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Molecular cloning of human cDNA for cathepsin K: novel cysteine proteinase predominantly expressed in bone.

Authors
  • Inaoka, T
  • Bilbe, G
  • Ishibashi, O
  • Tezuka, K
  • Kumegawa, M
  • Kokubo, T
Type
Published Article
Journal
Biochemical and biophysical research communications
Publication Date
Jan 05, 1995
Volume
206
Issue
1
Pages
89–96
Identifiers
PMID: 7818555
Source
Medline
License
Unknown

Abstract

We have previously cloned a rabbit cDNA clone (OC-2) from an osteoclast cDNA library by the differential screening. OC-2 was found to encode a novel cysteine proteinase, tentatively called cathepsin K, which is predominantly expressed in osteoclasts. By use of a rabbit OC-2 fragment as a probe, its human counterpart was cloned from a cDNA library of osteoarthritic hip bone. The cloned human cDNA (hOC-2) encoded a protein of 329 amino acid residues and its deduced amino acid sequence showed 94% homology to rabbit cathepsin K. Multiple alignment of amino acid sequences of human cathepsins B, H, L, S and K showed the highest homology of cathepsin K to cathepsin S 48%. Northern blot analysis showed that cathepsin K mRNA is expressed at high levels in some osteoarthritic hip bones and at a very high level in osteoclastoma compared to very low levels in other tissues. These results suggest that cathepsin K is closely involved in human osteoclastic bone resorption.

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