Proteomic approaches to uncover MMP function

Pascal Schlage; Ulrich auf dem Keller

doi:10.1016/j.matbio.2015.01.003

Proteomic approaches to uncover MMP function

Matrix Biol. 2015 May-Jul:44-46:232-8. doi: 10.1016/j.matbio.2015.01.003. Epub 2015 Jan 17.

Authors

Pascal Schlage¹, Ulrich auf dem Keller²

Affiliations

¹ Institute of Molecular Health Sciences, ETH Zurich, CH-8093 Zurich, Switzerland.
² Institute of Molecular Health Sciences, ETH Zurich, CH-8093 Zurich, Switzerland. Electronic address: ulrich.aufdemkeller@biol.ethz.ch.

PMID: 25603365
DOI: 10.1016/j.matbio.2015.01.003

Abstract

Proteomics has revolutionized protease research and particularly contributed to the identification of novel substrates and their sites of cleavage as key determinants of protease function. New technologies and rapid advancements in development of powerful mass spectrometers allowed unprecedented insights into activities of matrix metalloproteinases (MMPs) within their complex extracellular environments. Mass spectrometry-based proteomics extended our knowledge on MMP cleavage specificities and will help to develop more specific inhibitors as new therapeutics. Quantitative proteomics and N-terminal enrichment strategies have revealed numerous novel MMP substrates and shed light on their modes of action in vitro and in vivo. In this review, we provide an overview of current proteomic technologies in protease research and their application to the functional characterization of MMPs.

Keywords: Degradomics; Matrix metalloproteinases; Proteomics; TAILS; iTRAQ.

Publication types

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

MeSH terms

Animals
Humans
In Vitro Techniques
Mass Spectrometry
Matrix Metalloproteinases / metabolism*
Proteomics / methods*
Substrate Specificity

Substances

Matrix Metalloproteinases