| pubmed-article:10655149 | pubmed:abstractText | It is usually assumed that IRBP (interphotoreceptor retinoid-binding protein) is the only protein present in the interphotoreceptor matrix (IPM) capable of shuttling visual-cycle retinoids between photoreceptors and the retinal pigment epithelium. However, this laboratory previously presented qualitative evidence (Western blots) that serum albumin is present in human IPM. Furthermore, Ong and coworkers (1994) found that cultured RPE cells synthesize serum retinol-binding protein (RBP) and secrete it, mainly into the apical culture medium, which would correspond to the IPM in intact eyes. As both of these proteins can bind all- trans -retinol and 11- cis -retinal, it was of interest to quantify the amounts of albumin and RBP in human IPM. We used radial immunodiffusion to accomplish this. The average molar ratio of serum albumin to IRBP in these samples was 1.9; that of RBP to IRBP was 0.015. The presence of a high concentration of serum albumin in the IPM in situ was confirmed by the intense immunohistochemical staining seen in sections of fresh human eyes. The human case is not unique; various concentrations of albumin were found in the IPM of all vertebrate species examined (by gel electrophoresis). These results indicate that both serum albumin, because of its very high concentration in the IPM, and RBP, because of its comparatively tight binding to retinoids, need to be considered, along with IRBP, as proteins that may participate in visual-cycle transport. The accompanying paper addresses this concern. | lld:pubmed |
