Literature DB >> 17001087

Cyclic nucleotide-gated ion channels in rod photoreceptors are protected from retinoid inhibition.

Quanhua He1, Dmitriy Alexeev, Maureen E Estevez, Sarah L McCabe, Peter D Calvert, David E Ong, M Carter Cornwall, Anita L Zimmerman, Clint L Makino.   

Abstract

In vertebrate rods, photoisomerization of the 11-cis retinal chromophore of rhodopsin to the all-trans conformation initiates a biochemical cascade that closes cGMP-gated channels and hyperpolarizes the cell. All-trans retinal is reduced to retinol and then removed to the pigment epithelium. The pigment epithelium supplies fresh 11-cis retinal to regenerate rhodopsin. The recent discovery that tens of nanomolar retinal inhibits cloned cGMP-gated channels at low [cGMP] raised the question of whether retinoid traffic across the plasma membrane of the rod might participate in the signaling of light. Native channels in excised patches from rods were very sensitive to retinoid inhibition. Perfusion of intact rods with exogenous 9- or 11-cis retinal closed cGMP-gated channels but required higher than expected concentrations. Channels reopened after perfusing the rod with cellular retinoid binding protein II. PDE activity, flash response kinetics, and relative sensitivity were unchanged, ruling out pharmacological activation of the phototransduction cascade. Bleaching of rhodopsin to create all-trans retinal and retinol inside the rod did not produce any measurable channel inhibition. Exposure of a bleached rod to 9- or 11-cis retinal did not elicit channel inhibition during the period of rhodopsin regeneration. Microspectrophotometric measurements showed that exogenous 9- or 11-cis retinal rapidly cross the plasma membrane of bleached rods and regenerate their rhodopsin. Although dark-adapted rods could also take up large quantities of 9-cis retinal, which they converted to retinol, the time course was slow. Apparently cGMP-gated channels in intact rods are protected from the inhibitory effects of retinoids that cross the plasma membrane by a large-capacity buffer. Opsin, with its chromophore binding pocket occupied (rhodopsin) or vacant, may be an important component. Exceptionally high retinoid levels, e.g., associated with some retinal degenerations, could overcome the buffer, however, and impair sensitivity or delay the recovery after exposure to bright light.

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Year:  2006        PMID: 17001087      PMCID: PMC2151575          DOI: 10.1085/jgp.200609619

Source DB:  PubMed          Journal:  J Gen Physiol        ISSN: 0022-1295            Impact factor:   4.086


  67 in total

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Journal:  Exp Eye Res       Date:  1978-03       Impact factor: 3.467

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Journal:  Exp Eye Res       Date:  1974-01       Impact factor: 3.467

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Journal:  J Gen Physiol       Date:  2004-10       Impact factor: 4.086

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  4 in total

1.  Signalling beyond photon absorption: extracellular retinoids and growth factors modulate rod photoreceptor sensitivity.

Authors:  Alex S McKeown; Priyamvada M Pitale; Timothy W Kraft
Journal:  J Physiol       Date:  2016-01-23       Impact factor: 5.182

2.  Vitamin A activates rhodopsin and sensitizes it to ultraviolet light.

Authors:  Sadaharu Miyazono; Tomoki Isayama; François C Delori; Clint L Makino
Journal:  Vis Neurosci       Date:  2011-11       Impact factor: 3.241

3.  Turning cones off: the role of the 9-methyl group of retinal in red cones.

Authors:  Maureen E Estevez; Petri Ala-Laurila; Rosalie K Crouch; M Carter Cornwall
Journal:  J Gen Physiol       Date:  2006-11-13       Impact factor: 4.086

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Authors:  Tomoki Isayama; S L McCabe England; R K Crouch; A L Zimmerman; C L Makino
Journal:  Vis Neurosci       Date:  2009-06-05       Impact factor: 3.241

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