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 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.
Sloane
Bonnie F
BF
Department of Pharmacology, Wayne State University, Detroit, MI 48201, USA. bsloane@med.wayne.edu
Yan
Shiqing
S
Podgorski
Izabela
I
Linebaugh
Bruce E
BE
Cher
Michael L
ML
Mai
Jianxin
J
Cavallo-Medved
Dora
D
Sameni
Mansoureh
M
Dosescu
Julie
J
Moin
Kamiar
K
D000818:Animals; D002401:Cathepsin B / Q000032:analysis / Q000378:metabolism*; D002450:Cell Communication / Q000502:physiology; D006801:Humans; D051379:Mice; D009369:Neoplasms / Q000201:enzymology* / Q000473:pathology; D017154:Stromal Cells / Q000502:physiology
D002401:Cathepsin B