Complementary positional proteomics for screening substrates of endo- and exoproteases.
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.
Van Damme
Petra
P
Department of Medical Protein Research, Vlaams Instituut voor Biotechnologie, Ghent, Belgium.
Staes
An
A
Bronsoms
Silvia
S
Helsens
Kenny
K
Colaert
Niklaas
N
Timmerman
Evy
E
Aviles
Francesc X
FX
Vandekerckhove
Joël
J
Gevaert
Kris
K
D000595:Amino Acid Sequence; D043422:Carboxypeptidases A / Q000378:metabolism*; D002460:Cell Line; D053804:Granzymes / Q000378:metabolism*; D006801:Humans; D008969:Molecular Sequence Data; D010446:Peptide Fragments; D040901:Proteomics / Q000379:methods*; D013379:Substrate Specificity
D010446:Peptide Fragments; C539656:CPA4, human; D043422:Carboxypeptidases A; D053804:Granzymes