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Matrix Metalloproteinases: How Much Can They Do?

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  1. Effects of Ketone Bodies on Brain Metabolism and Function in Neurodegenerative Diseases

    Research output: Contribution to journalReviewResearchpeer-review

  2. Matrix Metalloproteinase-3 is Key Effector of TNF-α-Induced Collagen Degradation in Skin

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  1. The wound healing effect of local leukocyte platelet-rich plasma after total hip arthroplasty: A randomized controlled trial

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  2. Topical Zinc Oxide Assessed in Two Human Wound-healing Models

    Research output: Contribution to journalJournal articleResearchpeer-review

  3. Staphylococcus aureus Augments Release of Matrix Metalloproteinase-8 from Human Polymorpho-nuclear Leukocytes

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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.

Original languageEnglish
Article number2678
JournalInternational Journal of Molecular Sciences
Issue number8
Number of pages9
Publication statusPublished - 12 Apr 2020

    Research areas

  • ADAM Proteins/metabolism, Animals, Humans, Matrix Metalloproteinase Inhibitors/pharmacology, Matrix Metalloproteinases/metabolism, Neoplasms/drug therapy, Protein Domains, Thrombospondins/metabolism, Wound healing, Cytokines, Inflammation, Interstitial collagens, Extracellular matrix, Proteinases

ID: 61924295