scholarly journals Probing Human Red Cone Opsin Activity with Retinal Analogues

2011 ◽  
Vol 74 (3) ◽  
pp. 391-394 ◽  
Author(s):  
Masahiro Kono ◽  
Rosalie K. Crouch
Keyword(s):  
Cone Opsin ◽  
Retinal Analogues

Cone visual pigments of aquatic mammals

2005 ◽  
Vol 22 (6) ◽  
pp. 873-879 ◽  
Author(s):  
LUCY A. NEWMAN ◽  
PHYLLIS R. ROBINSON
Keyword(s):  
Color Vision ◽  
Mammalian Cells ◽  
Marine Mammals ◽  
Light Availability ◽  
Splice Site Mutation ◽  
Harbor Seal ◽  
Site Mutation ◽  
Cetacean Species ◽  
Cone Opsin ◽  
Aquatic Mammals

It has long been hypothesized that the visual systems of animals are evolutionarily adapted to their visual environment. The entrance many millions of years ago of mammals into the sea gave these new aquatic mammals completely novel visual surroundings with respect to light availability and predominant wavelengths. This study examines the cone opsins of marine mammals, hypothesizing, based on previous studies [Fasick et al. (1998) and Levenson & Dizon (2003)], that the deep-dwelling marine mammals would not have color vision because the pressure to maintain color vision in the dark monochromatic ocean environment has been relaxed. Short-wavelength-sensitive (SWS) and long-wavelength-sensitive (LWS) cone opsin genes from two orders (Cetacea and Sirenia) and an additional suborder (Pinnipedia) of aquatic mammals were amplified from genomic DNA (for SWS) and cDNA (for LWS) by PCR, cloned, and sequenced. All animals studied from the order Cetacea have SWS pseudogenes, whereas a representative from the order Sirenia has an intact SWS gene, for which the corresponding mRNA was found in the retina. One of the pinnipeds studied (harp seal) has an SWS pseudogene, while another species (harbor seal) appeared to have an intact SWS gene. However, no SWS cone opsin mRNA was found in the harbor seal retina, suggesting a promoter or splice site mutation preventing transcription of the gene. The LWS opsins from the different species were expressed in mammalian cells and reconstituted with the 11-cis-retinal chromophore in order to determine maximal absorption wavelengths (λmax) for each. The deeper dwelling Cetacean species had blue shifted λmax values compared to shallower-dwelling aquatic species. Taken together, these findings support the hypothesis that in the monochromatic oceanic habitat, the pressure to maintain color vision has been relaxed and mutations are retained in the SWS genes, resulting in pseudogenes. Additionally, LWS opsins are retained in the retina and, in deeper-dwelling animals, are blue shifted in λmax.

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.

Use of retinal analogues for the study of visual pigment function

2002 ◽  
pp. 29-48 ◽  
Author(s):  
Rosalie K. Crouch ◽  
Vladimir Kefalov ◽  
Wolfgang Gartner ◽  
M. Carter Cornwall
Keyword(s):  
Visual Pigment ◽  
Retinal Analogues

A Novel Missense Mutation in Both OPN1LW and OPN1MW Cone Opsin Genes Causes X-Linked Cone Dystrophy (XLCOD5)

2011 ◽  
pp. 595-601 ◽  
Author(s):  
Jessica C. Gardner ◽  
Tom R. Webb ◽  
Naheed Kanuga ◽  
Anthony G. Robson ◽  
Graham E. Holder ◽  
...  
Keyword(s):  
Missense Mutation ◽  
Cone Dystrophy ◽  
Cone Opsin ◽  
Opsin Genes

Synthesis of C11-to-C14 methyl-shifted all-trans-retinal analogues and their activities on human aldo-keto reductases

2020 ◽  
Vol 18 (25) ◽  
pp. 4788-4801
Author(s):  
Aurea Rivas ◽  
Raquel Pequerul ◽  
Vito Barracco ◽  
Marta Domínguez ◽  
Susana López ◽  
...  
Keyword(s):  
Vitamin A ◽  
Retinal Analogues

Human aldo-keto reductases (AKRs) are enzymes involved in the reduction, among other substrates, of all-trans-retinal to all-trans-retinol (vitamin A), thus contributing to the control of the levels of retinoids in organisms.

Three cone opsin genes and cone cell arrangement in retina of juvenile Pacific bluefin tuna Thunnus orientalis

2008 ◽  
Vol 74 (2) ◽  
pp. 314-321 ◽  
Author(s):  
Taeko MIYAZAKI ◽  
Jun KOHBARA ◽  
Kenji TAKII ◽  
Yasunori ISHIBASHI ◽  
Hidemi KUMAI
Keyword(s):  
Bluefin Tuna ◽  
Pacific Bluefin Tuna ◽  
Thunnus Orientalis ◽  
Cone Cell ◽  
Cone Opsin ◽  
Cell Arrangement ◽  
Opsin Genes
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