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Metalloproteases and the Degradome

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Matrix Metalloproteinase Protocols

Part of the book series: Methods in Molecular Biology ((MIMB,volume 622))

Abstract

Metalloproteases comprise a heterogeneous group of proteolytic enzymes whose main characteristic is the utilization of a metal ion to polarize a water molecule and perform hydrolytic reactions. These enzymes represent the most densely populated catalytic class of proteases in many organisms and play essential roles in multiple biological processes. In this chapter, we will first present a general description of the complexity of metalloproteases in the context of the degradome, which is defined as the complete set of protease genes encoded by the genome of a certain organism. We will also discuss the functional relevance of these enzymes in a large variety of biological and pathological conditions. Finally, we will analyze in more detail three families of metalloproteases: ADAMs (a disintegrin and metalloproteinase), ADAMTSs (ADAMs with thrombospondin domains), and MMPs (matrix metalloproteinases) which have a growing relevance in a number of human pathologies including cancer, arthritis, neurodegenerative disorders, and cardiovascular diseases.

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Authors and Affiliations

  1. Departamento de Bioquímica y Biología Molecular, Universidad de Oviedo, Oviedo, Spain

    Alejandro P. Ugalde, Gonzalo R. Ordóñez, Pedro M. Quirós, Xose S. Puente & Carlos López-Otín

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  1. Alejandro P. Ugalde
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  2. Gonzalo R. Ordóñez
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  3. Pedro M. Quirós
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  4. Xose S. Puente
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  5. Carlos López-Otín
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  1. School of Biological Sciences, University of East Anglia, Norwich, NR47TJ, United Kingdom

    Ian M. Clark

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Ugalde, A.P., Ordóñez, G.R., Quirós, P.M., Puente, X.S., López-Otín, C. (2010). Metalloproteases and the Degradome. In: Clark, I. (eds) Matrix Metalloproteinase Protocols. Methods in Molecular Biology, vol 622. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-60327-299-5_1

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  • DOI: https://doi.org/10.1007/978-1-60327-299-5_1

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