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Rhodopsin
Rhodopsin, also known as visual purple, is a protein encoded by the RHO gene and a G-protein-coupled receptor (GPCR). It is the opsin of the rod cells in the retina and a light-sensitive receptor protein that triggers visual phototransduction in rods. Rhodopsin mediates dim light vision and thus is extremely sensitive to light. When rhodopsin is exposed to light, it immediately photobleaches. In humans, it is regenerated fully in about 30 minutes, after which the rods are more sensitive. Defects in the rhodopsin gene cause eye diseases such as retinitis pigmentosa and congenital stationary night blindness. Names Rhodopsin was discovered by Franz Christian Boll in 1876. The name rhodospsin derives from Ancient Greek () for "rose", due to its pinkish color, and () for "sight". It was coined in 1878 by the German physiologist Wilhelm Friedrich Kühne (1837-1900). When George Wald discovered that rhodopsin is a holoprotein, consisting of retinal and an apoprotein, ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Opsin
Animal opsins are G-protein-coupled receptors and a group of proteins made light-sensitive via a chromophore, typically retinal. When bound to retinal, opsins become Retinylidene proteins, but are usually still called opsins regardless. Most prominently, they are found in photoreceptor cells of the retina. Five classical groups of opsins are involved in vision, mediating the conversion of a photon of light into an electrochemical signal, the first step in the visual transduction cascade. Another opsin found in the mammalian retina, melanopsin, is involved in circadian rhythms and pupillary reflex but not in vision. Humans have in total nine opsins. Beside vision and light perception, opsins may also sense temperature, sound, or chemicals. Structure and function Animal opsins detect light and are the molecules that allow us to see. Opsins are G-protein-coupled receptors (GPCRs), which are chemoreceptors and have seven transmembrane domains forming a binding pocket for a ligand ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Retinal
Retinal (also known as retinaldehyde) is a polyene chromophore. Retinal, bound to proteins called opsins, is the chemical basis of visual phototransduction, the light-detection stage of visual perception (vision). Some microorganisms use retinal to convert light into metabolic energy. In fact, a recent study suggests most living organisms on our planet ~3 billion years ago used retinal to convert sunlight into energy rather than chlorophyll. Since retinal absorbs mostly green light and transmits purple light, this gave rise to the Purple Earth Hypothesis. There are many forms of vitamin A — all of which are converted to retinal, which cannot be made without them. Retinal itself is considered to be a form of vitamin A when eaten by an animal. The number of different molecules that can be converted to retinal varies from species to species. Retinal was originally called retinene, and was renamed after it was discovered to be vitamin A aldehyde. Vertebrate animals ingest r ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Retinitis Pigmentosa
Retinitis pigmentosa (RP) is a genetic disorder of the eyes that causes loss of vision. Symptoms include trouble seeing at night and decreasing peripheral vision (side and upper or lower visual field). As peripheral vision worsens, people may experience " tunnel vision". Complete blindness is uncommon. Onset of symptoms is generally gradual and often begins in childhood. Retinitis pigmentosa is generally inherited from one or both parents or rarely it can be caused by a miscoding during DNA division. It is caused by genetic miscoding of proteins in one of more than 300 genes involved. The underlying mechanism involves the progressive loss of rod photoreceptor cells that line the retina of the eyeball. The rod cells secrete a neuroprotective substance (Rod-derived cone viability factor, RdCVF) that protects the cone cells from apoptosis (cell death). However, when the rod cells die, this substance is no longer provided. This is generally followed by the loss of cone photorece ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Visual Phototransduction
Visual phototransduction is the sensory transduction process of the visual system by which light is detected to yield nerve impulses in the rod cells and cone cells in the retina of the eye in humans and other vertebrates. It relies on the visual cycle, a sequence of biochemical reactions in which a molecule of retinal bound to opsin undergoes photoisomerization, initiates a cascade that signals detection of the photon, and is indirectly restored to its photosensitive isomer for reuse. Phototransduction in some invertebrates such as fruit flies relies on similar processes. Photoreceptors The photoreceptor cells involved in vertebrate vision are the rods, the cones, and the photosensitive ganglion cells (ipRGCs). These cells contain a chromophore ( 11-''cis''-retinal, the aldehyde of vitamin A1 and light-absorbing portion) that is bound to a cell membrane protein, opsin. Rods deal with low light level and do not mediate color vision. Cones, on the other hand, can code th ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
G-protein-coupled Receptor
G protein-coupled receptors (GPCRs), also known as seven-(pass)-transmembrane domain receptors, 7TM receptors, heptahelical receptors, serpentine receptors, and G protein-linked receptors (GPLR), form a large group of evolutionarily-related proteins that are cell surface receptors that detect molecules outside the cell and activate cellular responses. Coupling with G proteins, they are called seven-transmembrane receptors because they pass through the cell membrane seven times. Text was copied from this source, which is available under Attribution 2.5 Generic (CC BY 2.5) license. Ligands can bind either to extracellular N-terminus and loops (e.g. glutamate receptors) or to the binding site within transmembrane helices (Rhodopsin-like family). They are all activated by agonists although a spontaneous auto-activation of an empty receptor can also be observed. G protein-coupled receptors are found only in eukaryotes, including yeast, choanoflagellates, a ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Rod Cell
Rod cells are photoreceptor cells in the retina of the eye that can function in lower light better than the other type of visual photoreceptor, cone cells. Rods are usually found concentrated at the outer edges of the retina and are used in peripheral vision. On average, there are approximately 92 million rod cells (vs ~6 million cones) in the human retina. Rod cells are more sensitive than cone cells and are almost entirely responsible for night vision. However, rods have little role in color vision, which is the main reason why colors are much less apparent in dim light. Structure Rods are a little longer and leaner than cones but have the same basic structure. Opsin-containing disks lie at the end of the cell adjacent to the retinal pigment epithelium, which in turn is attached to the inside of the eye. The stacked-disc structure of the detector portion of the cell allows for very high efficiency. Rods are much more common than cones, with about 120 million rod cells com ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Vitamin A
Vitamin A is a fat-soluble vitamin and an essential nutrient for humans. It is a group of organic compounds that includes retinol, retinal (also known as retinaldehyde), retinoic acid, and several provitamin A carotenoids (most notably beta-carotene -carotene. Vitamin A has multiple functions: it is essential for embryo development and growth, for maintenance of the immune system, and for vision, where it combines with the protein opsin to form rhodopsin the light-absorbing molecule necessary for both low-light ( scotopic vision) and color vision. Vitamin A occurs as two principal forms in foods: A) retinol, found in animal-sourced foods, either as retinol or bound to a fatty acid to become a retinyl ester, and B) the carotenoids alpha-carotene, β-carotene, gamma-carotene, and the xanthophyll beta-cryptoxanthin (all of which contain β-ionone rings) that function as provitamin A in herbivore and omnivore animals which possess the enzymes that cleave and con ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Photoreceptor Protein
Photoreceptor proteins are light-sensitive proteins involved in the sensing and response to light in a variety of organisms. Some examples are rhodopsin in the photoreceptor cells of the vertebrate retina, phytochrome in plants, and bacteriorhodopsin and bacteriophytochromes in some bacteria. They mediate light responses as varied as visual perception, phototropism and phototaxis, as well as responses to light-dark cycles such as circadian rhythm and other photoperiodisms including control of flowering times in plants and mating seasons in animals. Structure Photoreceptor proteins typically consist of a protein attached to a non-protein chromophore (sometimes referred as photopigment, even so photopigment may also refer to the photoreceptor as a whole). The chromophore reacts to light via photoisomerization or photoreduction, thus initiating a change of the receptor protein which triggers a signal transduction cascade. Chromophores found in photoreceptors include retina ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cone Opsin
Vertebrate visual opsins are a subclass of ciliary opsins and mediate vision in vertebrates. They include the opsins in human rod and cone cells. They are often abbreviated to ''opsin'', as they were the first opsins discovered and are still the most widely studied opsins. Opsins Opsin refers strictly to the apoprotein (without bound retinal). When an opsin binds retinal to form a holoprotein, it is referred to as Retinylidene protein. However, the distinction is often ignored, and opsin may refer loosely to both (regardless of whether retinal is bound). Opsins are G-protein-coupled receptors (GPCRs) and must bind retinal — typically 11-''cis''-retinal — in order to be photosensitive, since the retinal acts as the chromophore. When the Retinylidene protein absorbs a photon, the retinal isomerizes and is released by the opsin. The process that follows the isomerization and renewal of retinal is known as the visual cycle. Free 11-''cis''-retinal is photosensitive and ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Congenital Stationary Night Blindness
Congenital stationary night blindness (CSNB) is a rare non-progressive retinal disorder. People with CSNB often have difficulty adapting to low light situations due to impaired photoreceptor transmission. These patients may also have reduced visual acuity, myopia, nystagmus, and strabismus. CSNB has two forms -- complete, also known as type-1 (CSNB1), and incomplete, also known as type-2 (CSNB2), which are distinguished by the involvement of different retinal pathways. In CSNB1, downstream neurons called bipolar cells are unable to detect neurotransmission from photoreceptor cells. CSNB1 can be caused by mutations in various genes involved in neurotransmitter detection, including ''NYX''. In CSNB2, the photoreceptors themselves have impaired neurotransmission function; this is caused primarily by mutations in the gene ''CACNA1F'', which encodes a voltage-gated calcium channel important for neurotransmitter release. CSNB has been identified in horses and dogs as the result of mutat ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cryptochrome
Cryptochromes (from the Greek κρυπτός χρώμα, "hidden colour") are a class of flavoproteins found in plants and animals that are sensitive to blue light. They are involved in the circadian rhythms and the sensing of magnetic fields in a number of species. The name ''cryptochrome'' was proposed as a ''portmanteau'' combining the '' chromatic'' nature of the photoreceptor, and the '' cryptogamic'' organisms on which many blue-light studies were carried out. The two genes ''Cry1'' and ''Cry2'' code the two cryptochrome proteins CRY1 and CRY2. In insects and plants, CRY1 regulates the circadian clock in a light-dependent fashion, whereas in mammals, CRY1 and CRY2 act as light-independent inhibitors of CLOCK- BMAL1 components of the circadian clock. In plants, blue-light photoreception can be used to cue developmental signals. Besides chlorophylls, cryptochromes are the only proteins known to form photoinduced radical-pairs '' in vivo''. These appear to enable some a ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
George Wald
George Wald (November 18, 1906 – April 12, 1997) was an American scientist who studied pigments in the retina. He won a share of the 1967 Nobel Prize in Physiology or Medicine with Haldan Keffer Hartline and Ragnar Granit. In 1970, Wald predicted that “civilization will end within 15 or 30 years unless immediate action is taken against problems facing mankind.” Research As a postdoctoral researcher, Wald discovered that vitamin A was a component of the retina. His further experiments showed that when the pigment rhodopsin was exposed to light, it yielded the protein opsin and a compound containing vitamin A. This suggested that vitamin A was essential in retinal function. In the 1950s, Wald and his colleagues used chemical methods to extract pigments from the retina. Then, using a spectrophotometer, they were able to measure the light absorbance of the pigments. Since the absorbance of light by retina pigments corresponds to the wavelengths that best activate ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
