Complementary positional proteomics for screening substrates of endo- and exoproteases

Petra Van Damme; An Staes; Silvia Bronsoms; Kenny Helsens; Niklaas Colaert; Evy Timmerman; Francesc X Aviles; Joël Vandekerckhove; Kris Gevaert

doi:10.1038/nmeth.1469

Complementary positional proteomics for screening substrates of endo- and exoproteases

Nat Methods. 2010 Jul;7(7):512-5. doi: 10.1038/nmeth.1469. Epub 2010 Jun 6.

Authors

Petra Van Damme¹, An Staes, Silvia Bronsoms, Kenny Helsens, Niklaas Colaert, Evy Timmerman, Francesc X Aviles, Joël Vandekerckhove, Kris Gevaert

Affiliation

¹ Department of Medical Protein Research, Vlaams Instituut voor Biotechnologie, Ghent, Belgium.

PMID: 20526345
DOI: 10.1038/nmeth.1469

Abstract

We describe a positional proteomics approach to simultaneously analyze N- and C-terminal peptides and used it to screen for human protein substrates of granzyme B and carboxypeptidase A4 in human cell lysates. This approach allowed comprehensive proteome studies, and we report the identification of 965 database-annotated protein C termini, 334 neo-C termini resulting from granzyme B processing and 16 neo-C termini resulting from carboxypeptidase A4 processing.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Carboxypeptidases A / metabolism*
Cell Line
Granzymes / metabolism*
Humans
Molecular Sequence Data
Peptide Fragments
Proteomics / methods*
Substrate Specificity

Substances

Peptide Fragments
CPA4, human
Carboxypeptidases A
Granzymes