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The substrate specificity profile of human granzyme A

Petra Van Damme UGent, Sebastian Maurer-Stroh, Han Hao, Niklaas Colaert UGent, Evy Timmerman UGent, Frank Eisenhaber, Joël Vandekerckhove UGent and Kris Gevaert UGent (2010) BIOLOGICAL CHEMISTRY. 391(8). p.983-997
abstract
The exact biological function of granzyme A, a granule-associated serine protease belonging to the tryptase family of proteases, is still a matter of debate because conflicting roles have been suggested, such as initiation of caspase-independent apoptosis-like cell death and endogenous modulation of inflammatory processes. In contrast to its well-studied family member, granzyme B, far less is known about the physiological targets of granzyme A. Using an N-terminal peptide-centric proteomics technology, the substrate specificity of human granzyme A was extensively characterized at the level of macromolecular protein substrates. Overall, more than 260 cleavage sites, almost exclusively favoring basic residues at the P1 position, in approximately 200 unique protein substrates, including the well-known in vitro substrates APEX-endonuclease 1 and different histones, were identified. Further substrate characterization was used to delineate physical properties in the substrate specificity profiles, which further highlights important aspects in protease/substrate biology.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (proceedingsPaper)
publication status
published
subject
keyword
proteolytic hotspots, protease degradomics, granzyme A, COFRADIC, proteomics, LYMPHOCYTE PROTEASE GRANZYME, INDEPENDENT CELL-DEATH, N-TERMINAL PEPTIDES, AMINO-ACID-RESIDUES, SECONDARY STRUCTURE, MEDIATED APOPTOSIS, ACTIVATED DNASE, CLEAVES, PREDICTION, PROTEINS
journal title
BIOLOGICAL CHEMISTRY
Biol. Chem.
volume
391
issue
8
pages
983 - 997
conference name
6th General Meeting of the International-Proteolysis-Society
conference location
Gold Coast, Australia
conference start
2009-10-26
conference end
2009-10-30
Web of Science type
Proceedings Paper
Web of Science id
000281198700015
JCR category
BIOCHEMISTRY & MOLECULAR BIOLOGY
JCR impact factor
3.603 (2010)
JCR rank
101/284 (2010)
JCR quartile
2 (2010)
ISSN
1431-6730
DOI
10.1515/BC.2010.096
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
1064461
handle
http://hdl.handle.net/1854/LU-1064461
date created
2010-10-26 14:38:11
date last changed
2013-01-30 09:41:34
@article{1064461,
  abstract     = {The exact biological function of granzyme A, a granule-associated serine protease belonging to the tryptase family of proteases, is still a matter of debate because conflicting roles have been suggested, such as initiation of caspase-independent apoptosis-like cell death and endogenous modulation of inflammatory processes. In contrast to its well-studied family member, granzyme B, far less is known about the physiological targets of granzyme A. Using an N-terminal peptide-centric proteomics technology, the substrate specificity of human granzyme A was extensively characterized at the level of macromolecular protein substrates. Overall, more than 260 cleavage sites, almost exclusively favoring basic residues at the P1 position, in approximately 200 unique protein substrates, including the well-known in vitro substrates APEX-endonuclease 1 and different histones, were identified. Further substrate characterization was used to delineate physical properties in the substrate specificity profiles, which further highlights important aspects in protease/substrate biology.},
  author       = {Van Damme, Petra and Maurer-Stroh, Sebastian and Hao, Han and Colaert, Niklaas and Timmerman, Evy and Eisenhaber, Frank and Vandekerckhove, Jo{\"e}l and Gevaert, Kris},
  issn         = {1431-6730},
  journal      = {BIOLOGICAL CHEMISTRY},
  keyword      = {proteolytic hotspots,protease degradomics,granzyme A,COFRADIC,proteomics,LYMPHOCYTE PROTEASE GRANZYME,INDEPENDENT CELL-DEATH,N-TERMINAL PEPTIDES,AMINO-ACID-RESIDUES,SECONDARY STRUCTURE,MEDIATED APOPTOSIS,ACTIVATED DNASE,CLEAVES,PREDICTION,PROTEINS},
  language     = {eng},
  location     = {Gold Coast, Australia},
  number       = {8},
  pages        = {983--997},
  title        = {The substrate specificity profile of human granzyme A},
  url          = {http://dx.doi.org/10.1515/BC.2010.096},
  volume       = {391},
  year         = {2010},
}

Chicago
Van Damme, Petra, Sebastian Maurer-Stroh, Han Hao, Niklaas Colaert, Evy Timmerman, Frank Eisenhaber, Joël Vandekerckhove, and Kris Gevaert. 2010. “The Substrate Specificity Profile of Human Granzyme A.” Biological Chemistry 391 (8): 983–997.
APA
Van Damme, Petra, Maurer-Stroh, S., Hao, H., Colaert, N., Timmerman, E., Eisenhaber, F., Vandekerckhove, J., et al. (2010). The substrate specificity profile of human granzyme A. BIOLOGICAL CHEMISTRY, 391(8), 983–997. Presented at the 6th General Meeting of the International-Proteolysis-Society.
Vancouver
1.
Van Damme P, Maurer-Stroh S, Hao H, Colaert N, Timmerman E, Eisenhaber F, et al. The substrate specificity profile of human granzyme A. BIOLOGICAL CHEMISTRY. 2010;391(8):983–97.
MLA
Van Damme, Petra, Sebastian Maurer-Stroh, Han Hao, et al. “The Substrate Specificity Profile of Human Granzyme A.” BIOLOGICAL CHEMISTRY 391.8 (2010): 983–997. Print.