Molecular properties of rod and cone visual pigments from purified chicken cone pigments to mouse rhodopsin in situ

2005 ◽  
Vol 4 (9) ◽  
pp. 667 ◽  
Author(s):  
Hiroo Imai ◽  
Shigeki Kuwayama ◽  
Akishi Onishi ◽  
Takefumi Morizumi ◽  
Osamu Chisaka ◽  
...  
Keyword(s):  
Visual Pigments ◽  
Molecular Properties ◽  
Cone Pigments

The visual pigments of wild white sturgeon (Acipenser transmontanus)

1995 ◽  
Vol 73 (4) ◽  
pp. 805-809 ◽  
Author(s):  
A. J. Sillman ◽  
M. E. Sorsky ◽  
E. R. Loew
Keyword(s):  
Vitamin A ◽  
Fresh Water ◽  
Visual Pigment ◽  
Visual Pigments ◽  
White Sturgeon ◽  
Acipenser Transmontanus ◽  
Estuarine Water ◽  
Cone Pigments ◽  
Partial Bleaching

The visual pigments of the anadromous white sturgeon (Acipenser transmontanus) taken from relatively saline estuarine water were characterized by means of in situ microspectrophotometry and partial bleaching analysis of a digitonin extract. The three cone pigments (λmax = 605, 539, and ca. 460 nm) and one rod pigment (λmax = 541 nm) of the wild sturgeon are the same as those of cultured sturgeon that spend their entire lives in fresh water. All the visual pigments incorporate a chromophore based on vitamin A2. Unlike other anadromous fishes during the "saline phase," the white sturgeon shows no evidence of the presence of any vitamin A1 based visual pigment in the retina.

The visual pigments of the bottlenose dolphin (Tursiops truncatus)

1998 ◽  
Vol 15 (4) ◽  
pp. 643-651 ◽  
Author(s):  
JEFFRY I. FASICK ◽  
THOMAS W. CRONIN ◽  
DAVID M. HUNT ◽  
PHYLLIS R. ROBINSON
Keyword(s):  
Color Vision ◽  
Bottlenose Dolphin ◽  
Visual Pigments ◽  
Nucleotide Position ◽  
Long Wavelength ◽  
Terrestrial Mammals ◽  
Cone Opsin ◽  
Cone Pigments ◽  
The Common

To assess the dolphin's capacity for color vision and determine the absorption maxima of the dolphin visual pigments, we have cloned and expressed the dolphin opsin genes. On the basis of sequence homology with other mammalian opsins, a dolphin rod and long-wavelength sensitive (LWS) cone opsin cDNAs were identified. Both dolphin opsin cDNAs were expressed in mammalian COS-7 cells. The resulting proteins were reconstituted with the chromophore 11-cis-retinal resulting in functional pigments with absorption maxima (λmax) of 488 and 524 nm for the rod and cone pigments respectively. These λmax values are considerably blue shifted compared to those of many terrestrial mammals. Although the dolphin possesses a gene homologous to other mammalian short-wavelength sensitive (SWS) opsins, it is not expressed in vivo and has accumulated a number of deletions, including a frame-shift mutation at nucleotide position 31. The dolphin therefore lacks the common dichromatic form of color vision typical of most terrestrial mammals.

The photoreceptors and visual pigments in the retina of the white sturgeon, Acipenser transmontanus

1990 ◽  
Vol 68 (7) ◽  
pp. 1544-1551 ◽  
Author(s):  
A. J. Sillman ◽  
M. D. Spanfelner ◽  
E. R. Loew
Keyword(s):  
Vitamin A ◽  
Visual Pigment ◽  
Visual Pigments ◽  
Spectrophotometric Analysis ◽  
White Sturgeon ◽  
Acipenser Transmontanus ◽  
Light Regimen ◽  
Cone Pigment ◽  
Spectral Absorbance

The photoreceptors in the retina of the white sturgeon, Acipenser transmontanus (Chondrostei), were studied by means of scanning electron microscopy, in situ microspectrophotometry, and spectrophotometric analysis of visual pigment extracts. The white sturgeon retina is simple in that it contains only two morphologically distinct photoreceptors. The retina is dominated by rods with large outer segments, but there is a substantial population (40%) of single cones. Evidence was found for only one rod visual pigment and one cone visual pigment. Peak spectral absorbance (λmax) of the rod pigment is near 539 nm, whereas λmax of the cone pigment is near 605 nm. Both visual pigments are porphyropsin types with chromophores based on vitamin A2. No detectable rhodopsin based on vitamin A1 is ever present, regardless of season or light regimen. The results are discussed in terms of the sturgeon's behavior, as well as the implications for the evolution of color vision.

Photic Environment, Visual Pigments, and the Limits of the Visible Spectrum

Perception ◽  
1997 ◽  
Vol 26 (1_suppl) ◽  
pp. 160-160
Author(s):  
V I Govardovskii
Keyword(s):  
Visible Spectrum ◽  
Blue Shift ◽  
Short Wave ◽  
Visual Pigments ◽  
Limiting Factor ◽  
Spectral Position ◽  
Dark Noise ◽  
Water Fish ◽  
Cone Pigments ◽  
Purkinje Shift

The limits of the visible spectrum are set by the light available for vision, and by the visual pigment absorbance. The hundreds of visual pigments studied to the present day have absorbance maxima spread within the range from 350 to 620 nm. Yet this diversity is used for vision quite nonuniformly: rod and cone visual pigments are tightly clustered around a few preferred positions in the spectrum, eg near 500 nm in the rods of land animals. The so-called ‘sensitivity hypothesis’ assumes that the clustering is to maximise the number of absorbed photons available in the animals' light environment. In most cases, however, visual pigments are substantially more short-wave (blue-shifted) than is necessary for maximum quantal absorption. Examples of the ‘blue shift’ are the Purkinje shift during cone - rod transition in dark adaptation, the hypsochromic shift of rod visual pigments in deep-water fish, and a similar shift in the cone pigments of geckos and some snakes as a result of evolutionary adaptation to nocturnal habits. It is argued that an important limiting factor in vision is the dark noise produced by thermal isomerisation of the chromophore. Measurements of the dark noise in rods with different visual pigments show that the noise increases steeply when the absorbance maximum is shifted to longer wavelengths, thus precluding the use of long-wave pigments for vision at low intensities. The optimum spectral position of a pigment may be that which ensures a maximum light-to-noise ratio in a particular photic environment.

The effect of light history on the photolysability of human visual pigments in situ

1966 ◽  
Vol 164 (994) ◽  
pp. 96-105 ◽  
Keyword(s):  
Spectral Composition ◽  
Difference Spectra ◽  
Variable Intensity ◽  
Density Spectrum ◽  
Cone Pigments ◽  
History Of ◽  
Fundus Reflectometry ◽  
Light History

The foveae of two subjects were studied by the method of rapid fundus reflectometry (RFR). Difference spectra were obtained after the eye had dark-adapted for at least 12 min and then been exposed to a bleaching light of variable intensity and spectral composition. It is found that if the period of dark-adaptation is preceded by an exposure to intense light, designed to eliminate the previous light history of the retina, the density spectrum is lower than in the absence of such a clearing exposure, provided the latter is such as to furnish on average more than one quantum per visual pigment molecule within approximately 500 msec. It is shown that, within limits, cone pigments studied with RFR show properties similar to those obtained with visual purple in vitro .

Two opsins from the compound eye of the crab Hemigrapsus sanguineus

1996 ◽  
Vol 199 (2) ◽  
pp. 441-450 ◽  
Author(s):  
K Sakamoto ◽  
O Hisatomi ◽  
F Tokunaga ◽  
E Eguchi
Keyword(s):  
Photoreceptor Cell ◽  
Compound Eye ◽  
Visual Pigments ◽  
Amino Acid Residues ◽  
Hemigrapsus Sanguineus ◽  
Brachyuran Crab ◽  
Maximal Absorption ◽  
Retinular Cells ◽  
Cdna Nucleotide

The primary structures of two opsins from the brachyuran crab Hemigrapsus sanguineus were deduced from the cDNA nucleotide sequences. Both deduced proteins were composed of 377 amino acid residues and included residues highly conserved in visual pigments of other species, and the proteins were 75 % identical to each other. The distribution of opsin transcripts in the compound eye, determined by in situ hybridization, suggested that the mRNAs of the two opsins were expressed simultaneously in all of the seven retinular cells (R1-R7) forming the main rhabdom in each ommatidium. Two different visual pigments may be present in one photoreceptor cell in this brachyuran crab. The spectral sensitivity of the compound eye was also determined by recording the electroretinogram. The compound eye was maximally sensitive at about 480 nm. These and previous findings suggest that both opsins of this brachyuran crab produce visual pigments with maximal absorption in the blue-green region of the spectrum. Evidence is presented that crustaceans possess multiple pigment systems for vision.

scholarly journals Inflammatory pain alters blood-brain barrier permeability and tight junctional protein expression

2001 ◽  
Vol 280 (3) ◽  
pp. H1241-H1248 ◽  
Author(s):  
J. D. Huber ◽  
K. A. Witt ◽  
S. Hom ◽  
R. D. Egleton ◽  
K. S. Mark ◽  
...  
Keyword(s):  
Protein Expression ◽  
Western Blot ◽  
Blood Brain Barrier ◽  
Inflammatory Pain ◽  
Molecular Properties ◽  
Brain Barrier ◽  
Peripheral Inflammation ◽  
Blood Brain ◽  
Junctional Protein

Effects of inflammatory pain states on functional and molecular properties of the rat blood-brain barrier (BBB) were investigated. Inflammation was produced by subcutaneous injection of formalin, λ-carrageenan, or complete Freund's adjuvant (CFA) into the right hind paw. In situ perfusion and Western blot analyses were performed to assess BBB integrity after inflammatory insult. In situ brain perfusion determined that peripheral inflammation significantly increased the uptake of sucrose into the cerebral hemispheres. Capillary depletion and cerebral blood flow analyses indicated the perturbations were due to increased paracellular permeability rather than vascular volume changes. Western blot analyses showed altered tight junctional protein expression during peripheral inflammation. Occludin significantly decreased in the λ-carrageenan- and CFA-treated groups. Zonula occluden-1 expression was significantly increased in all pain models. Claudin-1 protein expression was present at the BBB and remained unchanged during inflammation. Actin expression was significantly increased in the λ-carrageenan- and CFA-treated groups. We have shown that inflammatory-mediated pain alters both the functional and molecular properties of the BBB. Inflammatory-induced changes may significantly alter delivery of therapeutic agents to the brain, thus affecting dosing regimens during chronic pain.

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