Cathepsin B and tumor proteolysis: contribution of the tumor microenvironment

Semin Cancer Biol. 2005 Apr;15(2):149-57. doi: 10.1016/j.semcancer.2004.08.001. Epub 2004 Dec 30.


Tumor-stromal interactions induce expression of matrix metalloproteinases and serine proteases and, as shown recently, the cysteine protease cathepsin B. We speculate that such interactions upregulate the transcription factor Ets1, resulting in increased cathepsin B expression. This would be consistent with the observed concomitant upregulation of matrix metalloproteinases and serine proteases as well as with the ability of extracellular matrices and their binding partners to alter cathepsin B expression and secretion. Using a confocal assay to analyze the contribution of tumor-stromal interactions to proteolysis, we have been able to confirm enhanced degradation of extracellular matrices by all three classes of proteases.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Animals
  • Cathepsin B / analysis
  • Cathepsin B / metabolism*
  • Cell Communication / physiology
  • Humans
  • Mice
  • Neoplasms / enzymology*
  • Neoplasms / pathology
  • Stromal Cells / physiology


  • Cathepsin B