Relating matrix metalloproteinase structure to function: Why the “hemopexin” domain?

doi:10.1016/S0945-053X(97)90025-1

Matrix Biology

Volume 15, Issues 8–9, March 1997, Pages 511-518

https://doi.org/10.1016/S0945-053X(97)90025-1 Get rights and content

Abstract

Matrix metalloproteinases are thought to be key players in the remodelling activity of cells associated with both physiological and pathological processes. They share a relatively conserved structure with a number of identifiable modules linked to their specific functions. The structure of the individual domains of a number of matrix metalloproteinases have now ben elucidated. Here we review these data in the light of complementary studies on the behaviour of these enzymes in biological systems. In particular we focus on the C-terminal hemopexin-like domains which was intriguingly specific roles in individual matrix metalloproteinases.

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Citation Excerpt :
Twenty five members of the MMP family have been identified in humans. On the basis of substrate specificity and homology, MMPs can be divided into six groups: collagenases, gelatinases, stromelysins, matrilysins, membrane-type MMPs (MT-MMPs), and other MMPs (Murphy & Knäuper, 1997; Murphy & Nagase, 2008; Visse & Nagase, 2003). MMPs contribute to various physiological processes, e.g. embryonic development, tissue turnover, and wound healing, as well as to pathological processes, e.g. cancer, cardiovascular diseases, arthritis, periodontitis, and fibrosis (Hadler-Olsen, Winberg, & Uhlin-Hansen, 2013; Agewall, 2006; Malemud, 2006; Sorsa, Tjäderhane, & Salo, 2004).
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There is a growing evidence that matrix metalloproteinase (MMP)-2 and MMP-9 (gelatinases) play an important role in the pathogenesis of numerous disorders, especially with inflammatory etiology and extracellular matrix (ECM) remodeling. Despite the fact that gelatinases involve in liver cirrhosis is provided in the literature, their role in the pathogenesis of chronic pancreatitis and non-specific inflammatory bowel diseases is still under investigation.
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^a: Dr. Gillian Murphy, Department of Cell and Molecular Biology, Strangeways Research Laboratory, Worts' Causeway, Cambridge, CB1 4RN, United Kingdom.

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MinireviewRelating matrix metalloproteinase structure to function: Why the “hemopexin” domain?

Abstract

J. Biol. Chem.

Curr. Opin. Cell Biol.

Structure

FEBS Lett.

Kidney Inst.

FEBS Lett.

J. Biol. Chem.

J. Mol. Biol.

J. Biol. Chem.

J. Biol. Chem.

J. Biol. Chem.

Structure

Methods Enzymol.

J. Biol. Chem.

J. Biol. Chem.

J. Biol. Chem.

FEBS Lett.

J. Biol. Chem.

J. Biol. Chem.

J. Biol. Chem.

J. Biol. Chem.

Regulation of development and differentiation by the extracellular matrix

Development

Binding of latent high Mr active forms of stromelysin to collagen is mediated by the C-terminal domain

J. Cell Sci.

The gelatin-binding site of human 72 kDa type IV collagenase (gelatinase A)

Biochem. J.

Storemelysin-1: Three-dimensional structure of the inhibited catalytic domain and of the C-truncated proenzyme

Protein. Sci.

Minireview
Relating matrix metalloproteinase structure to function: Why the “hemopexin” domain?