Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
11029390 | The International Journal of Biochemistry & Cell Biology | 2018 | 52 Pages |
Abstract
Both mythologically and logically, snakes have always fascinated man. Snakes have attracted both awe and fear not only because of the elegant movement of their limbless bodies, but also because of the potency of their deadly venoms. Practically, in 2017, the world health organization (WHO) listed snake envenomation as a high priority neglected disease, as snakes inflict up to 2.7 million poisonous bites, around 100.000 casualties, and about three times as many invalidities on man. The venoms of poisonous snakes are a cocktail of potent compounds which specifically and avidly target numerous essential molecules with high efficacy. The individual effects of all venom toxins integrate into lethal dysfunctions of almost any organ system. It is this efficacy and specificity of each venom component, which after analysis of its structure and activity may serve as a potential lead structure for chemical imitation. Such toxin mimetics may help in influencing a specific body function pharmaceutically for the sake of man's health. In this review article, we will give some examples of snake venom components which have spurred the development of novel pharmaceutical compounds. Moreover, we will provide examples where such snake toxin-derived mimetics are in clinical use, trials, or consideration for further pharmaceutical exploitation, especially in the fields of hemostasis, thrombosis, coagulation, and metastasis. Thus, it becomes clear why a snake captured its symbolic place at the Asclepius rod with good reason still nowadays.
Keywords
DICvWFGPCRACEflavin adenine dinucleotidePLA2BPPNGFFDPSnake venom thrombin-like enzymeSVMPSnake venom serine proteinaseCLRPMMPSVSPECMG-protein coupled receptorl-amino acid oxidaseNOxROSADAMphospholipase A2Angiotensin-converting enzymedisseminated intravascular coagulationNADPH oxidaseFADCRISPParEMTSnake venomTissue factorVon Willebrand factorBasal membraneVascular endothelial growth factorVascular Endothelial Growth Factor (VEGF)nerve growth factorplasminogen activatorLAAOExtracellular matrixmatrixmetalloproteinaseMetastasisSnake venom metalloproteinasefibrin degradation productMimeticsHemostasisBradykinin-potentiating peptidePlateletCNG channelcyclic nucleotide-gated channelEpithelial-mesenchymal transitionGlycoproteinReactive oxygen speciesProteinase-activated receptor
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Authors
Maria-Inacia Estevão-Costa, Raquel Sanz-Soler, Benjamin Johanningmeier, Johannes A. Eble,