Unit

UNIT 10.8 Matrix Metalloproteinases

  1. Henning Birkedal-Hansen1,
  2. Susan Yamada1,
  3. Jack Windsor2,
  4. Anne Havernose Pollard3,
  5. Guy Lyons4,
  6. William Stetler-Stevenson5,
  7. Bente Birkedal-Hansen5

Published Online: 1 SEP 2008

DOI: 10.1002/0471143030.cb1008s40

Current Protocols in Cell Biology

Current Protocols in Cell Biology

How to Cite

Birkedal-Hansen, H., Yamada, S., Windsor, J., Pollard, A. H., Lyons, G., Stetler-Stevenson, W. and Birkedal-Hansen, B. 2008. Matrix Metalloproteinases. Current Protocols in Cell Biology. 40:10.8:10.8.1–10.8.23.

Author Information

  1. 1

    National Institute of Dental Research, National Institutes of Health, Bethesda, Maryland

  2. 2

    University of Indiana School of Dentistry, Indianapolis, Indiana

  3. 3

    University of Copenhagen School of Dentistry, Copenhagen, Denmark

  4. 4

    Kanematsu Laboratories, Royal Prince Alfred Hospital, Sydney, Australia

  5. 5

    Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, Maryland

Publication History

  1. Published Online: 1 SEP 2008
  2. Published Print: SEP 2008

Abstract

Matrix metalloproteinases are a class of enzymes that play an important role in the remodeling of the extracellular matrix in development and cancer metastasis. This unit describes a set of methods—cell-mediated dissolution of type-1 collagen fibrils, direct and reverse zymography, enzyme capture based on α2-macroglobulin and TIMP-1 and -2, and demonstration of cryptic thiol groups in metalloproteinase precursors—that are used to characterize the functions of matrix metalloproteinases and their inhibitors. Curr. Protoc. Cell Biol. 40:10.8.1-10.8.23. © 2008 by John Wiley & Sons, Inc.

Keywords:

  • matrix metalloproteinases;
  • type-1 collagen;
  • zymography;
  • α2-macroglobulin;
  • TIMP-1 and -2