Nonhuman cells correctly sort and process the human lysosomal enzyme cathepsin D.
Nonhuman cells correctly sort and process the human lysosomal enzyme cathepsin D.
复制标题
非人类细胞正确分类和处理人类溶酶体酶组织蛋白酶 D。
DOI：
10.1021/bi00434a057
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发表时间：
1989
期刊：
影响因子：
2.9
通讯作者：
Sola,J
中科院分区：
文献类型：
--
作者：
Conner,GE;Udey,JA;Pinto,C;Sola,J
Gregory E. Conner,** Jenny A. Udey, Cristina Pinto, 1 and Juan Sola Department of Anatomy and Cell Biology, University of Miami School of Medicine, Miami, Florida 33101 Received October 4, 1988; Revised Manuscript Received December 20, 1988 abstract: Cathepsin D, like most lysosomal enzymes, undergoes multiple proteolytic cleavages during its lifetime. Although the significance of the earliest cleavages of cathepsin D is apparent (loss of the NH2-terminal signalpeptide and activation peptide), functions of the two later cleavages are not understood and do not occur in all species. To examine these later events, a cDNA coding for human cathepsin D, which is normally processed to a two-chain form, was isolated and then expressed in mammalian cells from species which do not process the enzyme to the two-chain form. Analysis of the expressed human cathepsinD demonstrated proteolytic processing identical with that seen in normal human fibroblasts. Since processing to the two-chain form of the enzyme occurs in the lysosome, these studies revealed that the humancathepsin D was correctly sorted. The data also indicated that the sorting mechanism was conserved between diverse species and that late proteolytic processing in a variety of species was not determined by the presence or
