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Matrix Metalloproteinase

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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Salvato in:
Natura: Online
Lingua:inglese
Pubblicazione: MDPI - Multidisciplinary Digital Publishing Institute 2021
Soggetti:
hemagglutinin-B
transwell co-cultures
matrix metalloproteinases
TNF-α
matrix metalloproteinase
peritoneal mesothelial cell
gastric cancer
metastatic dissemination
MT4-MMP
cancer
diseases
aggrecan
aggrecanase
ADAMTS
cartilage
arthritis
MMP-2
MMP-9
inhibitor
allodynia
caspase-3
neuropathic
pain
dorsal root ganglion
spinal nerve ligation
tuberculosis
tuberculous meningitis
HIV-TB-associated IRIS
extracellular matrix breakdown
adult
pediatric
lung
central nervous system
matrix-metalloproteinase
monocytes
inflammation
phagocytosis
apoptosis
blood sampling
anticoagulants
high-molecular-weight heparin
IL-16
sICAM-1
IL-8
T cells
a disintegrin and metalloproteinase
EMMPRIN
CD147
ectodomain shedding
MMPs
PTMs
glycosylation
phosphorylation
glycosaminoglycans
interleukin
IL-6
IL-11
trans-signaling
metalloproteases
ADAM
MMP
meprin
matrix metalloproteinases (MMPs)
protease
signaling
invasion
chemokine
cytokine
proteomics
interferon
Agkistrodon venom
metalloproteinase
fibrinogen
antithrombotic
metabolomics
extracellular matrix
cytokines
proteinases
interstitial collagens
wound healing
thema EDItEUR::G Reference, Information and Interdisciplinary subjects::GP Research and information: general
thema EDItEUR::P Mathematics and Science::PS Biology, life sciences
Accesso online:ONIX_20210501_9783039366484_740
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Riassunto: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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