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a special pigment found in the rods and cones of the retina

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2017/07/04 04:55:01」(JST)

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Photopigments are unstable pigments that undergo a chemical change when they absorb light. The term is generally applied to the non-protein chromophore moiety of photosensitive chromoproteins, such as the pigments involved in photosynthesis and photoreception. In medical terminology, "photopigment" commonly refers to the photoreceptor proteins of the retina.^{[citation needed]}

Photosynthetic pigments

Photosynthetic pigment (converting light into biochemical energy). Examples for photosynthetic pigments are chlorophyll, carotenoids and phycobilins. These pigments enter a high-energy state upon absorbing a photon which they can release in the form of chemical energy. This can occur via light-driven pumping of ions across a biological membrane (e.g. in the case of the proton pump bacteriorhodopsin) or via excitation and transfer of electrons released by photolysis (e.g. in the photosystems of the thylakoid membranes of plant chloroplasts). In chloroplasts, the light-driven electron transfer chain in turn drives the pumping of protons across the membrane.

Photoreceptor pigments

The pigments in photoreceptor proteins either change their conformation or undergo photoreduction when they absorb a photon. This change in the conformation or redox state of the chromophore then affects the protein conformation or activity and triggers a signal transduction cascade. Examples for photoreceptor pigments include retinal (for example in rhodopsin), flavin (for example in cryptochrome), and bilin (for example in phytochrome).^{[citation needed]}

Photopigments of the vertebrate retina

In medical terminology, the term photopigment is applied to opsin-type photoreceptor proteins, specifically rhodopsin and photopsins, the photoreceptor proteins in the retinal rods and cones of vertebrates that are responsible for visual perception, but also melanopsin and others.

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1. 網膜色素変性症：治療 retinitis pigmentosa treatment
2. 正常な加齢 normal aging

English Journal

Regeneration of Photopigment Is Enhanced in Mouse Cone Photoreceptors Expressing RPE65 Protein.

Tang PH, Wheless L, Crouch RK.SourceDepartments of Neuroscience, Medicine-Division of Biostatistics and Epidemiology, and Ophthalmology, Medical University of South Carolina, Charleston, South Carolina 29425.
The Journal of neuroscience : the official journal of the Society for Neuroscience.J Neurosci.2011 Jul 13;31(28):10403-11.
As cone photoreceptors mediate vision in bright light, their photopigments are bleached at a rapid rate and require substantial recycling of the chromophore 11-cis-retinal (RAL) for continued function. The retinal pigment epithelium (RPE) supplies 11-cis-RAL to both rod and cone photoreceptors; howe
PMID 21753017

Early onset and differential temporospatial expression of melanopsin isoforms in the developing chicken retina.

Verra DM, Contin MA, Hicks D, Guido ME.SourceDepartamento de Quimica Biologica, CIQUIBC (Centro de Investigaciones en Quimica Biologica de Cordoba), Facultad de Ciencias Quimicas, Universidad Nacional de Cordoba CONICET (Consejo Nacional de Investigaciones Cientificas y Tecnicas), Cordoba, Argentina.
Investigative ophthalmology & visual science.Invest Ophthalmol Vis Sci.2011 Jul 7;52(8):5111-20. Print 2011 Aug.
Purpose. Retinal ganglion cells (RGCs) expressing the photopigment melanopsin (Opn4) display intrinsic photosensitivity. In this study, the presence of nonvisual phototransduction cascade components in the developing chicken retina and primary RGCs cultures was investigated, focusing on the two Opn4
PMID 21676907

Japanese Journal

評議員会指名講演眼画像診断の進歩黄斑疾患の病態--画像診断による形態と機能解析 (第114回日本眼科学会総会)

飯田知弘
日本眼科学会雑誌 115(3), 238-275[含英語文要旨], 2011-03
NAID 40018749192

オプシンファミリーの分子進化と機能多様性

小柳光正
比較生理生化学 25(2), 50-57, 2008-04-20
　オプシンは, 視覚や概日リズムの光調節など動物の光受容システムの入り口に位置し, オプシンのアミノ酸配列に基づく性質が光受容の大部分の性質を決める。ほとんどの動物において複数のオプシン遺伝子が存在することが知られており, 多様なオプシンの機能を調べることは, 光受容システムの分子基盤やその進化を知る上で重要である。筆者らはオプシンの機能多様性を調べる目的で, ナメクジウオやヤツメウナギから …
NAID 10025616930