Reprint
Matrix Metalloproteinase
Edited by
August 2020
262 pages
- ISBN978-3-03936-648-4 (Hardback)
- ISBN978-3-03936-649-1 (PDF)
This is a Reprint of the Special Issue Matrix Metalloproteinase that was published in
Biology & Life Sciences
Chemistry & Materials Science
Medicine & Pharmacology
Summary
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.