Methods for Studying Activation of Matrix Metalloproteinases

  • Vera Knäuper
  • Gillian Murphy
Protocol
Part of the Methods in Molecular Biology book series (MIMB, volume 622)

Abstract

The degradation of the extracellular matrix during development and in disease is thought to result from the combined action of several proteolytic enzyme systems, including the matrix metalloproteinases (MMPs), serine proteinases, and cysteine proteinases. The majority of the soluble MMPs are synthesized as proenzymes which require extracellular activation in order to gain proteolytic activity and the analysis of their activation mechanism is a prerequisite for understanding MMP-mediated proteolysis.

The emphasis of this chapter is the provision of the experimental tools to study MMP activation in vitro and in cellular model systems. Hence, we use the activation of procollagenase-3 (proMMP-13) and progelatinase A (proMMP-2) as examples of the methods used.

Key words

Activation proenzyme latency APMA trypsin 

Notes

Acknowledgments

The authors would like to thank Dr. C. López-Otín, Dr. A. M. Pendas, Dr. S. Cowell, Dr. M. Balbin, Dr. G. Velasco and M. L. Stewart for their contribution to our work during the years.

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Copyright information

© Humana Press, a part of Springer Science+Business Media, LLC 2010

Authors and Affiliations

  • Vera Knäuper
    • 1
  • Gillian Murphy
    • 2
  1. 1.Dental SchoolCardiff UniversityCardiffUK
  2. 2.Department of OncologyUniversity of CambridgeCambridgeUK

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