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Licensed Unlicensed Requires Authentication Published by De Gruyter June 11, 2010

The substrate specificity profile of human granzyme A

  • Petra Van Damme , Sebastian Maurer-Stroh , Han Hao , Niklaas Colaert , Evy Timmerman , Frank Eisenhaber , Joël Vandekerckhove and Kris Gevaert
From the journal Biological Chemistry

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.


Corresponding authors ;

Received: 2010-2-2
Accepted: 2010-4-29
Published Online: 2010-06-11
Published in Print: 2010-08-01

©2010 by Walter de Gruyter Berlin New York

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