Apoptosis, or programmed cell death, is a physiological type of cell death that is essential for metazoans (animals). Metazoans require apoptosis both for the development, and the normal functioning of the adult organism. Abnormal levels of apoptosis have been involved in the pathogenesis of numerous human diseases including cancer, disorders of the immune system, neurodegenerative diseases (such as Alzheimer's and Parkinson's), as well as cardiac arrest and stroke damage. Apoptosis is initiated upon activation of a group of cysteine proteases called caspases, which cleave cellular substrates at specific sites, triggering apoptosis. Bcl-xL, an anti-apoptotic member of the Bcl-2 family of proteins, has been identified as one of the substrates for caspase cleavage. Bcl-xL is cleaved at the C-terminus of the amino acid residue aspartate (D) 61, which converts Bcl-xL into a pro-apoptotic protein. Our laboratory has identified BMRP (Bcl-2 interacting Mitochondrial Ribosomal Protein) as a novel Bcl-2 interacting protein with pro-apoptotic activity. We have generated a recombinant construct that drives the expression in mammalian cells of a mutant of Bcl-xL with enhanced anti-apoptotic activity (hBcl-xLD61A). This mutant will help us further our characterization studies of the role that BMRP plays in apoptosis signaling pathways.

Generation of a mutant hBclxL construct to be used in functional analysis of the pro-apoptotic protein BMRP

247th National Meeting (2014)

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