The structure, regulation, and function of human matrix metalloproteinase-13

M. F. Leeman, Stephanie Curran, Graeme Ian Murray

Research output: Contribution to journalEditorial

161 Citations (Scopus)

Abstract

Matrix metalloproteinase-13 (MMP-13) is a proteolytic enzyme that belongs to a large family of extracellular matrix-degrading endopeptidases that are characterized by a zinc-binding motif at their catalytic sites. MMP-13 has a key role in the MMP activation cascade and appears to be critical in bone metabolism and homeostasis. It also has an important role in tumor invasion and metastasis. This commentary provides a detailed overview of the regulatory mechanisms, structure, and function of human MMP-13 and highlights the key factors involved in the biology of this important molecule.

Original languageEnglish
Pages (from-to)149-166
Number of pages17
JournalCritical Reviews in Biochemistry and Molecular Biology
Volume37
Issue number3
DOIs
Publication statusPublished - 2002

Keywords

  • HUMAN OSTEOARTHRITIC CARTILAGE
  • HUMAN COLLAGENASE-3 MMP-13
  • SQUAMOUS-CELL CARCINOMAS
  • ACTIVATED PROTEIN-KINASE
  • FIBROBLAST-GROWTH-FACTOR
  • HEMOPEXIN-LIKE DOMAIN
  • N-TERMINAL KINASE
  • GENE-EXPRESSION
  • TUMOR INVASION
  • MESSENGER-RNA

Cite this

The structure, regulation, and function of human matrix metalloproteinase-13. / Leeman, M. F.; Curran, Stephanie; Murray, Graeme Ian.

In: Critical Reviews in Biochemistry and Molecular Biology, Vol. 37, No. 3, 2002, p. 149-166.

Research output: Contribution to journalEditorial

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KW - SQUAMOUS-CELL CARCINOMAS

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KW - FIBROBLAST-GROWTH-FACTOR

KW - HEMOPEXIN-LIKE DOMAIN

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