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Degradomics reveals that cleavage specificity profiles of caspase-2 and effector caspases are alike

Magdalena Wejda UGent, Francis Impens UGent, Nozomi Takahashi UGent, Petra Van Damme UGent, Kris Gevaert UGent and Peter Vandenabeele UGent (2012) JOURNAL OF BIOLOGICAL CHEMISTRY. 287(41). p.33983-33995
abstract
Caspase-2 is considered an initiator caspase because its long prodomain contains a CARD domain that allows its recruitment and activation in several complexes by homotypic death domain-fold interactions. Because little is known about the function and specificity of caspase-2 and its physiological substrates, we compared the cleavage specificity profile of recombinant human caspase-2 with those of caspase-3 and -7 by analyzing cell lysates using N-terminal COmbined FRActional DIagonal Chromatography (COFRADIC). Substrate analysis of the 68 cleavage sites identified in 61 proteins revealed that the protease specificities of human caspases-2, -3, and -7 largely overlap, revealing the DEVD down arrow G consensus cleavage sequence. We confirmed that Asp(563) in eukaryotic translation initiation factor 4B (eIF4B) is a cleavage site preferred by caspase-2 not only in COFRADIC setup but also upon co-expression in HEK 293T cells. These results demonstrate that activated human caspase-2 shares remarkably overlapping protease specificity with the prototype apoptotic executioner caspases-3 and -7, suggesting that caspase-2 could function as a proapoptotic caspase once released from the activating complex.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
N-TERMINAL PEPTIDES, FRACTIONAL DIAGONAL CHROMATOGRAPHY, CYTOSOLIC PHOSPHOLIPASE A(2), FAS-INDUCED APOPTOSIS, CELL-DEATH, QUANTITATIVE PROTEOMICS, INFLAMMATORY CASPASES, GENOTOXIC STRESS, STRUCTURAL BASIS, DNA-DAMAGE
journal title
JOURNAL OF BIOLOGICAL CHEMISTRY
J. Biol. Chem.
volume
287
issue
41
pages
33983 - 33995
Web of Science type
Article
Web of Science id
000309654200006
JCR category
BIOCHEMISTRY & MOLECULAR BIOLOGY
JCR impact factor
4.651 (2012)
JCR rank
61/288 (2012)
JCR quartile
1 (2012)
ISSN
0021-9258
DOI
10.1074/jbc.M112.384552
project
Ghent researchers on unfolded proteins in inflammatory disease (GROUP-ID)
project
Ghent researchers on unfolded proteins in inflammatory disease (GROUP-ID)
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
3053575
handle
http://hdl.handle.net/1854/LU-3053575
date created
2012-11-15 12:05:00
date last changed
2014-05-12 11:01:58
@article{3053575,
  abstract     = {Caspase-2 is considered an initiator caspase because its long prodomain contains a CARD domain that allows its recruitment and activation in several complexes by homotypic death domain-fold interactions. Because little is known about the function and specificity of caspase-2 and its physiological substrates, we compared the cleavage specificity profile of recombinant human caspase-2 with those of caspase-3 and -7 by analyzing cell lysates using N-terminal COmbined FRActional DIagonal Chromatography (COFRADIC). Substrate analysis of the 68 cleavage sites identified in 61 proteins revealed that the protease specificities of human caspases-2, -3, and -7 largely overlap, revealing the DEVD down arrow G consensus cleavage sequence. We confirmed that Asp(563) in eukaryotic translation initiation factor 4B (eIF4B) is a cleavage site preferred by caspase-2 not only in COFRADIC setup but also upon co-expression in HEK 293T cells. These results demonstrate that activated human caspase-2 shares remarkably overlapping protease specificity with the prototype apoptotic executioner caspases-3 and -7, suggesting that caspase-2 could function as a proapoptotic caspase once released from the activating complex.},
  author       = {Wejda, Magdalena and Impens, Francis and Takahashi, Nozomi and Van Damme, Petra and Gevaert, Kris and Vandenabeele, Peter},
  issn         = {0021-9258},
  journal      = {JOURNAL OF BIOLOGICAL CHEMISTRY},
  keyword      = {N-TERMINAL PEPTIDES,FRACTIONAL DIAGONAL CHROMATOGRAPHY,CYTOSOLIC PHOSPHOLIPASE A(2),FAS-INDUCED APOPTOSIS,CELL-DEATH,QUANTITATIVE PROTEOMICS,INFLAMMATORY CASPASES,GENOTOXIC STRESS,STRUCTURAL BASIS,DNA-DAMAGE},
  language     = {eng},
  number       = {41},
  pages        = {33983--33995},
  title        = {Degradomics reveals that cleavage specificity profiles of caspase-2 and effector caspases are alike},
  url          = {http://dx.doi.org/10.1074/jbc.M112.384552},
  volume       = {287},
  year         = {2012},
}

Chicago
Wejda, Magdalena, Francis Impens, Nozomi Takahashi, Petra Van Damme, Kris Gevaert, and Peter Vandenabeele. 2012. “Degradomics Reveals That Cleavage Specificity Profiles of Caspase-2 and Effector Caspases Are Alike.” Journal of Biological Chemistry 287 (41): 33983–33995.
APA
Wejda, M., Impens, F., Takahashi, N., Van Damme, P., Gevaert, K., & Vandenabeele, P. (2012). Degradomics reveals that cleavage specificity profiles of caspase-2 and effector caspases are alike. JOURNAL OF BIOLOGICAL CHEMISTRY, 287(41), 33983–33995.
Vancouver
1.
Wejda M, Impens F, Takahashi N, Van Damme P, Gevaert K, Vandenabeele P. Degradomics reveals that cleavage specificity profiles of caspase-2 and effector caspases are alike. JOURNAL OF BIOLOGICAL CHEMISTRY. 2012;287(41):33983–95.
MLA
Wejda, Magdalena, Francis Impens, Nozomi Takahashi, et al. “Degradomics Reveals That Cleavage Specificity Profiles of Caspase-2 and Effector Caspases Are Alike.” JOURNAL OF BIOLOGICAL CHEMISTRY 287.41 (2012): 33983–33995. Print.