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.
Highlights
Extracellular Matrix Enzymes and Immune Cell BiologyFaculty of Health, School of Medicine, Deakin University, Geelong, VIC, Australia
The extracellular matrix (ECM) forms the structural architecture surrounding cells and plays a key role in supporting tissue integrity and cellular functions
Remodelling of the ECM by metalloproteinase enzymes has being increasingly linked to immunity, especially immune cell migration (Bradley et al, 2012; McMahon et al, 2016; Chen et al, 2018; Boyd et al, 2020)
Summary
Faculty of Health, School of Medicine, Deakin University, Geelong, VIC, Australia. 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. Specialty section: This article was submitted to Protein Chemistry and Enzymology, a section of the journal Frontiers in Molecular Biosciences
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