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Two isoforms of chicken melanopsins show blue light sensitivity
Author(s) -
Torii Masaki,
Kojima Daisuke,
Okano Toshiyuki,
Nakamura Atsushi,
Terakita Akihisa,
Shichida Yoshinori,
Wada Akimori,
Fukada Yoshitaka
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.10.019
Subject(s) - melanopsin , photopigment , opsin , gene isoform , biology , circadian rhythm , pineal gland , retina , microbiology and biotechnology , intrinsically photosensitive retinal ganglion cells , retinal , vertebrate , rhodopsin , gene , endocrinology , neuroscience , genetics , biochemistry , retinal ganglion cell
Melanopsin is a vertebrate non‐visual opsin and functions as a circadian photoreceptor in mammalian retinas. Here we found the expression of two kinds of melanopsin genes in the chicken pineal gland and identified the presence of five isoforms derived from these two genes. Reconstitution of the recombinant proteins with 11‐ cis ‐retinal revealed that at least two of these melanopsin protein isoforms can function as blue‐sensitive photopigments with absorption maxima at 476–484 nm. These values are consistent with maximal sensitivities of action spectra determined from the physiological and behavioral studies on mammalian melanopsins. The melanopsin isoforms found in this study may function as pineal circadian photoreceptors.
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