The Overexpression of Cathepsin D Senzitizes Brest Cancer Cells to TRAIL-induced Apoptosis
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Year of publication | 2011 |
Type | Conference abstract |
MU Faculty or unit | |
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Description | 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. The lysosomal permeabilization pathway therefore offers a therapeutic window between cancer cells and normal tissue. TRAIL represents an anti-cancer therapeutic that can induce both classical and lysosomal apoptotic signaling. The lysosomal aspartic protease cathepsin D (cath-D) acts as mediator of induced-apoptosis by various chemotherapeutics. It has been suggested that cath-D can alter apoptosis pathways in enzymatic activity-dependent and independent manner. We conclude that Cath-D sensitizes breast carcinoma cells MDA-MB-231 to TRAIL-induced apoptosis in enzymatic activity-dependent manner. |
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