Disease relevance of Bothrops

• The morphological effects of an aqueous solution of Nistatin, of Clostridium septicum and Tityus serrulatus toxins, of Bothrops jararaca and Agkistrodon piscivorus venoms on the vessels of the tendinous portion of the diaphragm were investigated in guinea-pigs [1].
• Thrombotic thrombocytopenia with severe depletion of plasma von Willebrand factor (vWF) was induced in normal large animals (5 dogs and 2 pigs) by botrocetin, a Bothrops factor requiring vWF for platelet agglutination [2].
• 3. Incubation of Bothrops jararaca plasma (BJP) with trypsin released a substance (or substances) that produced hypotension in the snake but not in the rat; this hypotensive effect was also potentiated by captopril [3].
• Inhibition of local hemorrhage and dermonecrosis induced by Bothrops asper snake venom: effectiveness of early in situ administration of the peptidomimetic metalloproteinase inhibitor batimastat and the chelating agent CaNa2EDTA [4].
• These results suggest that hyperalgesia induced by Bothrops asper venom is, at least partially, mediated by bradykinin, phospholipase A(2) activity and leukotrienes [5].

High impact information on Bothrops

• Cloning and sequence analysis of a Bothrops jararaca cDNA encoding a precursor of seven bradykinin-potentiating peptides and a C-type natriuretic peptide [6].
• Primary structure of two-chain botrocetin, a von Willebrand factor modulator purified from the venom of Bothrops jararaca [7].
• Alternagin-C (ALT-C), a disintegrin-like protein purified from the venom of the Brazilian snake Bothrops alternatus, interacts with the major collagen I receptor, the alpha(2)beta(1) integrin, inhibiting collagen binding [8].
• Complete amino acid sequence and identification of the platelet glycoprotein Ib-binding site of jararaca GPIb-BP, a snake venom protein isolated from Bothrops jararaca [9].
• We present here the entire 142- and 123-residue amino acid sequence of the respective alpha and beta subunits and also demonstrate that the platelet GPIb-binding site resides on the beta and not on the alpha subunit based on an enzyme-linked immunosorbent assay using biotin-labeled jararaca GPIb-BP and competing ligands [9].

Chemical compound and disease context of Bothrops

• In conclusion, the use of orally-administered chloramphenicol for victims of Bothrops snake bite with signs of local envenoming on admission, is not effective for the prevention of local infections [10].
• Hyperalgesia induced by Bothrops jararaca venom in rats: role of eicosanoids and platelet activating factor (PAF) [11].

Biological context of Bothrops

• A 1.8-kb cDNA clone was isolated from a Bothrops jararaca venom gland cDNA library that encodes a 256-aa precursor for bradykinin-potentiating peptides (angiotensin-converting enzyme inhibitors) and a C-type natriuretic peptide (CNP) [6].
• Blood coagulation induced by the venom of Bothrops atrox. 1. Identification, purification, and properties of a prothrombin activator [12].
• The serine peptidases, thrombocytin and PA-BJ, isolated from the venom of Bothrops atrox and Bothrops jararaca, respectively, induce platelet aggregation and granule secretion without clotting fibrinogen [13].
• No hydrolysis of thyrotropin-releasing factor or bradykinin potentiating nonapeptide from B. jararaca is observed [14].
• The region comprising amino acid residues 115-129 of myotoxin II, a Lys49 phospholipase A2 from the venom of Bothrops asper, was previously shown to constitute a heparin binding site, and to be associated with its toxic activities [15].

Anatomical context of Bothrops

• Bothropstoxin-I (BthTx-I) is a homodimeric Lys49-phospholipase A(2) isolated from Bothrops jararacussu venom which damages liposome membranes via a Ca(2+)-independent mechanism [16].
• Angiostatin-like peptides derived from human plasminogen digestion by jararhagin, a metalloproteinase isolated from B. jararaca venom, inhibited endothelial cell proliferation in vitro [17].
• Effect of heparin and antivenom on skeletal muscle damage produced by Bothrops jararacussu venom [18].
• Maurício Rocha e Silva is well known as the discoverer of bradykinin, the powerful hypotensive and smooth muscle stimulating polypeptide which was first detected in plasma following the addition of Bothrops jararaca venom [19].
• In addition, plaque forming cells making IgG1 subclass in BALB/cAn mitogen-stimulated spleens and in myelomas are preferentially killed by venom of pit viper Bothrops asper [20].

Associations of Bothrops with chemical compounds

• Heparin binds to phospholipase A2 myotoxins from Bothrops asper snake venom, inhibiting their toxic activities [21].
• Enzyme activity required the presence of chloride ions and was inhibited by EDTA and by low concentrations of Bothrops bradykinin-potentiating peptides [22].
• Neutralizing interaction between heparins and myotoxin II, a lysine 49 phospholipase A2 from Bothrops asper snake venom. Identification of a heparin-binding and cytolytic toxin region by the use of synthetic peptides and molecular modeling [21].
• The thrombin-like enzyme from Bothrops atrox snake venom. Properties of the enzyme purified by affinity chromatography on p-aminobenzamidine-substituted agarose [23].
• Inhibition of myotoxic activity of Bothrops asper myotoxin II by the anti-trypanosomal drug suramin [24].

Gene context of Bothrops

• Purification of botrocetin from Bothrops jararaca venom. Analysis of the botrocetin-mediated interaction between von Willebrand factor and the human platelet membrane glycoprotein Ib-IX complex [25].
• The deduced amino acid sequence of CAGLP displays high similarity with Bothrops insularis snake protein calglandulin (80%) [26].
• The results indicate the presence of an angiotensin receptor in the heart of B. jararaca snake pharmacologically distinct from angiotensin AT1 and AT2 receptors [27].
• Role of TNF-alpha, IL-1beta and IL-6 in the local tissue damage induced by Bothrops asper snake venom: an experimental assessment in mice [28].
• Both venoms induced an early increment in serum IL-10, whereas IFN-gamma levels reached higher values in mice injected with B. jararaca venom than in those receiving B. asper venom [29].

Analytical, diagnostic and therapeutic context of Bothrops

• Bitiscetin showed a heterodimeric structure composed of disulfide-linked alpha (16kDa) and beta (13kDa) subunits on SDS-PAGE and showed a basic nature with pI value of 9.1, in contrast to botrocetin (pI 4.6), a vWF modulator isolated from another snake (Bothrops jararaca) venom [30].
• Crystallization of bothrombin, a fibrinogen-converting serine protease isolated from the venom of Bothrops jararaca [31].
• The acidic phospholipase A2 from Bothrops lanceolatus venom has been purified by gel filtration on Sephadex G-50 and ion exchange chromatography on CM-cellulose [32].
• Several bradykinin potentiators were identified in the venom of Bothrops jararacussu by chromatographic techniques and biological assays [33].
• In addition, 4-nerolidylcatechol inhibited representatives of groups I and III of PLA(2)s. Its preincubation with Bothrops myotoxins significantly reduced their myotoxic and edema-inducing activities in animal experiments [34].

References