Molecular characterization and genomic mapping of human IPM 200, a second member of a novel family of proteoglycans.
نویسندگان
چکیده
We report herein the characterization of the cDNA for a novel human chondroitin sulfate proteoglycan, designated IPM 200, and the chromosomal location of its gene, designated IMPG2. IPM 200 was isolated from the retinal interphotoreceptor matrix, a unique extracellular matrix that occupies the subretinal space between the apices of the retinal pigment epithelium and the neural retina. The cDNA contains an open reading frame of 3,726 bp that codes for a core protein with a deduced molecular weight of 138.5 kDa. The deduced IPM 200 core protein contains a putative transmembrane domain, two EGF-like repeats, numerous N- and O-linked glycosylation consensus sequences and one consensus sequence for glycosaminoglycan attachment. IMPG2 maps to human chromosome 3q12.2-12.3. Based on homologies within their amino acid sequences we propose that IPM 200 and a previously described human proteoglycan, IPM 150, form a new family of extracellular matrix glycoconjugates.
منابع مشابه
Expression and characterization of the IPM 150 gene (IMPG1) product, a novel human photoreceptor cell-associated chondroitin-sulfate proteoglycan.
The interphotoreceptor matrix (IPM) occupies the extracellular space between the apical surface of the retinal pigmented epithelium and the external limiting membrane of the neural retina. This space contains two chondroitin sulfate proteoglycans, designated IPM 150 and IPM 200, which are likely to effect retinal adhesion and photoreceptor survival. In an effort to characterize human IPM 150, s...
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عنوان ژورنال:
- Molecular cell biology research communications : MCBRC
دوره 2 2 شماره
صفحات -
تاریخ انتشار 1999