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Review
. 2021 Aug 30:8:703868.
doi: 10.3389/fmolb.2021.703868. eCollection 2021.

Extracellular Matrix Enzymes and Immune Cell Biology

Meagan McMahon  1 , Siying Ye  1 , Jess Pedrina  1 , Daniel Dlugolenski  1 , John Stambas  1
Affiliations
Review

Extracellular Matrix Enzymes and Immune Cell Biology

Meagan McMahon et al. Front Mol Biosci. .

Abstract

Remodelling of the extracellular matrix (ECM) by ECM metalloproteinases is increasingly being associated with regulation of immune cell function. ECM metalloproteinases, including Matrix Metalloproteinases (MMPs), A Disintegrin and Metalloproteinases (ADAMs) and ADAMs with Thombospondin-1 motifs (ADAMTS) play a vital role in pathogen defence and have been shown to influence migration of immune cells. This review provides a current summary of the role of ECM enzymes in immune cell migration and function and discusses opportunities and limitations for development of diagnostic and therapeutic strategies targeting metalloproteinase expression and activity in the context of infectious disease.

Keywords: a disintegrin and metalloproteinases; a disintegrin and metalloproteinases with thombospondin-1 motifs; extracellular matrix; immunity; metalloproteinases.

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Conflict of interest statement

The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.

Figures

FIGURE 1
FIGURE 1
The metalloproteinase superfamily. The basic structural organisation of ADAMTS, ADAM and MMPs family members (including MMPs with a transmembrane domain, MT-MMP). Metalloproteinases generally contain similar proteinase domains. Differences in structure can be seen at the C-terminus or at the ancillary domain where ADAMTS enzymes contain Thrombospondin repeats; ADAMs are membrane-anchored through a transmembrane domain; and MMPs contain haemopexin-like regions.
See this image and copyright information in PMC

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