Time-resolved analysis of the matrix metalloproteinase 10 substrate degradome.

ABSTRACT: Proteolysis is an irreversible post-translational modification that affects intra- and intercellular communication by modulating the activity of bioactive mediators. Key to understanding protease function is the system-wide identification of cleavage events and their dynamics in physiological contexts. Despite recent advances in mass spectrometry-based proteomics for high-throughput substrate screening, current approaches suffer from high false positive rates and only capture single states of protease activity. Here, we present a workflow based on multiplexed terminal amine isotopic labeling of substrates for time-resolved substrate degradomics in complex proteomes. This approach significantly enhances confidence in substrate identification and categorizes cleavage events by specificity an

SUBMITTER: Schlage P 

PROVIDER: S-EPMC3916655 | biostudies-literature | 2014 Feb

REPOSITORIES: biostudies-literature