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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.
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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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
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Targeted therapy has developed significantly in the last one and half decades, prescribing specific medications for treatment of particular diseases, such as cancer, diabetes, and heart disease. One of the most exciting recent developments in targeted therapies was the isolation of disease-specific molecules from natural resources, such as animal venoms and plant metabolites/toxins, for use as templates for new drug motif designs. In addition, the study of venom proteins/peptides and toxins naturally targeted mammalian receptors and demonstrated high specificity and selectivity towards defined ion channels of cell membranes. Research has also focsed intensely on receptors. The focus of this Special Issue of Toxins addressed the most recent advances using animal venoms, such as frog secretions, bee/ant venoms and plant/fungi toxins, as medicinal therapy. Recent advances in venom/toxin/immunotoxins for targeted cancer therapy and immunotherapy, along with using novel disease-specific venom-based protein/peptide/toxin and currently available FDA-approved drugs for combinationtreatments will be discussed. Finally, we included an overview of select promising toad/snake venom-based peptides/toxins potentially able to address the forthcoming challenges in this field. Both research and review articles proposing novelties or overviews, respectively, were published in this Special Issue after rigorous evaluation and revision by expert peer reviewers.
cane toad --- n/a --- B cell non-Hodgkin lymphoma --- Malaysian cobras --- complement system --- decay accelerating factor --- neuroblastoma --- atopic dermatitis --- complement dependent cytotoxicity --- antioxidant enzymes --- bacterial adhesion --- cancer therapy --- N. kaouthia --- anuran skin secretion --- frog --- Apis mellifera syriaca --- solid phase extraction --- bee venom phospholipase A2 (bvPLA2) --- disintegrin --- toad toxins --- immunotoxins --- ribosome-inactivating proteins --- antimicrobial peptide (AMP) --- drug design --- Moxetumomab pasudotox --- snake venom --- antiviral activity --- in vitro effects --- bombesin-related peptide --- oxidative stress biomarkers --- half-life --- blood vessel formation --- target therapy --- 2 --- MYCN --- indolealkylamines --- Huachansu --- membrane attack complex --- bouganin --- bee venom --- SEM --- anticancer activity --- antimicrobial peptide --- house dust mite extract (DFE) --- mannose receptor --- O. hannah --- bicarinalin --- gastric cells --- melittin --- LC-ESI-MS --- dermaseptin --- smooth muscle --- apoptosis --- anticancer --- N. sumatrana --- Helicobacter pylori --- inflammation --- immunotherapy --- atopic dermatitis (AD) --- immunotoxin --- mantle cell lymphoma --- clearance --- mass spectrometry --- Bougainvillea --- rRNA N-glycosylase activity --- fungal toxin --- skin inflammation --- targeted therapy --- 4-dinitrochlorobenzene (DNCB) --- Bee venom --- VEGF --- Chansu --- bufadienolides --- obsessive–compulsive disorder (OCD) --- BLF1 --- antimicrobial activity --- orellanine --- VB6-845 --- acute lymphoblastic leukemia --- ribosome-inactivating protein --- CD206 --- molecular cloning --- cancer --- CD22 --- eIF4A --- obsessive-compulsive disorder (OCD)
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