Regular ArticleMolecular Characterization and Genomic Mapping of Human IPM 200, a Second Member of a Novel Family of Proteoglycans
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IMPG2-Related Maculopathy
2024, American Journal of OphthalmologyHuman retinal organoids harboring IMPG2 mutations exhibit a photoreceptor outer segment phenotype that models advanced retinitis pigmentosa
2022, Stem Cell ReportsCitation Excerpt :As such, it is not surprising that disruption of the IPM causes a variety of outer retinal disorders with profound visual consequences. A prominent component of the IPM is interphotoreceptor matrix proteoglycan 2 (IMPG2), an abundant protein that is secreted by both rod and cone photoreceptors (Acharya et al., 2000; Chen et al., 2003; Foletta et al., 2001; Kuehn and Hageman, 1999). IMPG2 is heavily glycosylated with glycosaminoglycans (GAGs) as well as N- and O-linked oligosaccharides, which together contribute to approximately 60% of its mass (Acharya et al., 2000).
Differentiating drusen: Drusen and drusen-like appearances associated with ageing, age-related macular degeneration, inherited eye disease and other pathological processes
2016, Progress in Retinal and Eye ResearchCitation Excerpt :IMPG1 (interphotoreceptor matrix proteoglycan 1) encodes SPACR, a 150 kDa sialoprotein associated with rod and cone photoreceptors. It is a major component of the interphotoreceptor matrix, the site where rods and cones interact with the RPE (Felbor et al., 1998; Kuehn and Hageman, 1999). SPACR is highly homologous to SPACRCAN (sialoprotein associated with photoreceptor cone and rod proteoglycans), a 200 kDa protein encoded by IMPG2 (interphotoreceptor matrix proteoglycan 2) and also found in the interphotoreceptor matrix (Acharya et al., 2000).
Frequency and clinical pattern of vitelliform macular dystrophy caused by mutations of interphotoreceptor matrix IMPG1 and IMPG2 genes
2014, OphthalmologyCitation Excerpt :Furthermore, the preservation of the RPE reflectivity and the lack of deposits in the sub-RPE space within the egg yolk macular dystrophy are additional SD-OCT criteria that enable distinguishing IMPG1- and IMPG2-linked vitelliform dystrophies from BEST1- and PRPH2-linked vitelliform dystrophies in cases of autosomal dominant inheritance (Fig 12 and Table 2, available at www.aaojournal.org).26–31 The preservation of RPE reflectivity, the occurrence of drusen-like lesions, and the localization of the deposit above the RPE as disclosed on SD-OCT could be related to the function of the IMPG1 and IMPG2 genes.11,12,17–21 Indeed, IMPG1 and IMPG2, its paralog, encode respectively a sialoglycoprotein associated with cones and rods and a chondroitin sulfate proteoglycan.
Mutations in IMPG2, Encoding interphotoreceptor matrix proteoglycan 2, cause autosomal-recessive retinitis pigmentosa
2010, American Journal of Human GeneticsCitation Excerpt :In this study, seven different mutations in IMPG2 were identified in seven families of various ethnic origins. IMPG2 encodes the retinal interphotoreceptor matrix proteoglycan IMPG2 (also known as IPM200 or SPACRCAN), that consists of 1,241 amino acids with a calculated molecular weight of 138.5 kDa.22,24 The IMPG2 protein is highly similar to IMPG1 (also known as SPACR) and is predicted to contain a signal peptide, two SEA domains, and two EGF-like domains in the large extracellular N-terminal part of the protein, a putative transmembrane domain, and a cytoplasmic tail.22,23
Glycosaminoglycan (GAG) biosynthesis and GAG-binding proteins
2010, Progress in Molecular Biology and Translational Science
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To whom correspondence should be addressed at University of Iowa Center for Macular Degeneration, Department of Ophthalmology and Visual Sciences, University of Iowa, 11190E PFP, 200 Hawkins Drive, Iowa City, IA 52240. Fax: (319) 335-7142. E-mail: [email protected].