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Journal article

Matrix Metalloproteinases: How Much Can They Do?

From

University of Copenhagen1

Department of Biotechnology and Biomedicine, Technical University of Denmark2

Protease Network Degradomics, Section for Protein Science and Biotherapeutics, Department of Biotechnology and Biomedicine, Technical University of Denmark3

Zinc-dependent matrix metalloproteinases (MMPs) belong to metzincins that comprise not only 23 human MMPs but also other metalloproteinases, such as 21 human ADAMs (a disintegrin and metalloproteinase domain) and 19 secreted ADAMTSs (a disintegrin and metalloproteinase thrombospondin domain). The many setbacks from the clinical trials of broad-spectrum MMP inhibitors for cancer indications in the late 1990s emphasized the extreme complexity of the participation of these proteolytic enzymes in biology.

This editorial mini-review summarizes the Special Issue, which includes four review articles and 10 original articles that highlight the versatile roles of MMPs, ADAMs, and ADAMTSs, in normal physiology as well as in neoplastic and destructive processes in tissue. In addition, we briefly discuss the unambiguous involvement of MMPs in wound healing.

Language: English
Publisher: MDPI AG
Year: 2020
Pages: 2678
ISSN: 14220067 and 16616596
Types: Journal article
DOI: 10.3390/ijms21082678
ORCIDs: 0000-0002-2263-0826 and auf dem Keller, Ulrich

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