Disease relevance of Viperidae

• The lethal toxicity of Crotalus durissus terrificus (Crotalinae, Viperidae) can be attributed mainly to the presence of a neurotoxic protein, crotoxin, which also shows phospholipase A2 activity [1].
• Cerastes cerastes venom in low concentrations (0.8-2.5 micrograms/ml) inhibited the response of the rat vas deferens to field stimulation, while higher concentrations (4-8 micrograms/ml) causes a contracture that was reversed by washing and transiently blocked by phentolamine [2].

Psychiatry related information on Viperidae

• Annual cycle of plasma testosterone in male copperheads, Agkistrodon contortrix (Serpentes, Viperidae): relationship to timing of spermatogenesis, mating, and agonistic behavior [3].

High impact information on Viperidae

• We have purified bitiscetin from Bitis arietans venom and investigated the mechanism whereby it promotes a form of vWF that is reactive with platelets [4].
• The disintegrin-like domains of these toxins differ from the disintegrin peptides found in crotalid and viperid venoms by the nature of their different disulfide bond structure and, in lieu of the disintegrins' signature Arg-Gly-Asp (RGD) integrin binding sequence, there is an XXCD disulfide-bonded cysteinyl sequence in that region [5].
• Characterization and platelet inhibitory activity of bitistatin, a potent arginine-glycine-aspartic acid-containing peptide from the venom of the viper Bitis arietans [6].
• The digestion and absorption of collagen, native and artificially cross-linked, has been examined in the rat and the Gaboon viper, by feeding known quantities and measuring the hydroxy-proline content of the faeces and of the contents of the gut at different levels, and comparing with an unabsorbable marker (polyethylene glycol) [7].
• In contrast to the basal recruitment of the galactose-binding lectins, the C-type lectins were shown to be Viperidae only, with the alpha-chains and beta-chains resulting from an early duplication event [8].

Biological context of Viperidae

• Bitiscetin, a C-type lectin-like protein isolated from the venom of the snake Bitis arientans, promotes the interactions between plasma von Willebrand factor (VWF) and platelet membrane glycoprotein Ib (GPIb) to induce platelet aggregation [9].
• Comparison of the ACLPREMT1 cDNA sequence with PLA2 cDNAs from Viperidae snakes shows that it has a similar organization: highly conserved 5' and 3' untranslated regions, a sequence encoding a 16-amino acid signal peptide, and the mature protein coding region [10].
• Nucleotide sequences of mitochondrial cytochrome b and 16S rRNA genes, totaling 946 bp, were used to reconstruct a molecular phylogeny of 42 species of the subfamily Viperinae representing 12 of the 13 recognized genera [11].
• Since in all Viperidae PLA2 multigene families the 5' and 3' flanking regions are highly conserved, we designed oligonucleotide primers that allow amplification of the whole PLA2 multigene family in a single step [12].
• The influence of body condition on 17-beta estradiol levels in relation to vitellogenesis in female Vipera aspis (Reptilia, Viperidae) [13].

Anatomical context of Viperidae

• Afaâcytin, an alpha beta-fibrinogenase from Cerastes cerastes (horned viper) venom, activates purified factor X and induces serotonin release from human blood platelets [14].
• In vitro assays performed with Torpedo synaptosomes showed a protective action of CICS against Viperidae beta-neurotoxins but not against other PLA2 neurotoxins, on primary and evoked liberation of acetylcholine [15].

Associations of Viperidae with chemical compounds

• The ANP/BNP natriuretic toxins are likely to be basal, whereas the CNP/BPP toxins are Viperidae only [8].
• The venoms of Viperidae snakes contain numerous serine proteinases that have been recognized to possess one or more of the essential activities of thrombin on fibrinogen and platelets [16].
• A comparison of the sequences of these crotalid neurotoxins revealed some common features of the possible neurotoxic sites, including residues 6, 11, 76-81 and 119-125 [17].
• In several myotoxins from the venoms of Viperidae snakes, this aspartic acid is substituted by lysine [18].
• The sequence is highly similar to those of high-molecular mass snake venom metalloproteinases from viperid and crotalid venoms comprised of metalloproteinase, disintegrin-like, and Cys-rich domains [19].

Gene context of Viperidae

• Crotalid venom vascular endothelial growth factors has preferential affinity for VEGFR-1. Characterization of Protobothrops mucrosquamatus venom VEGF [20].
• Structural comparison among VEGF-proteins from various viper venoms revealed that the two subfamilies of vipers (Crotalinae and Viperinae) have evolved with distinct receptor-specificities for VEGFR-1 and VEGFR-2, respectively [20].
• Bitiscetin, a platelet adhesion inducer isolated from venom of the snake Bitis arietans, activates the binding of the von Willebrand factor (VWF) A1 domain to glycoprotein Ib (GPIb) in vitro [21].
• The homology with other crotalid PLA2 cited in the literature varied from 60% to 90% [22].
• Kallikrein-like proteinase from bushmaster snake venom [23].

Analytical, diagnostic and therapeutic context of Viperidae

• Molecular cloning and expression of a functional snake venom serine proteinase, with platelet aggregating activity, from the Cerastes cerastes viper [16].
• Sandwich-type enzyme linked immunosorbent assays (ELISA) were developed to detect Lachesis muta muta (bushmaster) snake venom using antibodies against the plasminogen activator enzyme (LV-PA) [24].
• Each macroglobulin was characterized for proteinase inhibiting activity, molecular weight by polyacrylamide gel electrophoresis (PAGE), subunit size by sodium dodecyl sulfate (SDS)-PAGE, immunological cross-reactivity to other macroglobulins and antihemorrhagic activity against European viper (Vipera berus) venom [25].
• We report the cloning and sequence analysis of Cerastes vipera and Macrovipera lebetina transmediterranea cDNAs coding for short non-RGD (Arg-Gly-Asp) disintegrins and for dimeric disintegrin subunits [26].

References