Cathepsin D expression as a regulator of breast cancer cell migration and chemosensitivity
| Authors | |
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| Year of publication | 2011 |
| Type | Conference abstract |
| MU Faculty or unit | |
| Citation | |
| Description | The lysosomal aspartic protease cathepsin D (cath-D) is often over-expressed in breast cancer and acts as a mitogen on both cancer and stromal cells. The ability of cath-D to stimulate cancer cell migration remains controversial. To determine whether cath-D expression modulates breast cancer cell migration in vitro, we performed a real-time analysis of MDA-MB-231 breast cancer cell migration using novel methodology based on impedance measurement that enables continuous monitoring of the transition of the cells through a microporous membrane [xCELLigence equipped with CIM-plate 16 (Roche)]. We observed that altering cath-D level by either siRNA or cDNA tranfections significantly affected migration of MDA-MB-231 cells. Tumor cells have often impaired classical caspase-dependent apoptosis pathway and may be therefore more sensitive to agents that trigger alternative cell death pathways. Targeting lysosomes represents a method of choice as many human tumors have increased levels of lysosomal proteases. |
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