Matrix Metalloproteinases: How Much Can They Do?

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 ma...

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Detalles Bibliográficos
Autores principales: Ågren, Magnus S., auf dem Keller, Ulrich
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Editorial
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7215854/
https://www.ncbi.nlm.nih.gov/pubmed/32290531
http://dx.doi.org/10.3390/ijms21082678
Descripción
Sumario: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.

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