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Cloning and complete coding sequence of a novel human cathepsin expressed in giant cells of osteoclastomas
Author(s) -
Li YiPing,
Alexander Mary,
Wucherpfennig Anne L.,
Yelick Pamela,
Chen Wei,
Stashenko Philip
Publication year - 1995
Publication title -
journal of bone and mineral research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.882
H-Index - 241
eISSN - 1523-4681
pISSN - 0884-0431
DOI - 10.1002/jbmr.5650100809
Subject(s) - cathepsin e , cathepsin h , cathepsin a , cathepsin o , microbiology and biotechnology , cathepsin l1 , biology , cathepsin , cathepsin s , cathepsin l , cathepsin k , complementary dna , cdna library , cathepsin d , cathepsin c , cathepsin b , biochemistry , gene , osteoclast , enzyme , in vitro
A gene encoding a possible novel human cathepsin, a cysteine proteinase that is distinct from previously characterized enzymes, has been identified by differential screening of a human osteoclastoma cDNA library. This molecule, termed cathepsin X, appears to represent the human homolog of the osteoclast‐expressed rabbit cathepsin OC‐2. Cathepsin X (GenBank accession number U20280) is 93.9% identical to OC‐2 at the amino acid level, and is 92% identical at the nucleotide level within the coding region. Cathepsin X is 52.2 and 46.9% identical to cathepsins S and L, respectively, and is therefore clearly distinct from these enzymes. Cathepsin X mRNA was localized to multinucleated giant cells within the osteoclastoma tumor by in situ hybridization. These data strongly support the hypothesis that cathepsin X represents a novel cysteine proteinase which is expressed at high levels in osteoclasts.