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J Biol Chem. 1992 Jul 5;267(19):13708-13.

Phylogenetic conservation of cysteine proteinases. Cloning and expression of a cDNA coding for human cathepsin S.

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Institute of Physiological Chemistry, Martin Luther University, Halle, Federal Republic of Germany.


A 1.8-kilobase full-length cDNA of human cathepsin S, a lysosomal cysteine proteinase, has been isolated. The single long open reading frame encodes a polypeptide of 331 amino acids consisting of a 15-amino acid NH2-terminal signal peptide, a propeptide of 99 amino acids, and a mature polypeptide of 217 amino acids. The deduced amino acid sequence contains only one potential N-glycosylation site located in the propeptide. The NH2-terminal amino acid sequence of the mature polypeptide was confirmed by sequencing cathepsin S purified from human spleen. The cDNA detects a 1.9-kilobase transcript in poly(A)+ RNA from human fibroblasts. Expression of human cathepsin S in transfected baby hamster kidney cells resulted in up to more than 300-fold cathepsin S activity as compared to untransfected controls. In the expressing baby hamster kidney cells, human cathepsin S is transported to the lysosomes via the mannose 6-phosphate receptor pathway as shown by density gradient centrifugation, immunofluorescence, and detection of the 37-kDa cathepsin S precursor in the medium in the presence of NH4Cl. The deduced amino acid sequence of human cathepsin S exhibits a substantial degree of similarity with other human cysteine proteinases and papain indicating that they have a common ancestral gene and are members of a gene family.

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