Cardiolipin plays a significant role in mitochondrial respiration, energetics, sequestering of cytochrome c, cristae remodeling and apoptosis. Remodeling of the mitochondrial lipid bilayer during the apoptotic event is believed to be necessary to achieve the release of apoptogenic factors from the intermemebrane space. Tafazzin is the premier mitochondrial enzyme for lipid remodeling. It has been demonstrated that cardiolipin serves as a platform for membrane insertion in the outer mitochondrial membrane by members of the Bcl-2 proapoptotic family. The proapoptotic protein Bax may be recruited from the cytosol to the mitochondria as a response to cardiolipin’s translocation from the mitochondrial inner membrane (MIM) to the mitochondrial outer membrane (MOM). The association of cardiolipin and Bax is thought to result in the formation of lipidic pores and may be a crucial step for the induction of apoptosis. We suspect that tafazzin is necessary for adequate biosynthesis of cardiolipin and that knocking out tafazzin will result in low cardiolipin, disrupting apoptosis.
Our research seeks to determine if apoptosis is diminished or deficient in tafazzin knockdown cardiomyocyte H9c2 cells. Secondly, to determine if Bax translocates to and inserts in the mitochondrial outer membrane in the absence of normal tafazzin protein. Answers provided in this research may reveal an essential role for cardiolipin and Bax in the intrinsic apoptotic pathway.
December 28, 2025