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Interphotoreceptor matrix proteoglycan 2

SPACRCAN, IPM 200, IMPG2, interphotoreceptor matrix proteoglycan 2, PG10.2
The protein encoded by this gene binds chondroitin sulfate and hyaluronan and is a proteoglycan. The encoded protein plays a role in the organization of the interphotoreceptor matrix and may promote the growth and maintenance of the light-sensitive photoreceptor outer segment. Defects in this gene are a cause of retinitis pigmentosa type 56 and maculopathy, IMPG2-related.[provided by RefSeq, Mar 2011] (from NCBI)
Top mentioned proteins: AGE, Epidermal Growth Factor, ACID, HAD, CAN
Papers on SPACRCAN
Adult-onset foveomacular vitelliform dystrophy: A fresh perspective.
Boon et al., Jerusalem, Israel. In Prog Retin Eye Res, Jul 2015
A minority of AFVD patients have a mutation in the PRPH2, BEST1, IMPG1, or IMPG2 genes.
Frequency and clinical pattern of vitelliform macular dystrophy caused by mutations of interphotoreceptor matrix IMPG1 and IMPG2 genes.
Hamel et al., Montpellier, France. In Ophthalmology, 2014
PURPOSE: To assess the frequency of and to characterize the clinical spectrum and optical coherence tomography findings of vitelliform macular dystrophy linked to IMPG1 and IMPG2, 2 new causal genes expressed in the interphotoreceptor matrix.
IMPG2-associated retinitis pigmentosa displays relatively early macular involvement.
Klevering et al., Nijmegen, Netherlands. In Invest Ophthalmol Vis Sci, 2014
PURPOSE: To provide the first detailed clinical description in patients with RP caused by recessive mutations in IMPG2.
Homozygosity mapping in autosomal recessive retinitis pigmentosa families detects novel mutations.
Hamel et al., Montpellier, France. In Mol Vis, 2012
RESULTS: We found ten mutations, seven of which were novel mutations in eight known genes, including RP1, IMPG2, NR2E3, PDE6A, PDE6B, RLBP1, CNGB1, and C2ORF71, in ten out of 15 families.
Mutations in IMPG2, encoding interphotoreceptor matrix proteoglycan 2, cause autosomal-recessive retinitis pigmentosa.
den Hollander et al., Jerusalem, Israel. In Am J Hum Genet, 2010
identification of IMPG2 mutations in autosomal-recessive retinitis pigmentosa; data show that mutations in a structural component of the interphotoreceptor matrix can cause autosomal-recessive retinitis pigmentosa
Hyaluronan dynamics during retinal development.
Zako et al., Japan. In Brain Res, 2009
We have already shown the regulated expressions of hyaluronan binding molecules including versican, SPACR, and SPACRCAN, during retinal development.
Differential neuroglycan C expression during retinal degeneration in Rpe65-/- mice.
Schorderet et al., Sion, Switzerland. In Mol Vis, 2007
PURPOSE: An increased mRNA expression of the genes coding for the extracellular matrix proteins neuroglycan C (NGC), interphotoreceptor matrix proteoglycan 2 (IMPG2), and CD44 antigen (CD44) has been observed during retinal degeneration in mice with a targeted disruption of the Rpe65 gene (Rpe65-/- mouse).
Molecular cloning and characterization of chick SPACRCAN.
Zako et al., Japan. In J Biol Chem, 2006
Here, we verified that this 300-kDa molecule is chick SPACRCAN (sialoproteoglycan associated with cones and rods), another member of a novel interphotoreceptor matrix molecule family.
Insights into the evolution of the ErbB receptor family and their ligands from sequence analysis.
Staros et al., Nashville, United States. In Bmc Evol Biol, 2005
The recent identification of several new ligands for the ErbB receptors supports this characterization of an ErbB ligand; further, applying this characterization to available sequences suggests additional potential ligands for these receptors, the EGF modules from previously identified proteins: interphotoreceptor matrix proteoglycan-2, the alpha and beta subunit of meprin A, and mucins 3, 4, 12, and 17.
Spacrcan binding to hyaluronan and other glycosaminoglycans. Molecular and biochemical studies.
Hollyfield et al., Cleveland, United States. In J Biol Chem, 2004
Photoreceptors project from the outer retinal surface into a specialized glycocalyx, the interphotoreceptor matrix (IPM), which contains hyaluronan (HA) and two novel proteoglycans, Spacr and Spacrcan.
SPACRCAN in the interphotoreceptor matrix of the mouse retina: molecular, developmental and promoter analysis.
Hollyfield et al., Cleveland, United States. In Exp Eye Res, 2003
May play an important role in photoreceptor development and maintenance.
Organization of the human IMPG2 gene and its evaluation as a candidate gene in age-related macular degeneration and other retinal degenerative disorders.
Hageman et al., Iowa City, United States. In Invest Ophthalmol Vis Sci, 2001
PURPOSE: To characterize the genomic organization of human IMPG2, the gene encoding the retinal interphotoreceptor matrix (IPM) proteoglycan IPM 200, to evaluate its relationship to IPM 150, and to evaluate its involvement in inherited retinopathies, such as age-related macular degeneration, retinitis pigmentosa, and Leber congenital amaurosis.
SPACRCAN in the developing retina and pineal gland of the rat: spatial and temporal pattern of gene expression and protein synthesis.
Hollyfield et al., Bethesda, United States. In J Comp Neurol, 2001
SPACRCAN is a hyaluronan-binding proteoglycan that is present in the pineal gland and interphotoreceptor matrix of the retina.
Interphotoreceptor matrix in the fovea and peripheral retina of the primate Macaca mulatta: distribution and glycoforms of SPACR and SPACRCAN.
Rodriguez et al., Cleveland, United States. In Exp Eye Res, 2001
SPACR and SPACRCAN localization in the interphotoreceptor matrix (IPM) of the fovea and peripheral retina of Macaca mulatta was established with antibodies to these core proteins and the chondroitin sulfate epitopes and lectin binding properties of these molecules were defined.
Molecular characterization of the murine orthologue of the human retinal proteoglycan IPM 150.
Hageman et al., Iowa City, United States. In Mol Vis, 2000
Two members of this family, designated IPM 150 and IPM 200, have been extensively characterized.
Molecular characterization and genomic mapping of human IPM 200, a second member of a novel family of proteoglycans.
Hageman et al., Iowa City, United States. In Mol Cell Biol Res Commun, 1999
IPM 200 represents the second member of a novel family of retinal proteoglycans suspected to be involved in retinal adhesion and photoreceptor cell survival
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