Matrix Metalloproteinase

• Autore: Ågren Magnus S
• Pubblicazione: Basel, Switzerland, : MDPI - Multidisciplinary Digital Publishing Institute, 2020
• Descrizione fisica: 1 online resource (262 p.)
• Soggetto topico: Biology, life sciences; Research & information: general
• Soggetto non controllato: a disintegrin and metalloproteinase; ADAM; ADAMTS; adult; aggrecan; aggrecanase; Agkistrodon venom; allodynia; anticoagulants; antithrombotic; apoptosis; arthritis; blood sampling; cancer; cartilage; caspase-3; CD147; central nervous system; chemokine; cytokine; cytokines; diseases; dorsal root ganglion; ectodomain shedding; EMMPRIN; extracellular matrix; extracellular matrix breakdown; fibrinogen; gastric cancer; glycosaminoglycans; glycosylation; hemagglutinin-B; high-molecular-weight heparin; HIV-TB-associated IRIS; IL-11; IL-16; IL-6; IL-8; inflammation; inhibitor; interferon; interleukin; interstitial collagens; invasion; lung; matrix metalloproteinase; matrix metalloproteinases; matrix metalloproteinases (MMPs); matrix-metalloproteinase; meprin; metabolomics; metalloproteases; metalloproteinase; metastatic dissemination; MMP; MMP-2; MMP-9; MMPs; monocytes; MT4-MMP; neuropathic; pain; pediatric; peritoneal mesothelial cell; phagocytosis; phosphorylation; protease; proteinases; proteomics; PTMs; sICAM-1; signaling; spinal nerve ligation; T cells; TNF-α; trans-signaling; transwell co-cultures; tuberculosis; tuberculous meningitis; wound healing
• Persona (resp. second.): KellerUlrich; ÅgrenMagnus S
• Sommario/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.
• Titolo autorizzato: Matrix Metalloproteinase
• Formato: Materiale a stampa
• Livello bibliografico: Monografia
• Lingua di pubblicazione: Inglese
• Record Nr.: 9910557717203321
• Lo trovi qui: Univ. Federico II