Distribution of melanopsin positive neurons in pigmented and albino mice: evidence for melanopsin interneurons in the mouse retina [PDF]
Here we have studied the population of intrinsically photosensitive retinal ganglion cells (ipRGCs) in adult pigmented and albino mice. Our data show that although pigmented (C57Bl/6) and albino (Swiss) mice have a similar total number of ipRGCs, their distribution is slightly different: while in pigmented mice ipRGCs are more abundant in the temporal ...
Valiente-Soriano, FJ +8 more
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β-Arrestin-dependent deactivation of mouse melanopsin.
In mammals, the expression of the unusual visual pigment, melanopsin, is restricted to a small subset of intrinsically photosensitive retinal ganglion cells (ipRGCs), whose signaling regulate numerous non-visual functions including sleep, circadian ...
Evan G Cameron, Phyllis R Robinson
doaj +2 more sources
Loss of gq/11 genes does not abolish melanopsin phototransduction. [PDF]
In mammals, a subset of retinal ganglion cells (RGCs) expresses the photopigment melanopsin, which renders them intrinsically photosensitive (ipRGCs). These ipRGCs mediate various non-image-forming visual functions such as circadian photoentrainment and ...
Kylie S Chew +4 more
doaj +2 more sources
Evolution of melanopsin photoreceptors: discovery and characterization of a new melanopsin in nonmammalian vertebrates. [PDF]
In mammals, the melanopsin gene (Opn4) encodes a sensory photopigment that underpins newly discovered inner retinal photoreceptors. Since its first discovery in Xenopus laevis and subsequent description in humans and mice, melanopsin genes have been ...
James Bellingham +9 more
doaj +7 more sources
Melanopsin phototransduction: beyond canonical cascades [PDF]
ABSTRACT Melanopsin is a visual pigment that is expressed in a small subset of intrinsically photosensitive retinal ganglion cells (ipRGCs). It is involved in regulating non-image forming visual behaviors, such as circadian photoentrainment and the pupillary light reflex, while also playing a role in many aspects of image-forming vision,
Ely Contreras +3 more
openaire +3 more sources
Form vision from melanopsin in humans [PDF]
AbstractDetection and discrimination of spatial patterns is thought to originate with photoreception by rods and cones. Here, we investigated whether the inner-retinal photoreceptor melanopsin could represent a third origin for form vision. We developed a 4-primary visual display capable of presenting patterns differing in contrast for melanopsin vs ...
Annette E. Allen +2 more
openaire +4 more sources
Melanopsin expressing retinal ganglion cells represent a third class of ocular photoreceptors and are involved in irradiance detection and non-image-forming responses to light including pupil constriction, circadian entrainment, and regulation of sleep ...
Steven Hughes +3 more
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Melanopsin-Mediated Post-Illumination Pupillary Response in Idiopathic Rapid Eye Movement (REM) Sleep Behavior Disorder and Parkinson's Disease. [PDF]
Abstract Aims To conduct a case–control study to investigate melanopsin‐mediated post‐illumination pupillary response (PIPR) in patients with Parkinson's disease (PD), video‐polysomnography‐confirmed isolated/idiopathic rapid eye movement (REM) sleep behavior disorder (iRBD), and age‐matched healthy controls (HC). Methods PIPR was measured at 6 s after
Chan JWY +16 more
europepmc +2 more sources
Impact of Human Melanopsin Gene (OPN4) Polymorphisms (I394T, P10L) on Nocturnal Melatonin and Daily Rhythms in Young Adults. [PDF]
ABSTRACT The present study investigates the impact of two missense SNPs in the human melanopsin gene OPN4 ‐I394T (rs1079610) and P10L (rs2675703)‐ on non‐image‐forming (NIF) physiological and behavioural outputs in healthy young adults under real‐world conditions.
Vicente-Martínez J +5 more
europepmc +2 more sources
What are opsins? Opsins are generally considered members of the superfamily of G-protein coupled receptors. But not all opsins activate a G-protein. Their distinguishing features are a 7 transmembrane α-helical structure, and an ability to bind a vitamin A chromophore, retinaldehyde, using a lysine in the 7th α-helix.
Foster, Russell, Bellingham, James
openaire +3 more sources

