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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Cathepsin K, but not cathepsins B, L, or S, is abundantly expressed in human osteoclasts.

Random high throughput sequencing of a human osteoclast cDNA library was employed to identify novel osteoclast-expressed genes. Of the 5475 ESTs obtained, approximately 4% encoded cathepsin K, a novel cysteine protease homologous to cathepsins S and L; ESTs for other cathepsins were rare. In addition, ESTs for cathepsin K were absent or at low frequency in cDNA libraries from numerous other tissues and cells. In situ hybridization in osteoclastoma and osteophyte confirmed that cathepsin K mRNA was highly expressed selecively in osteoclasts; cathepsins S, L, and B were not detectable. Cathepsin K was not detected by in situ hybridization in a panel of other tissues. Western blot of human osteoclastoma or fetal rat humerus demonstrated bands of 38 and 27 kDa, consistent with sizes predicted for pro- and mature cathepsin K. Immunolocalization in osteoclastoma and osteophyte showed intense punctate staining of cathepsin K exclusively in osteoclasts, with a polar distribution that was more intense at the bone surface. The abundant expression of cathepsin K selectively in osteoclasts strongly suggests that it plays a specialized role in bone resorption. Furthermore, the data suggest that random sequencing of ESTs from cDNA libraries is a valuable approach for identifying novel cell-selective genes.[1]


  1. Cathepsin K, but not cathepsins B, L, or S, is abundantly expressed in human osteoclasts. Drake, F.H., Dodds, R.A., James, I.E., Connor, J.R., Debouck, C., Richardson, S., Lee-Rykaczewski, E., Coleman, L., Rieman, D., Barthlow, R., Hastings, G., Gowen, M. J. Biol. Chem. (1996) [Pubmed]
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