blue light establishes a photostationary state of 69% M and 31% P (Paulsen and Schwemer, 1983; M-state membranes).…”

Section: Irradiation Of Samplesmentioning

confidence: 99%

An arrestin homolog of blowfly photoreceptors stimulates visual‐pigment phosphorylation by activating a membrane‐associated protein kinase

Bentrop

Plangger

Paulsen

1993

European Journal of Biochemistry

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An arrestin homolog (Arr2, 49-kDa protein) of blowfly (Culliphoru erythrocephula) retinae undergoes light-dependent reversible binding to the photoreceptor membrane. In order to characterize this arrestin homolog and to study its function in a well-defined experimental system, we developed a purification scheme which used microvillar photoreceptor membranes as an affinity binding matrix. Additional purification steps included ammonium sulfate precipitation, gel filtration and binding to heparin-agarose. The molecular mass of purified Arr2, as judged by SDSPAGE, is in the range 45-49 kDa. The isoelectric point, as judged by gel isolelectric focussing, is 8.7. Arr2 is specific to the retina, where it is subject to phosphorylation at multiple sites.Binding of purified Arr2 to isolated photoreceptor membranes efficiently activates the lightinduced phosphorylation of visual pigment. Since the assay system used is deficient in rhodopsin phosphatase activity, the arrestin-stimulated phosphate incorporation into rhodopsin results solely from the activation of a protein kinase. Phosphorylation experiments with highly purified membrane preparations indicate that rhodopsin kinase is tightly associated with the rhabdomeric membrane or the microvillar cytoskeleton. Rhodopsin kinase is released from the membrane or inactivated upon treatment with urea. It is concluded that this anestin is a regulator protein that controls visualpigment phosphorylation by affecting the interaction of metarhodopsin and rhodopsin (metarhodopsin) kinase.Recent electrophysiological, biochemical and molecularbiology studies have substantially deepened the insight into the process of signal transduction in rhabdomeric photoreceptors (Minke and Selinger 1991 ;Pak, 1991 ;Smith et al., 1991), and it has become evident that certain features are common to the transduction cascades in both rhabdomeric and ciliary photoreceptors. For example, in both systems, excitation and adaptation are initiated by photoconversion of the visual pigment, rhodopsin (P), to its active form, metarhodopsin (M), (P+M). Accompanying conformational changes of opsin, the protein moiety of the visual pigment, trigger interactions with other components of the transduction cascade, namely enzymes and regulatory proteins. Searching for such components, we have previously identified a 49-kDa protein of blowfly photoreceptors which is buffer soluble in dark-adapted membrane preparations (Pstate membranes) and becomes tightly bound to the microvillar photoreceptor membrane upon P to M transition (M-state membranes; Bentrop and Paulsen, 1986). The affinity of the 49-kDa protein for the membrane is drastically reduced after photoconversion of M to P (M+P), and the protein can consequently be extracted from the (P state) membrane withCorrespondence to

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Photoregeneration and Sensitivity Control of Photoreceptors of Invertebrates

Cited by 93 publications

References 10 publications

Visual pigment processes and prolonged pupillary responses in insect photoreceptor cells

Visual pigment processes and prolonged pupillary responses in insect photoreceptor cells

A Purified Agonist-Activated G-Protein Coupled Receptor: Truncated Octopus Acid Metarhodopsin

An arrestin homolog of blowfly photoreceptors stimulates visual‐pigment phosphorylation by activating a membrane‐associated protein kinase

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