Human fibroblast collagenase. Complete primary structure and homology to an oncogene transformation-induced rat protein.
Human fibroblast collagenase. Complete primary structure and homology to an oncogene transformation-induced rat protein.
复制标题
DOI：
--
复制
发表时间：
1986-05
期刊：
影响因子：
--
通讯作者：
G. Goldberg;S. Wilhelm;A. Kronberger;E. Bauer;G. A. Grant;A. Eisen
中科院分区：
文献类型：
--
作者：
G. Goldberg;S. Wilhelm;A. Kronberger;E. Bauer;G. A. Grant;A. Eisen
我们已经确定了cDNA克隆的完整序列，代表全尺寸的人皮肤胶原酶mRNA。胶原酶以Mr 54,092的前酶形式合成，含有19个氨基酸的长信号肽。该酶的主要分泌产物包括次要的糖基化形式Mr 57,000，以及预测Mr 51,929的主要未修饰多肽。人皮肤前胶原酶的蛋白水解激活导致原酶氨基末端去除81个氨基酸残基。两个潜在的n -糖基化位点都包含在酶的蛋白水解活化形式中。该克隆编码区的一级结构与一种致癌基因诱导的大鼠蛋白同源，其功能尚不清楚，尽管初步观察表明它不是大鼠皮肤胶原酶。
We have determined the complete sequence of the cDNA clone representing the full size human skin collagenase mRNA. Collagenase is synthesized in preproenzyme form, Mr 54,092, with a 19 amino acid long signal peptide. The primary secretion products of the enzyme consist of a minor glycosylated form, Mr 57,000, and a major unmodified polypeptide of predicted Mr 51,929. Proteolytic activation of human skin procollagenase results in removal of 81 amino acid residues from the amino-terminal portion of the proenzyme. Both potential N-glycosylation sites are contained within the proteolytically activated form of the enzyme. The primary structure of the coding region of the presented clone is homologous to an oncogene-induced rat protein whose function is still unknown, although preliminary observations suggest that it is not rat skin collagenase.