| pubmed-article:15755727 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15755727 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:15755727 | lifeskim:mentions | umls-concept:C0035339 | lld:lifeskim |
| pubmed-article:15755727 | lifeskim:mentions | umls-concept:C0073111 | lld:lifeskim |
| pubmed-article:15755727 | lifeskim:mentions | umls-concept:C1511572 | lld:lifeskim |
| pubmed-article:15755727 | lifeskim:mentions | umls-concept:C1515655 | lld:lifeskim |
| pubmed-article:15755727 | pubmed:issue | 19 | lld:pubmed |
| pubmed-article:15755727 | pubmed:dateCreated | 2005-5-9 | lld:pubmed |
| pubmed-article:15755727 | pubmed:abstractText | The retinoid cycle is a recycling system that replenishes the 11-cis-retinal chromophore of rhodopsin and cone pigments. Photoreceptor-specific retinol dehydrogenase (prRDH) catalyzes reduction of all-trans-retinal to all-trans-retinol and is thought to be a key enzyme in the retinoid cycle. We disrupted mouse prRDH (human gene symbol RDH8) gene expression by targeted recombination and generated a homozygous prRDH knock-out (prRDH-/-) mouse. Histological analysis and electron microscopy of retinas from 6- to 8-week-old prRDH-/- mice revealed no structural differences of the photoreceptors or inner retina. For brief light exposure, absence of prRDH did not affect the rate of 11-cis-retinal regeneration or the decay of Meta II, the activated form of rhodopsin. Absence of prRDH, however, caused significant accumulation of all-trans-retinal following exposure to bright lights and delayed recovery of rod function as measured by electroretinograms and single cell recordings. Retention of all-trans-retinal resulted in slight overproduction of A2E, a condensation product of all-trans-retinal and phosphatidylethanolamine. We conclude that prRDH is an enzyme that catalyzes reduction of all-trans-retinal in the rod outer segment, most noticeably at higher light intensities and prolonged illumination, but is not an essential enzyme of the retinoid cycle. | lld:pubmed |
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| pubmed-article:15755727 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15755727 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15755727 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15755727 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:15755727 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15755727 | pubmed:month | May | lld:pubmed |
| pubmed-article:15755727 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:15755727 | pubmed:author | pubmed-author:PalczewskiKrz... | lld:pubmed |
| pubmed-article:15755727 | pubmed:author | pubmed-author:AlekseevAndre... | lld:pubmed |
| pubmed-article:15755727 | pubmed:author | pubmed-author:BaehrWolfgang... | lld:pubmed |
| pubmed-article:15755727 | pubmed:author | pubmed-author:ImanishiYoshi... | lld:pubmed |
| pubmed-article:15755727 | pubmed:author | pubmed-author:LiZhuZ | lld:pubmed |
| pubmed-article:15755727 | pubmed:author | pubmed-author:MaedaTadaoT | lld:pubmed |
| pubmed-article:15755727 | pubmed:author | pubmed-author:SapersteinDav... | lld:pubmed |
| pubmed-article:15755727 | pubmed:author | pubmed-author:KuksaVladimir... | lld:pubmed |
| pubmed-article:15755727 | pubmed:author | pubmed-author:RiekeFredF | lld:pubmed |
| pubmed-article:15755727 | pubmed:author | pubmed-author:MaedaAkikoA | lld:pubmed |
