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Time-lapse videomicroscopy examined the course of 100 randomly selected cells over 24 hours. Cumulative apoptotic deaths at 4-hour intervals were plotted against time. Mean deaths for each time point and experimental condition for a minimum of three independent experiments are given. Videomicroscopic measurements of apoptosis were confirmed against trypan blue exclusion (a measure of loss of viability).
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™ VSMC lysates were incubated with anti-Fas-protein G complexes (3 hours, 4°C), precipitated, separated by 10% SDS-polyacrylamide gel electrophoresis (PAGE) in nonreducing conditions, and blotted with mouse anti-human FADD IgC (1 μg/ml).
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2], and protease inhibitor cocktail (PIC, Sigma), resuspended in an equal volume of KEHM, and homogenized. The homogenate was centrifuged through a discontinuous sucrose gradient (1.6, 1.2, or 0.8 M sucrose in KEHM and PIC), and the Golgi-enriched fraction was collected from the 0.8/1.2 M sucrose interface, separated by 10% SDS-PAGE, blotted, and probed with mouse anti-Fas IgG (100 ng/ml) (#F22120, Transduction Labs). Fractions were compared against homogenate, and whole-cell lysate was isolated for protein immunoblots.
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Retroviruses encoding pBabe Hygro FADD-DN or control vector (pBabe Hygro) [A. O. Hueber et al., Science 278, 1305 (1997)] were synthesized as in (10), cells were selected in hygromycin (200 μg/ml), and resistant cells were pooled.
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A Nru-Dra III fragment from pcDNA3 crmA (16), cloned into the adenovirus shuttle plasmid pAdBglII, was cotransfected with Xba I-Cla I-digested sub360 genomic DNA [T. Ohno et al., Science 265, 781 (1994)] into 293 cells. Recombinant virus was isolated by plaque purification, propagated in 293 cells, and purified by caesium chloride centrifugation. Virus titers were determined by plaque assay. Target cell infection of 100% was obtained with a multiplicity of infection of 100 per cell.
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™, E. Nabel and G. Nabel for crmA adenovirus, D. Galloway for pLHPV-E6 type 16, A. Hueber for lpr and gld MEFs and pBabe DN-FADD, T. Suganuma for anti-galactosyl transferase, and F. Buss, G. Evan, and M. Oren for advice and comments. Supported by British Heart Foundation grants FS/ 97024, PG/95057, and PG/96040 (to M.B.) and CH/ 9400 (to P. W.), Medical Research Council grant G9310915 (to J.P.L), and NIH grant HL34073 and the Bruce and Ruth Rappaport Program in Vascular Biology (to R.S.).
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