The Structure of the Matrix B

On chemokine stimulation, leucocytes produce and secrete proteolytic enzymes for innate immunedefencemechanisms. Some of these proteasesmodify the biological activity of the chemokines. For instance, neutrophils secrete gelatinase B (matrix metalloproteinase-9, MMP-9) and neutrophil col-lagenase (MMP-8) after stimulation with interleukin-8/ CXCL8 (IL-8). Gelatinase B cleaves and potentiates IL-8, generating a positive feedback.

11p tumor12 20-04-2013 70 4   Download

Matrix metalloproteinase-9 (MMP-9) displays a preference for a broad range of substrates including extracellular matrix proteins and cytokines. MMP-9 plays an important role in physiological processes, as well as in inflammatory diseases and numerous cancers.

13p media19 05-03-2013 36 1   Download

Breast cancer cells exhibit excessive proteolysis, which is responsible for extensive extracellular matrix degradation, invasion and metastasis. Besides other proteases, lysosomal cysteine protease cathepsin B has been impli-cated in these processes and the impairment of its intracellular activity was suggested to reduce harmful proteolysis and hence diminish progression of breast tumors.

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Cathepsin B (EC 3.4.22.1) is a lysosomal cysteine protease with both endo-peptidase and exopeptidase activity. The former is associated with the deg-radation of the extracellular matrix proteins, which is a process required for tumour cell invasion and metastasis. In the present study, we show that 2A2 monoclonal antibody, raised by our group, is able to regulate cathep-sin B activity.

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Heparanase is an endo-b-D-glucuronidase capable of cleaving heparan sul-fate side chains at a limited number of sites, yielding heparan sulfate frag-ments of still appreciable size. Importantly, heparanase activity correlates with the metastatic potential of tumor-derived cells, attributed to enhanced cell dissemination as a consequence of heparan sulfate cleavage and remod-eling of the extracellular matrix and basement membrane underlying epithe-lial and endothelial cells.

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