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

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

doi:10.1080/10409230290771483

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

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

Research output: Contribution to journal › Editorial

165 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 language	English
Pages (from-to)	149-166
Number of pages	17
Journal	Critical Reviews in Biochemistry and Molecular Biology
Volume	37
Issue number	3
DOIs	https://doi.org/10.1080/10409230290771483
Publication status	Published - 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

Leeman, M. F., Curran, S., & Murray, G. I. (2002). The structure, regulation, and function of human matrix metalloproteinase-13. Critical Reviews in Biochemistry and Molecular Biology, 37(3), 149-166. https://doi.org/10.1080/10409230290771483

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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.",

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AU - Leeman, M. F.

AU - Curran, Stephanie

AU - Murray, Graeme Ian

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AB - 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.

KW - HUMAN OSTEOARTHRITIC CARTILAGE

KW - HUMAN COLLAGENASE-3 MMP-13

KW - SQUAMOUS-CELL CARCINOMAS

KW - ACTIVATED PROTEIN-KINASE

KW - FIBROBLAST-GROWTH-FACTOR

KW - HEMOPEXIN-LIKE DOMAIN

KW - N-TERMINAL KINASE

KW - GENE-EXPRESSION

KW - TUMOR INVASION

KW - MESSENGER-RNA

U2 - 10.1080/10409230290771483

DO - 10.1080/10409230290771483

M3 - Editorial

VL - 37

SP - 149

EP - 166

JO - Critical Reviews in Biochemistry and Molecular Biology

JF - Critical Reviews in Biochemistry and Molecular Biology

SN - 1040-9238

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Access to Document

10.1080/10409230290771483