Factbites
 Where results make sense
About us   |   Why use us?   |   Reviews   |   PR   |   Contact us  

Topic: Opsin


Related Topics
Eye

In the News (Wed 30 Dec 09)

  
  Opsin - Wikipedia, the free encyclopedia
Opsins are a group of light-sensitive 35-55 kDa membrane bound G protein-coupled receptors found in photoreceptor cells of the retina.
Cone opsins, employed in color vision, are low sensitivity, high acuity opsins located in the cone photoreceptor cells.
Opsin proteins covalently bind to a vitamin A-based retinaldehyde chromophore through a Schiff base linkage to a lysine residue in the seventh transmembrane alpha helix.
en.wikipedia.org /wiki/Opsin   (942 words)

  
 Opsin signature
Opsins are integral membrane proteins that belong to a superfamily of G- protein-coupled receptors (GPCRs).
Interestingly, the opsins also seem to be emerging as increasingly atypical of the superfamily, clustering most strongly, in phylogenetic analyses, with the olfactory receptors [4].
OPSIN is a 3-element fingerprint that provides a signature for the opsin family of GPCRs.
bioinf.man.ac.uk /dbbrowser/gpcrPRINTS/PR00238.html   (1294 words)

  
 retinalandrhodopsin
There are several different variants on the opsin molecules in organisms, and even slight differences in the cone cells of humans.
Different organisms have different opsins, and this is evident in the fact that many organisms see different wavelengths.
When the 11-cis-retinal is bound to an opsin, the delocalization of the electrons extends into the protein itself.
www.sas.upenn.edu /~tareilaj/retinalandrhodopsin.html   (412 words)

  
 Whiting Lab--Insect Genomics
All pigments consist of an opsin protein and a chromophore molecule, usually a carotene derivative.
Opsin variants can tune visual pigments to absorb wavelengths in the ultraviolet, blue, green, and red regions of the spectrum.
We have successfully amplified and sequenced the long-wavelength opsin gene from six individuals of fleas representing five families, and six individuals of scorpionflies.
whitinglab.byu.edu /flopsin.htm   (594 words)

  
 The Evolution of Color Vision
The main function of the opsin is to change shape after light absorption triggers the isomerization of the chromophore: the opsin is an enzyme that is activated by the chromophore's isomerization.
However, because of the linkage between the opsin and the chromophore, the opsin also serves to tune the wavelength dependence of the light induced isomerization reaction in the chromophore.
In at least one species, two of their opsin genes are (like our mid- and long- wave sensitive opsins) on the X chromosome.
talkorigins.org /faqs/vision.html   (4843 words)

  
 MAST634 Petrone   (Site not responding. Last check: 2007-10-09)
Opsin has been thoroughly studied in many organisms including fish, both of the euphotic and aphotic zones, rodents including mice and rats, and cows.
In the present study, the visual pigment protein opsin is compared in two crustaceans, the Japanese shore crab, Hemigrapsus sanguineus and the red swamp crayfish, also known as the Louisiana crayfish, Procambrus clarkii, in terms of protein sequences.
More, when the opsin protein sequences for the two crustaceans are aligned, only a 53.80 percent similarity is obtained.
www.udel.edu /chem/bahnson/Biochem3D/Projects/Petrone   (383 words)

  
 RHODOPSIN AS A CHEMICAL COMPLEX OF RHODONINE AND OPSIN
As a result, the chromophores of vision were deposited on the opsin substrates and thereby formed the complex conceptuallized as rhodopsin.
The opsin substrates were tracked until they were phagocytized by the RPE cells and the amino acids were returned to the blood stream associated with the choroid.
Rhodopsin as defined above is a chemical complex of Rhodonine and opsin that is non-functional in the absence of a de-excitation mechanism (the dendrites) and the associated electrical power source (the glutamate-based electrostenolytic mechanism) Both the dendrites and the electrostenolytic mechanism depend on the electrical conductivity of the IPM.
www.4colorvision.com /files/rhodopsin.htm   (2657 words)

  
 Circadian rhythms of behavioral cone sensitivity and long wavelength opsin mRNA expression: a correlation study in ...
In LD, the expression of LC opsin mRNA was low in the morning and high in the afternoon.
The increase of LC opsin mRNA expression by SKF38393
Expression of pineal ultraviolet- and green-like opsins in the pineal organ and retina of teleosts.
jeb.biologists.org /cgi/content/full/208/3/497   (4685 words)

  
 Medscape MEDLINE search: Opsin
Molecular genetic studies demonstrate that the human cone opsin gene array on the q-arm of the X-chromosome typically consists of one long-wave-sensitive (L) cone opsin gene and from one to several middle-wave-sensitive (M) cone opsin genes.
The visual receptor of rods and cones is a covalent complex of the apoprotein, opsin, and the light-sensitive chromophore, 11-cis-retinal.
Characterization of an opsin gene from the ascomycete Leptosphaeria maculans.
search.medscape.com /uslclient/searchMedline.do?queryText=Opsin   (1077 words)

  
 Characterization of the Long-Wavelength Opsin from Mecoptera and Siphonaptera: Does a Flea See? -- Taylor et al. 22 ...
PCR amplification of the LW opsin gene for the Mecoptera and
Characterization of the ultraviolet-sensitive opsin gene in the honey bee, Apis mellifera.
Spatial expression of opsins in the retina and brain of the tiger swallotail Papilio glaucus.
mbe.oxfordjournals.org /cgi/content/full/22/5/1165   (4664 words)

  
 Ostrer, Mol Vis 1998; 4:28.
The genes for red and green cone opsins are found in a tandem array on the distal long arm of the X chromosome, which may contain varying copy numbers of red, green and red/green hybrid genes; the blue opsin gene is a single-copy locus located at 7q22-qter [8-10].
The cone opsins share 40-44% homology with rhodopsin at the amino acid level, suggesting similar structures (The structure for the green opsin gene is shown in Figure 1) [8].
The green cone opsin differs from these other 7-transmembranous segment receptor proteins by not requiring glycosylation for signal transduction; however, the possibility cannot be excluded that unglycosylation of the cone opsin might have subtle effects on the stability of the protein that were not tested in this series of experiments.
www.molvis.org /molvis/v4/P28   (2452 words)

  
 Biosynthesis and vectorial transport of opsin on vesicles in retinal rod photoreceptors -- Papermaster et al. 34 (1): 5 ...
Biosynthesis and vectorial transport of opsin on vesicles in retinal rod photoreceptors -- Papermaster et al.
opsin, is released from the Golgi in the membranes of small vesicles.
opsin is detectable in the inner segment plasma membrane, although its
www.jhc.org /cgi/content/abstract/34/1/5   (503 words)

  
 Different Transmembrane Domains Associate with Distinct Endoplasmic Reticulum Components during Membrane Integration of ...
A set of 130-residue membrane integration intermediates of opsin (OP130) with a single cysteine probe located at residue 47-51 of TM1 were treated with BMH as described for Figure 1.
The position of this opsin fragment is indicated by a white triangle (lanes 22, 29, 36, 43, and 50).
TM1 of the original opsin integration intermediates (OP) was replaced by inserting the amino acid sequence of opsin TM2 in place of TM1.
www.molbiolcell.org /cgi/content/full/13/12/4114   (9179 words)

  
 Red/green-sensitive opsin signature
Opsins, the light-absorbing molecules that mediate vision [1,2], are integral membrane proteins that belong to a superfamily of G protein-coupled receptors (GPCRs).
The covalent link is in the form of a protonated Schiff base between the retinal and a lysine residue located in TM domain 7.
Opsins are the photoreceptors of animal retinas [5]: vertebrate rhodopsin is found in rod cells and mediates scotopic vision; red, green and blue opsins are found in cone cells and mediate photopic vision.
bioinf.man.ac.uk /dbbrowser/gpcrPRINTS/PR00575.html   (599 words)

  
 Opsin Photoisomerases in the Chick Retina and Pineal Gland: Characterization, Localization, and Circadian Regulation -- ...
Parapinopsin, a novel catfish opsin localized to the parapineal organ, defines a new gene family.
An opsin homologue in the retina and pigment epithelium.
The endogenous chromophore of retinal G protein-coupled receptor opsin from the pigment epithelium.
www.iovs.org /cgi/content/full/45/3/769   (4101 words)

  
 Myosin VIIa Participates in Opsin Transport through The Photoreceptor Cilium -- Liu et al. 19 (15): 6267 -- Journal of ...
Besharse JC, Wetzel MG (1995) Immunocytochemical localization of opsin in rod photoreceptors during periods of rapid disc assembly.
Nir I, Sagie G, Papermaster DS (1987) Opsin accumulation in photoreceptor inner segment plasma membranes of dystrophic RCS rats.
Papermaster DS, Schneider BG, Besharse JC (1985) Vesicular transport of newly synthesized opsin from the Golgi apparatus toward the rod outer segment.
www.jneurosci.org /cgi/content/full/19/15/6267   (6591 words)

  
 Chemicon - Product #AB5405 - Anti-Opsin, Red/Green
All three opsins are transmembrane proteins with seven membrane-spanning regions.
Strongest conservation is between the middle (green) and long (red) wavelength sensitive pigments on the X chromosome, suggesting a relatively recent duplication/divergence event (Nathans, 1989; Nathans et al., 1992).
The S cone (blue) opsin is located on chromosome 7 and seems to have stronger conservation with rhodopsin.
www.chemicon.com /browse/productdetail.asp?ProductID=AB5405   (407 words)

  
 Occupancy of the Chromophore Binding Site of Opsin Activates Visual Transduction in Rod Photoreceptors -- Kefalov et ...
opsin alone is sufficient for catalytic activation of the complex.
The state of opsin that is responsible for bleaching adaptation is a matter of controversy.
Noncovalent occupancy of the retinal-binding pocket of opsin diminishes bleaching adaptation of retinal cones.
www.jgp.org /cgi/content/full/113/3/491   (6602 words)

  
 Bee Phylogeny
Plasmids containing opsin inserts were isolated and sequenced using an ABI 373A automated sequencer.
Our opsin data set spans positions 434 to 1146 of the coding region in the Apis mellifera LW opsin paralog (Chang et al.
The major opsin in bees (Insecta: Hymenoptera): a promising nuclear gene for higher level phylogenetics.
www.entomology.cornell.edu /BeePhylogeny/rhodopsin.html   (487 words)

  
 Rex, Mol Vis 2002; 8:114-118.
In particular, we found significant differences for the pattern of expression of opsin in rods and cones, which may reflect different mechanisms for survival in these two types of photoreceptors.
Rod opsin immunolabeling remained robust even in detachments of 60 days duration [14] and, using Northern blot and in situ hybridization analysis [15], it was demonstrated that rod opsin mRNA continues to be expressed in long-term detached retinas.
Photoreceptor cells labeled with either the anti-sense probe for S-cone opsin or M-cone opsin were counted in 20 sections each of normal, detached, and reattached, mid-peripheral retina.
www.molvis.org /molvis/v8/a15   (2979 words)

  
 Gene Duplication and Spectral Diversification of Cone Visual Pigments of Zebrafish -- Chinen et al. 163 (2): 663 -- ...
Alignment of the deduced amino acid sequences of the zebrafish cone opsins.
The relative efficiencies of reverse transcription among the zebrafish opsin genes.
The relative expression levels of the cone opsin genes in the zebrafish eye measured by the real-time RT-PCR for (A) a 1-year-old fish at 1.5 hr after the onset of the light and (B) a 2-month-old fish at 7 hr after it.
www.genetics.org /cgi/content/full/163/2/663   (6946 words)

  
 Vertebrate Ancient-Long Opsin: A Green-Sensitive Photoreceptive Molecule Present in Zebrafish Deep Brain and Retinal ...
co-transfected with the opsin expression vector and pRSV-TAg and
Blackshaw S, Snyder SH (1997) Parapinopsin, a novel catfish opsin localized to the parapineal organ, defines a new gene family.
Foster RG, Follett BK, Lythgoe JN (1985) Rhodopsin-like sensitivity of extra-retinal photoreceptors mediating the photoperiodic response in quail.
www.jneurosci.org /cgi/content/full/20/8/2845   (4880 words)

  
 Pharyngula::Rhabdomeric and ciliary eyes
Light activates opsin by causing a conformation change in the photopigment, and opsin then binds to a G-protein, a common and versatile molecule used in many signal transduction cascades.
Early metazoans possessed a single type of precursor PRC [photoreceptor cell] that used an ancestral opsin for light detection and was involved in photoperiodicity control and possibly in phototaxis.
In prebilaterian ancestors, the opsin gene then duplicated into two paralogs, c-opsin and r-opsin, allowing the diversification of the precursor PRC into ciliary and rhabdomeric sister cell types.
pharyngula.org /index/weblog/comments/rhabdomeric_and_ciliary_eyes   (1889 words)

  
 source2
The inactive opsin binds 11-cis-retinal chromophore, is stabilized by the salt bridge between Glu113 and Lys296, and does not activate transducin.
The mutant opsin expressed in COS cells resembled wild-type rhodopsin in its spectral characteristics and its ability for the light-dependent activation of transducin.
However, in the absence of chromophore, the Ala292Glu mutant opsin was different from the wild-type opsin in that it activated transducin constitutively, just as the Glu113 or Lys296 mutant opsin (9).
www.cc.utah.edu /~kz30a50/source2.html   (1821 words)

  
 The cellular fate of mutant rhodopsin: quality control, degradation and aggresome formation -- Saliba et al. 115 (14): ...
Mutant opsin inclusions have the characteristics of an aggresome.
increase in the incidence of wild-type opsin aggresomes (Fig.
(A) GFP-tagged WT opsin in pEGFP was co-transfected with untagged WT opsin in pMT3 (WT-GFP/WT-opsin) at a vector ratio of 1:10.
jcs.biologists.org /cgi/content/full/115/14/2907   (7379 words)

  
 Rod photoreceptors, rod outer segment, rhodopsin, rod opsin, retinal degeneration, mouse UV cones, vitamin A ...
In the fly, carotenoid deprivation and replacement are relatively straightforward manipulations; in the vertebrate this is not the case, which may explain the relative paucity of such data in higher animals.
Upon administration of vitamin A to deprived animals, the opsin in these diminished outer segments recovers rapidly to functional rhodopsin; moreover, the outer segments recover in about two weeks, a time frame consistent with the turnover of an outer segment, as judged mainly by electroretinographic recording done by D.-M. Chen, in my laboratory.
A freeze fracture micrograph of a rod from the Katz et al 1991 work showing that the opsin density was the same in vitamin A deprived (B) and replete (A) rats.
starklab.slu.edu /vertvitA.htm   (791 words)

  
 Retinoids, retinoic acid, opsin gene expression in Drosophila, RA, RARE, RAR, GFP, UAS-GAL4, promoter-reporter, vitamin ...
Finally, we obtained these results from gel retardation: A consistent concentration of fly head extract retarded mobility of a labeled PCR fragment of the opsin promoter (-739 to -464); no retardarion for BSA control.
Sapp, R, J., Christianson, J. S., Stark, W. Turnover of membrane and opsin in visual receptors of normal and mutant Drosophila.
L., Marietta, R. G., Stark, W. Control of Drosophila opsin gene expression by carotenoids and retinoic acid: Northern and Western analyses.
starklab.slu.edu /vitArepl.htm   (509 words)

Try your search on: Qwika (all wikis)

Factbites
  About us   |   Why use us?   |   Reviews   |   Press   |   Contact us  
Copyright © 2005-2007 www.factbites.com Usage implies agreement with terms.