Affinity labeling displays the stepwise activation of ICE-related proteases by Fas, staurosporine, and CrmA-sensitive caspase-8

Oncogene
A TakahashiM Sasada

Abstract

The activation of multiple interleukin-1beta converting enzyme-related proteases (caspases) in apoptotic mammalian cells raises questions as to whether the multiple active caspases have distinct roles in apoptotic execution as well as how these proteases are organized in apoptotic signaling pathways. Here we used an affinity-labeling agent, YV(bio)KD-aomk, to investigate the caspases activated during apoptotic cell death. YV(bio)KD-aomk identified six distinct polypeptides corresponding to active caspases in Fas-stimulated Jurkat T cells. On staurosporine treatment, four polypeptides were detected. Competition experiments showed that the labeled caspases have distinct substrate preferences. Stepwise appearance of the labeled caspases in each cell death event was consistent with the view that the activated caspases are organized into protease cascades. Moreover, we found that stepwise activation of caspases similar to that induced by Fas ligation is triggered by exposing non-apoptotic Jurkat cell extracts to caspase-8 (MACH/FLICE/Mch5). Conversely, CrmA protein, a viral suppressor of Fas-induced apoptosis, inhibited the protease activity of caspase-8. Overall, these findings provide evidence that caspase-8, a CrmA-sensitive prot...Continue Reading

Citations

Nov 6, 2001·Journal of Biochemical and Biophysical Methods·N Shirasu, Y Shimohigashi
Sep 28, 1998·Biochimica Et Biophysica Acta·S H Kaufmann
Sep 19, 2003·Seminars in Nephrology·Gur P Kaushal
Jun 17, 2000·Progress in Neurobiology·K J BanasiakG G Haddad
Nov 14, 1997·Trends in Biochemical Sciences·P VillaW C Earnshaw
Feb 24, 2001·Cell Research·M WooT W Mak
Aug 5, 1999·The Biochemical Journal·S SatohK Shimotohno
Nov 3, 2005·Clinical Infectious Diseases : an Official Publication of the Infectious Diseases Society of America·Anuradha BalasubramanianRamesh K Ganju
Jan 26, 2000·Human Gene Therapy·J T BruderI Kovesdi
May 2, 1998·The EMBO Journal·C ScaffidiM E Peter
Feb 10, 2000·Annals of the New York Academy of Sciences·D K Miller
Jun 29, 2000·Annual Review of Biochemistry·W C EarnshawS H Kaufmann
Sep 8, 2001·Journal of Bone and Mineral Research : the Official Journal of the American Society for Bone and Mineral Research·O FromiguéJ J Body
Apr 1, 2013·Future Virology·Lisi AmslerVictor DeFilippis
Jul 22, 1998·Proceedings of the National Academy of Sciences of the United States of America·X LiuX Wang
Jan 5, 2001·Expert Opinion on Investigational Drugs·S M KornblauM Andreeff
Jan 29, 1999·FEBS Letters·P SchotteR Beyaert
May 10, 2006·Cytometry. Part a : the Journal of the International Society for Analytical Cytology·Xiaoli WuLiusheng He
Mar 4, 2005·The American Journal of Pathology·Thomas A NeffPeter A Ward
Dec 11, 2002·Biotechnology and Bioengineering·Tina M SauerwaldMichael J Betenbaugh
May 23, 2009·Renal Failure·Himanshu VashisthaPravin C Singhal
Feb 2, 1999·Experimental Cell Research·S C ChowG M Cohen
Aug 15, 1998·Archives of Biochemistry and Biophysics·K K WangH Allen
Feb 16, 2007·Cell Transplantation·Kimiaki TanakaNaoya Kobayashi
Apr 6, 2004·Free Radical Research·Joan B Mannick, Christopher M Schonhoff

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