Overview:
BID is a BH3 interacting death domain that heterodimerizes with either agonist BAX or antagonist BCL2 (1). BID is a member of the BCL-2 family of cell death regulators and is a mediator of mitochondrial damage induced by caspase-8 (CASP8). BID initiates apoptosis by binding to regulatory sites on prosurvival BCL2 proteins to directly neutralize their function. Multiple alternatively spliced transcript variants of BID have been found, but the full-length nature of some variants has not been defined. BID together with Cathepsins play an important role in the actions of Camptothecin on breast cancer cells (2).
References:
1. Hayakawa, A. et al:, Bid truncation mediated by caspases-3 and -9 in vinorelbine-induced apoptosis. Apoptosis. 2008;13(4):523-30.2. Lamparska-Przybysz. M. et al: Cathepsins and BID are involved in the molecular switch between apoptosis and autophagy in breast cancer MCF-7 cells exposed to camptothecin. J Physiol Pharmacol. 2005 Jun;56 Suppl 3:159-79.
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