CDNA CLONE TO CHICK CORNEAL CHONDROITIN DERMATAN SULFATE PROTEOGLYCAN REVEALS IDENTITY TO DECORIN
CDNA CLONE TO CHICK CORNEAL CHONDROITIN DERMATAN SULFATE PROTEOGLYCAN REVEALS IDENTITY TO DECORIN
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DOI：
10.1016/0003-9861(92)90562-b
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发表时间：
1992-07-01
影响因子：
3.9
通讯作者：
HASSELL, JR
中科院分区：
文献类型：
--
作者：
LI, W;VERGNES, JP;HASSELL, JR
通过用牛核心蛋白聚糖的cDNA克隆筛选从鸡角膜mRNA制备的文库来分离1.6kb的cDNA克隆。该cDNA含有编码aMr 39，683蛋白的开放阅读框。与来自角膜软骨素/硫酸皮肤素蛋白聚糖的核心蛋白的N-末端的序列的19个氨基酸匹配证实了该克隆是角膜蛋白聚糖，并且与人和牛核心蛋白聚糖的同源性证实了其作为核心蛋白聚糖的身份。推导的序列的结构特征包括一个16个氨基酸的信号肽，一个14个氨基酸的前肽，在N-和C-末端区域的半胱氨酸残基，和一个中央富含亮氨酸的区域（占蛋白质的63%）含有序列LXXLXLXXNXL/I的9个重复。鸡核心蛋白聚糖含有该序列的三个变体，它们串联连接形成一个单元，三个单元串联连接形成富含亮氨酸的区域。这些单元侧翼的β弯曲氨基酸的存在可用于将这些单元描绘为富含亮氨酸区域的结构元件。重复序列内的序列同源性和重复序列的间隔表明，该区域是由重复引起的。鸡核心蛋白聚糖与哺乳动物核心蛋白聚糖的主要区别在于起始于核心蛋白N-末端的19个氨基酸序列。在该区域内，作为软骨素/硫酸皮肤素侧链的潜在受体的丝氨酸之前是甘氨酸，而不是像哺乳动物核心蛋白聚糖和所有其他哺乳动物蛋白聚糖中那样之后是甘氨酸。
A 1.6-kb cDNA clone was isolated by screening a library prepared from chick corneal mRNA with a cDNA clone to bovine decorin. The cDNA contained an open reading frame coding for aMr39,683 protein. A 19-amino-acid match with sequence from the N-terminus of core protein from the corneal chondroitin/dermatan sulfate proteoglycan confirmed the clone as a corneal proteoglycan and the homology with human and bovine decorin confirmed its identity as decorin. Structural features of the deduced sequence include a 16-amino-acid signal peptide, a 14-amino-acid propeptide, cysteine residues at the N- and C-terminal regions, and a central leucine-rich region (comprising 63% of the protein) containing nine repeats of the sequence LXXLXLXXNXL/I. Chick decorin contains three variations of this sequence that are tandemly linked to form a unit and three units tandemly linked to form the leucine-rich region. The presence of β bend amino acids flanking the units may serve to delineate the units as structural elements of the leucine-rich region. Sequence homology within the repeats and the spacing of the repeats suggest that this region arose by duplication. Chick decorin primarily differs from mammalian decorins in the 19-amino-acid sequence that starts the N-terminus of the core protein. Within this region, the serine that serves as a potential acceptor for the chondroitin/dermatan sulfate side chain is preceded by a glycine instead of being followed by a glycine as it is in the mammalian decorins and all other mammalian proteoglycans.