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Collagenase (MMP-1) has the singular ability to degrade collagen types I, I1 and III at neutral pH, and production of this enzyme by tumor cells and neighboring normal fibroblasts contributes to the invasive potential of tumors. In normal fibroblasts, constitutive levels of MMP-1 are low, but can be stimulated by agents such as phorbol esters. In contrast, A2058 human melanoma cells show strikingly high constitutive levels of MMP-1 and can not be induced by phorbol. We used several kinase inhibitors, the PKC inhibitors Bisindolymaleimide (BE) or Calphostin C (CAL), and the soluble tyrosine kinase inhibitor Herbimycin (HERB), to investigate the signal/transduction mechanisms responsible for phorbol inducibility in rabbit fibroblasts and for high constitutive expression in A2058 cells. Western blot analysis showed that a 24 hour treatment with BIS (10-6 and lO-7M) or CAL (10hM) reduced MMP-1 levels in phorbol-stimulated fibroblasts but did not reduce MMP-1 levels in A2058 cells. In contrast, 24 hours exposure to HERB (104 and 10-7M) lowered MMP-1 levels in tumor cells but not in PMA-treated fibroblasts. Results of Northern blots were similar, with CAL causing a 70% reduction in MMP-1

Who reads Cancer Cell Invasion and Motility?

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); John Wiley & Sons Inc.; Wiley (ISSN 0730-2312)

Published

1995

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)