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Cones, retinal opsins

Foster Simplistically, in entrainment the rods and cones provide transitional information at the sharp junction between a LD cycle, and the inner retinal opsins provide irradiance information. What was striking about that rodless-coneless mouse under dim LD cycles is that it was phase advanced and the onsets were bouncing all over the place. Something about the precision of entrainment is lost with the rods and cones under relatively low light conditions. [Pg.45]

Land and marine animals possess rhodopsin. Certain freshwater fish and some amphibians have the pigment porphyropsin in place of rhodopsin. The function of porphyropsin is analogous to that of rhodopsin, and it contains 3-dehydroretinal in place of retinal. Cyanopsin (dehydroretinal + cone-type opsin) is found in the retinas of most freshwater fish. [Pg.716]

The distribution of rods and cones is shown in Figure 3b centered about the fovea, the area of the retina that has the highest concentration of cones with essentially no rods and also has the best resolving capabiUty, with a resolution about one minute of arc. The fovea is nominally taken as a 5° zone, with its central 1° zone designated the foveola. There are about 40 R and 20 G cones for each B cone in the eye as a whole, whereas in the fovea there are almost no B cones. A result of this is that color perception depends on the angle of the cone of light received by the eye. The extremely complex chemistry involved in the stimulation of opsin molecules, such as the rhodopsin of the rods, and the neural connections in the retinal pathway are well covered in Reference 21. [Pg.407]

In colour vision there are three specific types of cone cell corresponding to red, green and blue receptors. The chromophore is the same for all three colours, being 11-cis-retinal bound to a protein which is structurally similar to opsin. Colour selectivity is achieved by positioning specific amino acid side chains along the chromophore so as to perturb the absorption spectrum of the chromophore. [Pg.222]

In photoreceptor cells, the rods and cones of the human retina, the retinal is linked to a specific protein termed opsin. The resulting pigment is known as rhodopsin. When a photon of light of the proper wavelength hits a molecule of rhodopsin, two chemical events take place. First, the ll-c -retinal is converted to the all-trans form and, secondly, the all-trani-retinal is released from the rhodopsin ... [Pg.194]

There are several different rhodopsins in the cones. All of them contain retinal molecules as light-sensitive components, the absorption properties of which are modulated by the different proportions of opsin they... [Pg.358]

Vitamin A is essential for proper functioning of the retina, for the integrity of epithelial tissue, for growth and bone development and for reproduction. For vision the active vitamin appears to be retinal as the chromophore of both rods and cones is 11-cis-retinal which, in combination with the protein opsin, forms the photoreceptor rhodopsin. Retinoic acid is the active form associated with growth, differentiation, and transformation. Both all-trans and 9-cis retinoic acid act as a steroid hormone to affect cellular differentiation, especially for morphogenesis, reproduction and for immune responses. At... [Pg.475]

The evidence to-date shows that vertebrate photoreception is mediated by a closely related group of proteins termed opsins. These are G protein-coupled receptors characterized by their ability to bind a vitamin A based chromophore ( -cis-retinal) via a Schiff base linkage using a lysine residue in the 7th transmembrane a helix (Fig. 1). The primary events of image detection by the rods and cones occurs with the absorption of a photon of light by ll-r/r-retinal and its photoisomerization to the AUtrans state (Bums Baylor 2001, Menon et al 2001). Although photoreception is best understood in retinal rods and cones, photoreception is not confined to these structures. In non-mammalian... [Pg.3]

Studies on teleost fish and mammals have demonstrated the existence of non-rod, non-cone ocular photoreceptors. In the case of VA opsin in the roach, electrophysiological evidence suggests that one function of this photosensory photopigment is to modulate the activity of retinal horizontal cells. To what end remains unclear, but this fits with the general role of horizontal cells in the teleost... [Pg.17]

Gtl/ Gt2 Photons (rhodopsin and color opsins in retinal rod and cone cells) t cGMP phosphodiesterase - cGMP (phototransduction)... [Pg.44]

The light-sensitive protein complex in the rods, rho-dopsin, consists of 1 l-c/s-retinal bound as a Schiff s base to a protein, opsin. Rhodopsin is an integral constituent of membranes that form a stack of disks at one end of the cell. Cone cells, which are responsible for the perception of color, contain similar complexes in infoldings of the plasma membrane. [Pg.624]

One example of this process is found in the chemistry of vision. Ill the rods and cones of the eye, the aldehyde 11 -cis-retinal forms an imine by reaction with an amino group of the protein opsin. Studies have shown that the nitrogen of the imine of the product, called rhodopsin. is protonated. [Pg.773]

VKainin A (retinol) is present in many cells of the body. In the retina it is part of the rod photoreceptor pigment rhodopsin (=cis-retina] + a protein called opsin) and cone photoreceptor pigment iodopsin (= cis-retinal + a different opsin protein). When light strikes the cis-retinal part of the rhodopsin or iodopsin molecule, the "cis form changes to trans-retinal, a conformational in (he t i04 culv ti.c CIjUaU... [Pg.43]


See other pages where Cones, retinal opsins is mentioned: [Pg.5]    [Pg.39]    [Pg.139]    [Pg.125]    [Pg.125]    [Pg.95]    [Pg.493]    [Pg.715]    [Pg.2495]    [Pg.505]    [Pg.16]    [Pg.588]    [Pg.316]    [Pg.814]    [Pg.149]    [Pg.147]    [Pg.194]    [Pg.340]    [Pg.3]    [Pg.13]    [Pg.14]    [Pg.17]    [Pg.19]    [Pg.32]    [Pg.37]    [Pg.64]    [Pg.457]    [Pg.460]    [Pg.380]    [Pg.1328]    [Pg.616]    [Pg.13]    [Pg.161]    [Pg.285]    [Pg.505]   
See also in sourсe #XX -- [ Pg.126 ]

See also in sourсe #XX -- [ Pg.126 ]




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Opsin-retinal

Retin

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