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By Peter J. Quinn (Editor), Valerian E. Kagan (Editor)

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Additional info for Phospholipid Metabolism in Apoptosis (Subcellular Biochemistry, Volume 36) (Subcellular Biochemistry)

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Med. 189: 381-393. , 1998, Caspases: enemies within, Science 281: 13121316. , 2000, Susceptibility to drug-induced apoptosis correlates with differential modulation of Bad, Bcl-2 and protein levels, Cell Death and Differentiation 7: 574-586. , 1999, Nitric oxide-induced apoptosis in human leukemic lines requires mitochondrial lipid degradation and cytochrome c release, Blood 93: 2342-2352. , Nature Cell Biology 1: E209-216. , 2000, Permeabilization of the mitochrondrial inner membrane during apoptosis: impact of the adenine nucleotide translocator, Cell Death and Differentiation 7: 1146-1154.

44 Peter J. Quinn 1986). Methods of assessing transmembrane movement of sphingolipids have been reviewed by Sillence et al. (2000). Measurement of transmembrane movement of phospholipids using florescent or other probe methods requires demonstration that incorporation of the phospholipid analogs occurs by a monomeric transfer from an exogenous resevoir into the outer leaflet of the plasma membrane rather than a fusion of bilayer vectors containing the probes with the plasma membrane. This problem has been addressed by Gadella et al.

When the basic protein shuttles between complexes III and IV, cardiolipin facilitates the binding of cytochrome c to cytochrome c oxidase-containing membranes (Salamon and Tollin, 1996). In other words, cytochrome c oxidase in complex IV efficiently receives electrons from cytochrome c only in the presence of cardiolipin. , 2000). , 1997). The binding of cytochrome c to cardiolipin is very tight, apparently irreversible, and stoichiometric (Rytömaa and Kinnunen, 1995), suggesting that this unique phospholipid, cardiolipin, may anchor the small heme protein to the inner 24 Yoshihiro Shidoji et al.

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