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. 2008 Nov 17;183(4):681–696. doi: 10.1083/jcb.200803129

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© 2008 Gonzalvez et al.

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.jcb.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).

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Figure 3. — Tafazzin-deficient cells are defective in cytochrome c and Smac/Diablo release from mitochondria and in the activation of caspase-3 after Fas activation. (A) Caspase-3 activity of control (shCont1) and tafazzin-deficient HeLa cells (shTaz2) was monitored in untreated, anti-Fas antibody-treated for 14 h (Fas), and anti-Fas antibody– and DEVD-fmk–treated cells (FasDEVD). PARP and caspase-3 cleavage, both known caspase-3 targets, were analyzed by Western blotting. (B) Cytochrome c release from mitochondria before and after a 14-h treatment with anti-Fas antibody in the presence of DEVD-fmk was analyzed in control (shCont1) and tafazzin-knockdown (shTaz2) cells by immunostaining. The release of cytochrome c was evident in several cells in each microscopic field, judged by the diffusion of the protein in the cytosol and by the overall lower intensity of the immunostained protein (white arrows). Cells in which cytochrome c is retained in the mitochondria (punctuated staining and high intensity) are indicated by green arrows. DAPI was used to stain the nuclei. (C) Smac/Diablo release was analyzed as for cytochrome c. (D) Cytochrome c release was detected by a Western blot analysis of cytosolic fractions of the indicated cells treated as in B. Bars, 10 μm.