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Matrix Metalloproteinase 2 --- Matrix Metalloproteinase 9 --- Liver Diseases --- Liver Transplantation --- Tissue Inhibitor of Metalloproteinase-1 --- Tissue Inhibitor of Metalloproteinase-2 --- Reperfusion Injury --- Graft Rejection --- blood --- blood --- blood --- physiology --- blood --- blood --- enzymology --- enzymology

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Endometrium --- low Density Lipoprotein Receptor-Related Protein-2 --- Matrix Metalloproteinase 2

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Matrix metalloproteinases (MMPs) are members of an enzyme family and are critical for maintaining tissue allostasis. MMPs can catalyze normal turnover of the extracellular matrix (ECM) together with other metalloproteinases such as ADAM (a disintegrin and metalloproteinase) and ADAMTS (a disintegrin and metalloproteinase with thrombospondin motif) families. MMP activity is also regulated by a group of endogenous proteins called tissue inhibitor of metalloproteinases (TIMPs). All these proteins have a pivotal role involving ECM remodelling in normal physiological processes such as wound healing, embryogenesis, angiogenesis, bone remodelling, immunity, and the female reproductive cycle. An imbalance in the expression or activity of MMPs can also have important consequences in diseases such as cancer, cardiovascular disease, peripheral vascular disease, chronic leg ulcers, and multiple sclerosis. In recent years, MMPs have been found to play an important role in the field of precision medicine, as they may serve as biomarkers that may predict an individual’s disease predisposition, state, or progression. MMPs are also thought to be a sensible target for molecular therapy. The aim of this Special Issue is to explore the most recent findings in this field that may have an impact in healthcare systems.

hypersensitivity pneumonitis --- metalloproteinases --- genetic association --- autoantibodies --- MMP1 --- MMP2 --- SNPs --- MMPs --- TIMPs --- CKD --- peripheral vascular disease --- biomarkers --- proteinuria --- eGFR --- PAD. --- NGAL --- statins --- arterial aneurysms --- patients --- collagenases --- Crohn’s disease --- dental caries --- mouth --- periodontitis --- matrix metalloproteinase-9 --- dialysis --- on-line hemodiafiltration --- high-flux dialysis --- renal replacement therapy --- kidney transplantation --- Mac-1 --- CD147 --- leukocytes --- platelets --- adhesion --- integrin αMβ2 --- matrix metalloproteinases --- TIMP --- synthetic inhibitors --- RECK --- matrix metalloproteinase --- MAPKs --- ischemia/reperfusion --- eNOS --- iNOS --- inflammatory bowel disease --- inflammation --- NO --- MMP-9 --- cGMP --- Caco-2 --- matrix metalloproteinase-7 --- fibrosis --- acute kidney injury --- chronic kidney disease --- apoptosis --- health --- disease

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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.

Research & information: general --- Biology, life sciences --- 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 --- 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

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In the two last decades, proteases have constituted one of the primary and important targets in drug discovery. The U.S. FDA has approved more than 12 protease therapies in the last 10 years, and a number of next-generation or completely new proteases are under clinical development. Protease inhibition strategies are one of the fastest expanding areas in the field of of drugs that show considerable promise. This Special Issue will focus on the recent advances in the discovery and development of protease inhibitors, covering the synthesis of protease inhibitors, the design of new chemical entities acting as inhibitors of special/particular types of proteases, and their mode of actions (Frolova et al. 2020; Slapak et al. 2020; Künnapuu et al. 2021). In addition, the new applications of these interesting compounds/biomolecules and their limitations have been discussed and described (Wang et al. 2020; Bartošová-Sojková et al. 2021).

Research & information: general --- MMP --- MMP2 --- MMP9 --- MMP7 --- MMP14 --- matrix metalloproteases --- PDAC --- pancreatic cancer --- Bowman–Birk inhibitor --- ranacyclin --- trypsin inhibitor --- structure–activity relationship --- synergistic effect --- Gentamicin --- matrix metalloproteinase --- extracellular matrix --- nuclei --- cancer --- apoptosis --- immune response --- cysteine protease inhibitor --- stefin --- signal peptide --- parasite --- phylogenetic analysis --- diversification --- protein structure --- vascular endothelial growth factors (VEGFs) --- VEGF-A --- PlGF --- VEGF-B --- VEGF-C --- VEGF-D --- angiogenesis --- lymphangiogenesis --- CCBE1 --- proteases --- ADAMTS3 --- plasmin --- cathepsin D --- KLK3 --- prostate-specific antigen (PSA) --- thrombin --- wound healing --- metastasis --- proteolytic activation --- vascular biology --- lymphedema --- MMP --- MMP2 --- MMP9 --- MMP7 --- MMP14 --- matrix metalloproteases --- PDAC --- pancreatic cancer --- Bowman–Birk inhibitor --- ranacyclin --- trypsin inhibitor --- structure–activity relationship --- synergistic effect --- Gentamicin --- matrix metalloproteinase --- extracellular matrix --- nuclei --- cancer --- apoptosis --- immune response --- cysteine protease inhibitor --- stefin --- signal peptide --- parasite --- phylogenetic analysis --- diversification --- protein structure --- vascular endothelial growth factors (VEGFs) --- VEGF-A --- PlGF --- VEGF-B --- VEGF-C --- VEGF-D --- angiogenesis --- lymphangiogenesis --- CCBE1 --- proteases --- ADAMTS3 --- plasmin --- cathepsin D --- KLK3 --- prostate-specific antigen (PSA) --- thrombin --- wound healing --- metastasis --- proteolytic activation --- vascular biology --- lymphedema