The major soluble 19.6 kDa protein of the organic shell matrix of the freshwater snail Biomphalaria glabrata is an N-glycosylated dermatopontin

The major soluble 19.6 kDa protein of the organic shell matrix of the freshwater snail Biomphalaria glabrata is an N-glycosylated dermatopontin
复制标题

DOI:
10.1016/s1570-9639(03)00203-6
复制
发表时间:
2003-08-21
影响因子:
3.2
通讯作者:
Mann, K
Mann, K
中科院分区:
生物学3区
文献类型:
--
作者:
Marxen, JC;Nimtz, M;Mann, K

文献摘要

被引文献

相似文献

通过制备性电泳分离主要的光滑双脐螺壳基质蛋白19.6 kDa,并测序。148个氨基酸的序列显示与哺乳动物皮连蛋白序列的32%序列同一性和与先前描述的两种无脊椎动物皮连蛋白的34-37%序列同一性。壳基质皮连蛋白的一个独特特征是存在单个N-糖基化共有序列,其天冬酰胺完全用五糖修饰。通过质谱法和碳水化合物组成分析对该短N-聚糖进行序列分析,结果表明其为普遍存在的N-聚糖核心寡糖,但末端甘露糖为3-O-甲基化。皮桥蛋白广泛存在于哺乳动物细胞外基质中,包括生物矿物质如骨和牙齿的基质。它在无脊椎动物生物矿物中的出现表明,脊椎动物骨和软体动物壳等遗传学上遥远的生物矿物形成系统共享在长期进化过程中经历了令人惊讶的很少变化的组分。(C)2003 Elsevier B. V.保留所有权利。
The major Biomphalaria glabrata shell matrix protein of 19.6 kDa was isolated by preparative electrophoresis and sequenced. The sequence of 148 amino acids showed 32% sequence identity to mammalian dermatopontin sequences and 34-37% identity to two invertebrate dermatopontins described previously. A unique feature of the shell matrix dermatopontin was the presence of a single N-glycosylation consensus sequence, the asparagine of which was completely modified with a pentasaccharide. Sequence analysis of this short N-glycan by mass spectrometry and carbohydrate composition analysis indicated that it was the ubiquitous N-glycan core oligosaccharide with the exception that the terminal mannoses were 3-O-methylated. Dermatopontin is widespread in mammalian extracellular matrices, including the matrix of biominerals such as bone and teeth. Its occurrence in an invertebrate biomineral indicates that such phylogenetically distant biomineral-forming systems as vertebrate bone and mollusk shell share components which have undergone surprisingly few changes during a long evolution. (C) 2003 Elsevier B.V. All rights reserved.