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骨粘连蛋白是一种存在于骨骼中的细胞结合硫酸角质素蛋白聚糖,属于细胞外基质富含亮氨酸重复序列蛋白家族。

Osteoadherin, a cell-binding keratan sulfate proteoglycan in bone, belongs to the family of leucine-rich repeat proteins of the extracellular matrix.

作者信息

Sommarin Y, Wendel M, Shen Z, Hellman U, Heinegârd D

机构信息

Department of Cellular and Molecular Biology, Section for Connective Tissue Biology, Lund University, S-221 00 Lund, Sweden.

出版信息

J Biol Chem. 1998 Jul 3;273(27):16723-9. doi: 10.1074/jbc.273.27.16723.

Abstract

Osteoadherin is a recently described bone proteoglycan containing keratan sulfate. It promotes integrin (alphav beta3)-mediated cell binding (Wendel, M., Sommarin, Y., and Heinegârd, D. (1998) J. Cell Biol. 141, 839-847). The primary structure of bovine osteoadherin has now been determined by nucleotide sequencing of a cDNA clone from a primary bovine osteoblast expression library. The entire translated primary sequence corresponds to a 49,116-Da protein with a calculated isoelectric point for the mature protein of 5.2. The dominating feature is a central region consisting of 11 B-type, leucine-rich repeats ranging in length from 20 to 30 residues. The full, primary sequence contains four putative sites for tyrosine sulfation, three of which are at the N-terminal end of the molecule. There are six potential sites for N-linked glycosylation present. Osteoadherin shows highest sequence identity, 42%, to bovine keratocan and 37-38% identity to bovine fibromodulin, lumican, and human PRELP. Unique to osteoadherin is the presence of a large and very acidic C-terminal domain. The distribution of cysteine residues resembles that of other leucine-rich repeat proteins except for two centrally located cysteines. Northern blot analysis of RNA samples from various bovine tissues showed a 4.5-kilobase pair message for osteoadherin to be expressed in bone only. Osteoadherin mRNA was detected by in situ hybridization in mature osteoblasts located superficially on trabecular bone.

摘要

骨黏附素是一种最近被描述的含有硫酸角质素的骨蛋白聚糖。它促进整合素(αvβ3)介导的细胞黏附(温德尔,M.,索马林,Y.,和海内加德,D.(1998年)《细胞生物学杂志》141卷,839 - 847页)。现在,通过对来自原代牛成骨细胞表达文库的一个cDNA克隆进行核苷酸测序,已确定了牛骨黏附素的一级结构。整个翻译后的一级序列对应于一种49,116道尔顿的蛋白质,成熟蛋白的计算等电点为5.2。其主要特征是一个中央区域,由11个B型富含亮氨酸重复序列组成,长度从20到30个残基不等。完整的一级序列包含四个酪氨酸硫酸化的推定位点,其中三个位于分子的N末端。存在六个潜在的N - 糖基化位点。骨黏附素与牛角膜蛋白的序列同一性最高,为42%,与牛纤维调节蛋白、核纤层蛋白和人PRELP的同一性为37 - 38%。骨黏附素独特之处在于存在一个大的且酸性很强的C末端结构域。除了两个位于中央的半胱氨酸外,半胱氨酸残基的分布与其他富含亮氨酸重复序列的蛋白质相似。对来自各种牛组织的RNA样本进行的Northern印迹分析表明,骨黏附素的一条4.5千碱基对的信使核糖核酸仅在骨中表达。通过原位杂交在位于小梁骨表面的成熟成骨细胞中检测到了骨黏附素信使核糖核酸。

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