Structural and functional comparison of proteolytic enzymes from plant latex and snake venoms

Abstract

This work describes classification, functions, location, inhibition, activation, and therapeutic applications of proteases from snake venoms and vegetables. Snake venoms and vegetables can present toxins that unchain necrosis or proteolysis due to the direct cytotoxic action of venom proteases. These proteases are potential tools in the development of drugs for the prevention and treatment of several illnesses. We report herein mainly fibrinogenolytic metallo proteases and serine proteases ("thrombin-like"). These enzymes are extensively used in the treatment and prevention of thrombotic disorders, since they serve as defibrinogenating agents. The therapeutic uses of fibrin(ogen)olytic metallo proteases hold promise for clinical application due to potential in reversing the effects of thrombosis; this has been shown to be an alternative approach to the prevention and treatment of cardiovascular disorders, which are among the most prominent causes of mortality around the world. Plant proteases can be utilized for many cellular and molecular activities, in antibacterial and anticancer therapies, and in the treatment of snakebites, inhibiting snake venom activities such as blood-clotting, defibrinogenation, and fibrin(ogen)olytic and hemorrhagic actions. These toxins also display potential for clinical use in the treatment of hemostatic disorders.

Rapid Purification of a New P-I Class Metalloproteinase fromBothrops moojeniVenom with Antiplatelet Activity

“…BmooMP α -II fibrinogenolytic activity was completely inhibited by metal-chelating agents EDTA and 1,10-phenanthroline (Figure 3(b)), which remove metallic cofactors that are necessary for enzymatic catalysis [39]. These results, in addition to the sequence from the N-terminal and the molecular mass, corroborate the suggestion that this enzyme belongs to class P-I of the SVMPs.…”

Edema Induced by a Crotalus durissus terrificus Venom Serine Protease (Cdtsp 2) Involves the PAR Pathway and PKC and PLC Activation

“…In addition, these trypsin-like serine proteases induced moderate edema, as also observed with Cdtsp 2. However, remarkable volumes of edema were only observed in concentrations higher than 5 μg per animal (5 mg/mL) of Cdtsp 2, which is less intense than volumes of edema promoted by Cdt sPLA2 [29]. Cdtsp 2 induces substantial plasma coagulation, and mice passed away when more than 20 μg per animal (20 mg/mL) of Cdtsp 2 was used.…”

“…The COX-2 enzyme catalyzes the conversion of AA into various prostaglandins, such as PGE2, which are associated with an increase in the synthesis of proinflammatory cytokines, tumor necrosis factor alpha (TNF-α), and interleukin 1 beta (IL-1β). Furthermore, these mediators are formed following the hydrolytic action of PLA2 on cell membrane phospholipids, resulting in the release of AA, as well as the production of other metabolites such as 8-isoprostanes, which can undergo nonenzymatic peroxidation via intermediate reactive oxygen species [14,18,29,30,31,32,33,34,35]. …”

Purification and Characterization of BmooAi: A New Toxin fromBothrops moojeniSnake Venom That Inhibits Platelet Aggregation

“…Among the complex pool of proteins (more than 90% of the dry weight) are included enzymes such as acetylcholinesterases, aminotransferases, phosphoesterases, ADPases, phospholipases, hyaluronidases, L-amino acid oxidases (LAAOs), and proteases (metalloproteinases and serinoproteases) [1–5]. Protein C activators, growth factors (NGF, VEGF), lectins, precursors of bioactive peptides, von Willebrand factor binding proteins, disintegrins, and bradykinin potentiators are some representatives of nonenzymatic components from snake venom [2, 6].…”