Synthesis and characterization of cDNA encoding a cartilage-specific short collagen.
Synthesis and characterization of cDNA encoding a cartilage-specific short collagen.
复制标题
编码软骨特异性短胶原蛋白的 cDNA 的合成和表征。
DOI：
10.1073/pnas.81.10.3014
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发表时间：
1984
影响因子：
11.1
通讯作者：
Olsen,BR
中科院分区：
文献类型：
--
作者：
Ninomiya,Y;Olsen,BR
透明软骨含有一组独特的胶原蛋白。II型胶原蛋白最为丰富，约占软骨胶原蛋白总量的85%。此外，还描述了几种次要的胶原成分。为了研究软骨细胞特异性胶原的结构和发育调控，我们从胚胎鸡胸骨软骨mRNA中构建了cDNA文库。我们在这里报道了一个3200碱基对长的cDNA的分离和表征，该cDNA编码的胶原多肽具有不寻常的结构，因为该分子的总长度仅为原α 1（II）胶原链的一半左右。这种多肽的mRNA比编码间质胶原原α链的mRNA要小得多。此外，由cDNA编码的肽似乎包含至少三个具有三螺旋势的结构域，由短的非胶原肽分开。在这三个胶原结构域之间有几个半胱氨酸残基。
Hyaline cartilage contains a unique set of collagenous proteins. Type II collagen is the most abundant, constituting about 85% of the total cartilage collagen. In addition, several minor collagenous components have been described. To study the structure and developmental regulation of chondrocyte-specific collagens, we have constructed a cDNA library from embryonic chicken sternal cartilage mRNA. We report here on the isolation and characterization of a 3200 base-pair-long cDNA that codes for a collagenous polypeptide of unusual structure in that the total length of the molecule is only about half of pro alpha 1(II) collagen chains. The mRNA for this polypeptide is considerably smaller than mRNA encoding the pro alpha chains of interstitial collagens. In addition, the peptide encoded by the cDNA appears to contain at least three domains with triple-helical potential separated by short, noncollagenous peptides. Between the three collagenous domains are several cysteinyl residues.
对在不存在和存在纤连蛋白的情况下在胶原凝胶内培养的软骨细胞合成的三种低分子量胶原多肽的鉴定和部分表征。
影响因子：
4.1
作者：
Gary J. Gibson;T. C. M. Kielty;Clare Garner;Seth L. SCHORt;M. E. Grant
通讯作者：
M. E. Grant