HUMAN CATHEPSIN O2, A NOVEL CYSTEINE PROTEASE HIGHLY EXPRESSED IN OSTEOCLASTOMAS AND OVARY MOLECULAR-CLONING, SEQUENCING AND TISSUE DISTRIBUTION
HUMAN CATHEPSIN O2, A NOVEL CYSTEINE PROTEASE HIGHLY EXPRESSED IN OSTEOCLASTOMAS AND OVARY MOLECULAR-CLONING, SEQUENCING AND TISSUE DISTRIBUTION
复制标题
DOI：
10.1515/bchm3.1995.376.6.379
复制
发表时间：
1995-06-01
期刊：
影响因子：
--
通讯作者：
OKAMOTO, K
中科院分区：
文献类型：
--
作者：
BROMME, D;OKAMOTO, K
一种新型人类半胱氨酸蛋白酶全长1.6千碱基cDNA已被分离并测序。该核苷酸序列编码一个329个氨基酸的多肽，由15个残基的n端信号肽、99个残基的前肽和215个氨基酸的成熟蛋白组成。推导出的氨基酸序列包含两个潜在的n -糖基化位点，一个位于前区，一个位于成熟酶中。将cathepsin O2的氨基酸序列与已知的人类溶酶体半胱氨酸蛋白酶的氨基酸序列进行比较，发现其与cathepsin L和s有很大程度的相似性。Northern blot分析表明，该酶在破骨细胞瘤和卵巢中主要表达，因此将其命名为cathepsin O2。人类组织蛋白酶O2在破骨细胞瘤中极高的表达水平表明这种新酶在骨重塑和骨相关疾病中起主要作用。
A 1.6-kilobase full-length cDNA of a novel human cysteine protease has been isolated and sequenced. The nucleotide sequence encodes a polypeptide of 329 amino acids composed of a 15-residue N-terminal signal peptide, a 99-residue propeptide, and a mature protein of 215 amino acids. The deduced amino acid sequence contains two potential N-glycosylation sites, one located in the proregion and one in the mature enzyme. Comparison of the amino acid sequence of cathepsin O2 with that of known human lysosomal cysteine proteases revealed a substantial degree of similarity to cathepsins L, and S. Northern blot analysis indicates predominant levels of expression in osteoclastomas and ovary and therefore the enzyme was named cathepsin O2. The extremely high expression levels of human cathepsin O2 in osteoclastomas suggest a major role of this novel enzyme in bone remodelling and bone related diseases.