High impact information on Rlbp1

• The photosensitivity of Rlbp1(-/-) mice is normal but rhodopsin regeneration, 11-cis-retinal production, and dark adaptation after illumination are delayed by >10-fold [1].
• These findings support a role for CRALBP as an acceptor of 11-cis-retinol in the isomerization reaction of the visual cycle [1].
• In contrast, purified cellular retinaldehyde-binding protein from retinal pigment epithelium carries only 11-cis-retinaldehyde as an endogenous ligand [2].
• The binding site of cellular retinaldehyde-binding protein from frozen retina is nearly fully occupied with these two ligands (saturation greater than 0.9 mol of retinoids/mol of protein) [2].
• RESULTS: In comparison to wild-type mice, the retina of Nrl(-/-) mice contained elevated levels of RPE65 and cellular retinaldehyde-binding protein (CRALBP), suggesting a particular role of these two proteins for the retinoid metabolism of cones [3].

Biological context of Rlbp1

• Our results suggest a potential role for Rlbp1 and Stx12 in ethanol preference in mice, a conclusion supported by the location of these genes in quantitative trait loci (QTL) regions for this phenotype [4].
• Genetic segregation of brain gene expression identifies retinaldehyde binding protein 1 and syntaxin 12 as potential contributors to ethanol preference in mice [4].
• METHODS: A genomic clone encompassing the 5' end of the CRALBP gene through exon 6 was isolated from a mouse 129/Sv genomic DNA library [5].
• These findings were confirmed by immunoblot analysis, where down-regulation of nestin expression with simultaneous up-regulation of CRALBP, GFAP and PKCalpha was observed [6].

Anatomical context of Rlbp1

• Cellular retinaldehyde binding protein in developing retinal astrocytes [7].
• Immunocytochemical studies showed an increase in the proportion of cells expressing glial cell markers, most of which co-expressed CRALBP, GFAP, and vimentin [6].
• This study showed that Muller cells in degenerating retinas of RCS rats and rd/rd mice ultimately exhibited decreased immunolabelling for CAC and CRALBP at the more advanced stages of retinopathy, which coincided with the loss of photoreceptors [8].
• In retinas of 6-week-old RCS rats, Muller cells and their processes were immunolabelled for CRALBP, which spanned from the nerve fiber layer (NFL) through the outer nuclear layer [8].

Associations of Rlbp1 with chemical compounds

• Tissue for immunohistochemistry was fixed by immersion in 4% paraformaldehyde and immunostained using rabbit polyclonal antisera to CRALBP or glial fibrillary acidic protein (GFAP), while fresh tissue was homogenized for Western analysis [7].

Other interactions of Rlbp1

• They were compared with changes in the lipid content and association of retinal proteins, such as postsynaptic density protein 95, glial fibrillary acidic protein, and cellular retinaldehyde-binding protein [9].
• Immunostaining with antibodies to cellular retinaldehyde-binding protein (CRALBP) and glutamine synthetase showed that the GFP-expressing cells were Müller cells [10].
• Proteomic analyses of the isolated apical RPE demonstrated the presence of CRALBP, EBP50, 11-cis-retinol dehydrogenase, cellular retinol-binding protein 1, and interphotoreceptor retinoid-binding protein [11].
• However, such integration occurred exclusively where CRALBP, CD44, and neurocan immunolabeling appeared disrupted in the interface, but coincided with high GFAP expression within the rd1 retina [12].

Analytical, diagnostic and therapeutic context of Rlbp1

• Cellular retinaldehyde-binding protein from retina purifies with two endogenous ligands which cochromatograph on high performance liquid chromatography with 11-cis-retinaldehyde and 11-cis-retinol and occur in a ratio of approximately 3:1, respectively [2].

References