Hiraki Y, Tanaka H, Inoue H, Kondo J, Kamizono A, Suzuki F
Department of Biochemistry and Calcified-Tissue Metabolism, Faculty of Dentistry, Osaka University, Japan.
Biochem Biophys Res Commun. 1991 Mar 29;175(3):971-7. doi: 10.1016/0006-291x(91)91660-5.
Here we report the structure and bioactivity of 25 kDa glycoprotein (chondromodulin-I) as a tissue-specific functional matrix component identified and cloned for the first time. Chondromodulin-I purified from fetal bovine cartilage markedly stimulated DNA synthesis of cultured growth-plate chondrocytes in the presence of basic fibroblast growth factor (FGF). Bovine chondromodulin-I cDNA revealed that the mature protein consists of 121 amino acids with three possible glycosylation sites and is coded as the C-terminal part of a larger precursor. On northern blot analysis, expression of chondromodulin-I mRNA was observed only in cartilage.
在此，我们报道了首次鉴定并克隆出的一种组织特异性功能基质成分——25 kDa糖蛋白（软骨调节素-I）的结构和生物活性。在碱性成纤维细胞生长因子（FGF）存在的情况下，从胎牛软骨中纯化得到的软骨调节素-I显著刺激了培养的生长板软骨细胞的DNA合成。牛软骨调节素-I cDNA显示，成熟蛋白由121个氨基酸组成，有三个可能的糖基化位点，并且被编码为一个更大前体的C末端部分。在Northern印迹分析中，仅在软骨中观察到软骨调节素-I mRNA的表达。
