The C-proteinase that processes procollagens to fibrillar collagens is identical to the protein previously identified as bone morphogenic protein-1
The C-proteinase that processes procollagens to fibrillar collagens is identical to the protein previously identified as bone morphogenic protein-1
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DOI：
10.1073/pnas.93.10.5127
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发表时间：
1996-05-14
影响因子：
11.1
通讯作者：
Prockop, DJ
中科院分区：
文献类型：
--
作者：
Li, SW;Sieron, AL;Prockop, DJ
骨形态发生蛋白-1（BMP-1）最初被鉴定为当植入啮齿动物的异位部位时诱导新骨形成的几种BMP之一。然而，BMP-1与其他BMP的不同之处在于其结构与转化生长因子β不相似。相反，它有一个大的结构域同源的金属内肽酶从小龙虾，表皮生长因子样结构域，和三个区域的内部序列同源性被称为CUB结构域。因此，BMP-1是需要锌的内肽酶的“astacin家族”的成员。许多astacins已被证明在胚胎孵化，背/腹图案，和早期发育决策中发挥关键作用。在这里，我们已经获得了前胶原C-蛋白酶（EC 3.4.24.19）的氨基酸序列和分离的cDNA克隆，该酶是将前胶原加工成纤维状胶原所必需的。结果表明，前胶原C-蛋白酶与BMP-1相同。
Bone morphogenic protein-1 (BMP-1) was originally identified as one of several BMPs that induced new bone formation when implanted into ectopic sites in rodents. BMP-1, however, differed from other BMPs in that it its structure was not similar to transforming growth factor beta. Instead, it had a large domain homologous to a metalloendopeptidase isolated from crayfish, an epidermal growth-factor-like domain, and three regions of internal sequence homology referred to as CUB domains. Therefore, BMP-1 was a member of the ''astacin families'' of zinc-requiring endopeptidases. Many astacins have been shown to play critical roles in embryonic hatching, dorsal/ventral patterning, and early developmental decisions. Here, we have obtained amino acid sequences and isolated cDNA clones for procollagen C-proteinase (EC 3.4.24.19), an enzyme that is essential for the processing of procollagens to fibrillar collagens. The results demonstrate that procollagen C-proteinase is identical to BMP-1.