Cathepsin B and tumor proteolysis: contribution of the tumor microenvironment

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 consist...

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Bibliographic Details
Published in:Seminars in cancer biology 2005-04, Vol.15 (2), p.149-157
Main Authors: Sloane, Bonnie F., Yan, Shiqing, Podgorski, Izabela, Linebaugh, Bruce E., Cher, Michael L., Mai, Jianxin, Cavallo-Medved, Dora, Sameni, Mansoureh, Dosescu, Julie, Moin, Kamiar
Format: Article
Language:English
Subjects:
Animals
Bone
Cathepsin B - analysis
Cathepsin B - metabolism
Cell Communication - physiology
Cysteine proteases
Endothelial cells
Humans
Inflammatory cells
Mice
Neoplasms - enzymology
Neoplasms - pathology
Stromal Cells - physiology
Stromal elements
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Summary: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.
ISSN:1044-579X
1096-3650
DOI:10.1016/j.semcancer.2004.08.001