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Interphotoreceptor retinol-binding protein is a large glycoprotein known to bind retinoids and found primarily in the interphotoreceptor matrix of the retina between the retinal pigment epithelium and the photoreceptor cells. Zusätzlich bieten wir Ihnen Retinol Binding Protein 3, Interstitial Antikörper (73) und Retinol Binding Protein 3, Interstitial Proteine (17) und viele weitere Produktgruppen zu diesem Protein an.
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Our study, which provides the first structure of an IRBP with bound ligand, supports a potential role for fatty acids in regulating retinoid binding.
The 629-643 RBP-3 peptide is a major uveitogenic peptide for the induction of autoimmune uveoretinitis in C57BL/6J mice and the persistent clinical disease induced with one peptide leads to epitope spreading.
We propose that down-regulation of IRBP may represent an early and novel pathogenic mechanism in degenerative retinal diseases
Although death signaling proteins are increased, the caspase-dependent and independent apoptotic pathways are mildly activated in Irbp-deficient retinas.
Secretory defect and cytotoxicity: the potential disease mechanisms for the retinitis pigmentosa (RP)-associated interphotoreceptor retinoid-binding protein (IRBP).
In addition to its role in the visual cycle, IRBP is needed for normal eye development.
IRBP is essential to normal cone function and demonstrate that differences exist in the visual cycle of rods and cones.
these findings suggest that IRBP plays an important role in the delivery of 11-cis-retinol to cones and can facilitate cone function in the presence of light
Tumor formation in mice with somatic inactivation of the retinoblastoma gene in interphotoreceptor retinol binding protein-expressing cells.
analysis of the structure and sequence of the IRBP gene
data show that presence of IRBP is necessary in ocular and pineal gland tissues for expression of autoimmune uveitis
Expression of IRBP within the thymus is critical to prevent spontaneous autoimmunity against the eye, even in the presence of autoimmune regulator aire.
Data indicate that IRBP is essential to normal cone function and demonstrate that IRBP has a cone-specific visual cycle function.
Activation of IRBP-specific T cells from mice immunized with uveitogenic IRBP(1-20) peptide under T-helper cell interleukin (IL)17-polarizing conditions is associated with increased expansion of T cells expressing the gamma delta T cell receptor.
this report is the first to describe the retinal dystrophy in children caused by homozygous nonsense RBP3 mutations, highlighting the requirement for IRBP in normal eye development and visual function.
CMPK1 and RBP3 are associated with corneal curvature in Asian populations.
We found that most patients with macular telangiectasia-2 possess retinal autoantibodies, the most prevalent of which were directed against AGL, RBP3, and CK-B.
The mouse retina promotes cone dark adaptation eightfold faster than the retinal pigment epithelium. However, complete cone recovery requires both visual cycles.
It is likely that mutations in RGR, RBP3, and possibly RBP1 occur rarely in inherited retinal dystrophies.
Underproduction of IRBP is an early event in the human diabetic retina and is associated with retinal neurodegeneration.
studies suggest that IRBP and S-Ag can initiate innate and, in sensitive individuals, adaptive immune response by attracting iDCs and T and B cells expressing CXCR3 and CXCR5
analysis of IRBP proteolysis is useful as a biomarker for uveitis
Mutations in RBP3 are an infrequent cause of autosomal recessive retinitis pigmentosa.
In interphotoreceptor retinoid-binding protein transgenic mice cone dysfunction appears to be caused by abnormal trafficking of cone opsins due to impaired delivery of all-transretinaldehyde chromophore without IRBP.
IRBP is able to bind a variety of carotenoids at an affinity comparable to retinoids and with much stronger affinity than any fatty acid tested.
In mouse immunization studies Ehrlichia canis amino acid sequence 44-59 is identified as a candidate mimicry epitope for interphotoreceptor retinoid-binding protein (IRBP) 201-216 and is capable of preventing ocular inflammation.
KLF15 binds to multiple 9 bp consensus sites in the Rhodospin and IRBP promoters including the CRS-1 and G-rich repressor elements.
Localized to interphotoreceptor matrix, where it is available for binding and transport of visual cycle retinoids.
Interphotoreceptor retinol-binding protein is a large glycoprotein known to bind retinoids and found primarily in the interphotoreceptor matrix of the retina between the retinal pigment epithelium and the photoreceptor cells. It is thought to transport retinoids between the retinal pigment epithelium and the photoreceptors, a critical role in the visual process.The human IRBP gene is approximately 9.5 kbp in length and consists of four exons separated by three introns. The introns are 1.6-1.9 kbp long. The gene is transcribed by photoreceptor and retinoblastoma cells into an approximately 4.3-kilobase mRNA that is translated and processed into a glycosylated protein of 135,000 Da. The amino acid sequence of human IRBP can be divided into four contiguous homology domains with 33-38% identity, suggesting a series of gene duplication events. In the gene, the boundaries of these domains are not defined by exon-intron junctions, as might have been expected. The first three homology domains and part of the fourth are all encoded by the first large exon, which is 3,180 base pairs long. The remainder of the fourth domain is encoded in the last three exons, which are 191, 143, and approximately 740 base pairs long, respectively.
irbp gene 2
, retinol-binding protein 3
, interphotoreceptor retinoid-binding protein
, retinol binding protein 3, interstitial
, retinol-binding protein 3-like
, interstitial retinol-binding protein
, interphotoreceptor retinoid binding protein
, interphotoreceptor retinol- binding protein
, 7S protein
, protein 7S