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3643141742
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note
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Single-letter abbreviations for the amino acid residues are as follows: A, Cys; D, Asp; E, Glu; F, Phe; G, Gly; H, His; I, Ile; K. Lys; L, Leu; M, Met; N, Asn; P, Pro; Q, Gln; R, Arg; S, Ser; T, Thr, V, Val; W, Trp; X, any amino acid; and Y, Tyr.
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6
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3643115704
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unpublished data
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M. H. Cardone et al., unpublished data.
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0029079275
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NIH 3T3 cells expressing activated oncogenic Akt were generated by viral infection of NIH 3T3 cells with a retrovirus expressing v-akt [T. Franke et al., Cell 81, 727 (1995)].
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Franke, T.1
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20
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3643052015
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note
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4, 10 mM β-glycerophosphate, and protease inhibitors. Lysates were precleared with protein A-or protein G-Sepharose with preimmune serum. Casp9 was immunoprecipitated with a monoclonal antibody (mAb) to FLAG or a polyclonal antibody to Casp9. washed, and analyzed by SDS-polyacrylamide gel elertrophoresis (SDS-PAGE) and autoradiography or by phosphoimager analysis.
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21
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3643082381
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note
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6-artive Casp9 and verified to be specific for Casp9 by immunoblotting experiments using a panel of recombinant caspases, including Casp3, Casp6, Casp7, Casp8, and Casp10.
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23
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0031053586
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H. Dudek et al., Science 275, 661 (1997).
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3643142777
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note
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2, 1 mM DTT, and 3 μM ATP].
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25
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Q. Deveraux et al., EMBO J. 17, 2215 (1998).
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3643088656
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note
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GST-Akt was expressed from a recombinant baculo-virus in Sf9 cells with activated forms of PI3K to achieve kinase activation. GST-Akt was purified from Sf9 lysates by glutathione-Sepharose affinity chromatography.
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28
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3643134320
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note
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32P]ATP. Immobilized Akt was removed by centrifugation, and half the sample (20 μl) was incubated with 10 μM Ac-DEVD-pNA (Alexis) and 2 μM purified pro-Casp3 in a final volume of 0.1 ml of caspase buffer (50 mM Hepes, 1 mM EDTA, 0.1% CHAPS, 10% sucrose, and 5 mM dithiothreitol). Caspase activity was based on cleavage of the colorimetric substrate Ac-DEVD-pNA (5) and was normalized relative to Akt-untreated (mock) material. For Casp9 measurements, the addition of pro-Casp3 created a coupled Casp9 → Casp3 → DEVD-pNA reaction, because Casp9 does not efficiently cleave DEVD (16). Activity percent was measured and normalized to mock-treated samples. Anti-HA immune complexes prepared from control-transfected cells and immobilized GST control protein resulted in no significant alterations of caspase activity (4).
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29
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3643075106
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note
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600 ≅ 0.6 to 0.8 and ∼25°C for 4 hours for the S183A mutant and for 1 hour for the S196A mutant. Proteins were affinity purified by Ni-chelate Sepharose (Pharmacia).
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3643120851
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note
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4oAc (pH 4.0) at room temperature. The samples were then analyzed by SELDI as described above. An 80-dalton increase in mass indicated that the peptide fragment was phosphorylated.
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32
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3643114646
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note
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Casp9 mutants were generated by site-directed polymerase chain reaction (PCR) mutagenesis from a human pro-Casp9 cDNA (V. Dixit) and subcloned into pcDNA3-FLAG, pCMV2-FLAG, or pET23b plasmids. The primer pairs used to generate the S183A and S196A mutants were 5′-CCGCACCCGCACTG-GCGCGAACATCGACTGTGAG-3′ plus 5′-CTCACAGT-CGATGTTCGCGCCAGTGCGGGTGCGG-3′; and 5′-CGGCGTCGCTTCTCCGCGCTGCATTTCCTGGTGG-3′ plus 5′-CCACCATGAAATGCAGCGCGGAGAAGCGACG-CCG-3′, respectively. PCR was performed for 16 cycles at 95°C for 30 s, 55°C for 1 min, and 68°C for 12 min. Twenty microliters of the reactions was digested with Dpn I (10 U) for subsequent subcloning into plasmids.
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3643079223
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note
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We thank J. Rhim for 267 Ki-Ras cells; T. G. Sambandan for mass spectroscopy advice; I. Tamm for IAP measurements; S. Kitada for help with cell lines; T. Bobo, A. Sinskey, and P. Sorger for support and the members of the Reed lab for helpful discussions. This work was partially supported by a Biomeasure grant to M.C., a Department of Defense Breast Cancer grant to N.R., a Danish Natural Science Foundation grant (9600412) to H.R.S., and grants CA-69381 and CA-69515 from NIH and the National Cancer Institute.
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