Molecular characterization and genomic mapping of human IPM 200, a second member of a novel family of proteoglycans.
Molecular characterization and genomic mapping of human IPM 200, a second member of a novel family of proteoglycans.
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DOI：
10.1006/mcbr.1999.0161
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发表时间：
1999-08-01
期刊：
影响因子：
--
通讯作者：
Hageman, G S
中科院分区：
文献类型：
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作者：
Kuehn, M H;Hageman, G S
我们在此报告的一种新的人硫酸软骨素蛋白聚糖，指定IPM 200的cDNA的表征，其基因的染色体定位，指定IMPG 2。IPM 200分离自视网膜光感受器间基质，一种独特的细胞外基质，其占据视网膜色素上皮和神经视网膜的顶点之间的视网膜下空间。该cDNA含有一个3，726 bp的开放阅读框，编码一个推测分子量为138.5 kDa的核心蛋白。推断的IPM 200核心蛋白包含一个推定的跨膜结构域，两个EGF样重复序列，许多N-和O-连接的糖基化的共识序列和一个糖胺聚糖附着的共识序列。IMPG 2定位于人染色体3q12.2-12.3。基于其氨基酸序列内的同源性，我们提出IPM 200和先前描述的人蛋白聚糖IPM 150，形成一个新的细胞外基质糖缀合物家族。
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.