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Volumn 282, Issue 5392, 1998, Pages 1318-1321

Regulation of cell death protease caspase-9 by phosphorylation

Author keywords

[No Author keywords available]

Indexed keywords

PROTEINASE;

EID: 0032515027     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.282.5392.1318     Document Type: Article
Times cited : (2770)

References (44)
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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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    • 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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    • 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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    • 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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    • note
    • 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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