Disease relevance of Crotalus

• Two peptic fragments (residues 37-88 and 43-88) of guinea pig myelin basic protein which are capable of inducing experimental allergic encephalomyelitis in Lewis rats were cleaved to shorter fragments with alpha-protease (Crotalus atrox proteinase, EC 3.4.24.1) and thermolysin (EC 3.4.24.4) [1].
• One peptide was derived from a phage display library, the other from the integrin-binding moiety of the toxin from the American pit viper, Crotalus molossus molossus [2].
• Pseudomonas exotoxin A, ricin, tumor necrosis factor alpha (TNF-alpha), diphtheria toxin (DT), Crotalus durissus terrificus toxin, crotalus adamenteus toxin, Naja naja toxin, and Naja mocambique toxin were evaluated [3].
• The substrate analog, N alpha-dansyl-N omega-(1,N6-etheno-ADP-ribosyl)arginine methyl ester, was used to assay the catalytic activities of dinitrogenase reductase activating glycohydrolase from Rhodospirillum rubrum and nucleotide pyrophosphatase from Crotalus adamanteus [4].
• The role of peripheral potassium channels on the antinociceptive effect of Crotalus durissus terrificus venom, a mixed delta- and kappa-opioid receptor agonist, was investigated in hyperalgesia induced by carrageenin or prostaglandin E(2) [5].

High impact information on Crotalus

• Cloning and sequencing shows that the primary structure of the human s-PLA2 has about 37% homology with that of bovine pancreatic PLA2 and 44% homology with that of Crotalus atrox PLA2 [6].
• Here we investigated involvement of the Src family in the proximal signals through the GPVI-FcRgamma complex, using the snake venom convulxin from Crotalus durissus terrificus, which specifically recognizes GPVI and activates platelets through cross-linking GPVI [7].
• The N-terminal sequence revealed significant homology to pig pancreatic kallikrein and to kallikrein like enzymes from Crotalus atrox and Crotalus adamanteus venom [8].
• Adamalysin II, a 24 kDa zinc endopeptidase from the snake venom of Crotalus adamanteus, is a member of a large family of metalloproteinases isolated as small proteinases or proteolytic domains of mosaic haemorrhagic proteins from various snake venoms [9].
• The reconstitutable apoprotein of Crotalus adamanteus L-amino acid oxidase was prepared using hydrophobic interaction chromatography [10].

Chemical compound and disease context of Crotalus

• The second neurotoxic effects is myokymia, a type of fasciculation most frequently reported after bites by Crotalus horridus horridus (timber rattlesnake) and Crotalus atrox (Western diamondback rattlesnake) [11].
• In addition, inhibitory zones of Staphylococcus aureus in an agar diffusion test showed that PLA(2) from Crotalus atrox venom was able to catalyze the release of gentamicin from PEG-liposomes [12].
• Studies were conducted to see whether exogenous phospholipase C from Clostridium perfringens, phospholipase A2 from Crotalus adamanteus venom, arachidonic acid and 1-oleoyl-2-acetyl-sn-glycerol (OAG) mimic the anti-ketogenic action of vasopressin in isolated rat hepatocytes [13].

Biological context of Crotalus

• In this investigation we have expressed in insect cells the disintegrin-like/cysteine-rich (DC) domains of the Crotalus atrox hemorrhagic metalloproteinase atrolysin A and demonstrated that the recombinant protein (A/DC) can inhibit collagen- and ADP-stimulated platelet aggregation [14].
• Platelet activation and signal transduction by convulxin, a C-type lectin from Crotalus durissus terrificus (tropical rattlesnake) venom via the p62/GPVI collagen receptor [15].
• LPE-induced hydrolysis of PE was found to depend on contamination of the LPE by PLA2 from Crotalus atrox, employed in the commercial synthesis of the lysophosphatide from the precursor used, phosphatidylethanolamine [16].
• In previous reports, we described the purification and cDNA cloning from Crotalus atrox of a vascular apoptosis-inducing protein (VAP1) that specifically induces apoptosis in vascular endothelial cells [17].
• Arterial infusion of norepinephrine increased arterial pressure by more than 100% and reduced blood volumes 8.6 and 17.0% in Elaphe and Crotalus, respectively [18].

Anatomical context of Crotalus

• RESULTS: Of the phospholipase A2 toxins, Crotalus durissus terrificus and Naja mocambique are active against the PSA secreting LNCaP cell line; however, the effect is reversible, and no other hormone refractory prostate cell line tested is sensitive [3].
• The inhibitory effect of the plant flavonoid, rutin, on group I phospholipase A2 (PLA2-I) from porcine pancreas and Naja naja, and on group II phospholipase A2 (PLA2-II) from Vipera russelli and Crotalus atrox was investigated [19].
• Glycerol monoethers in the scent gland secretions of the western diamondback rattlesnake (Crotalus atrox; Serpentes, Crotalinae) [20].
• The molecular mechanism of Ca(2+) release by myotoxin a (MTYX), a polypeptide toxin isolated from the venom of prairie rattlesnakes (Crotalus viridis viridis), was investigated in the heavy fraction of sarcoplasmic reticulum (HSR) of rabbit skeletal muscles [21].
• Immunochemical detection of purified crotoxin from Crotalus durissus terrificus venom in the motor end plate of striated muscle in CBA/J mice [22].

Associations of Crotalus with chemical compounds

• Antithrombotic effect of crotalin, a platelet membrane glycoprotein Ib antagonist from venom of Crotalus atrox [23].
• The DNA from FUra-treated S-49 cells was purified by cesium chloride gradient centrifugation and degraded to nucleosides by DNase I and Crotalus atrox snake venom [24].
• Human fibrinogen exposed to protease III from Crotalus atrox venom is cleaved near the NH2 terminus of the B beta chain yielding a species of Mr 325,000 (Fg325) with impaired thrombin clottability [25].
• Complete primary structure of a galactose-specific lectin from the venom of the rattlesnake Crotalus atrox. Homologies with Ca2(+)-dependent-type lectins [26].
• L-Methionine sulfoximine is a substrate of L-amino acid oxidase (Crotalus adamanteus), glutamine transaminase, and gamma-cystathionase [27].

Gene context of Crotalus

• Exogenous Naja naja group I PLA2 had little effect on the mineralization of bone nodules; however, Crotalus adamanteus group II PLA2 inhibited mineralization at concentrations similar to those found in the media from IL-1 alpha-treated cultures [28].
• Convulxin (CVX), a C-type snake protein from Crotalus durissus terrificus venom, is the quintessential agonist for studies of the collagen receptor, glycoprotein VI (GPVI) and its role in platelet adhesion to collagens [29].
• These results suggested the presence of (6-4) photolyase in cultured goldfish cells as in Drosophila, Xenopus and Crotalus [30].
• Sequence studies on the NH2-terminal region of the protein indicate that LV-Ka shares a high degree of sequence homology with the kallikrein-like enzymes EI and EII from Crotalus atrox, with crotalase from Crotalus adamanteus and significant homology with other serine proteinases from snake venoms and vertebrate serum enzymes [31].
• Kallikrein-like enzyme from Crotalus ruber ruber (red rattlesnake) venom [32].

Analytical, diagnostic and therapeutic context of Crotalus

• We have used alkyl ether analogs of ethanolamine and choline phospholipids as ligands to purify phospholipase A2 (EC 3.1.1.4) from Crotalus adamanteus venom by affinity chromatography [33].
• Toxins from the venoms of Crotalus durissus terrificus, Crotalus s. scutulatus and Crotalus viridis concolor were compared using gel filtration, ion-exchange chromatography on DEAE-Sephacel and denaturing and non-denaturing polyacrylamide gel electrophoresis [34].
• The venom of Crotalus durissus terrificus was fractionated by reverse-phase HPLC to obtain crotapotins (F5 and F7) and PLA2 (F15, F16, and F17) of high purity [35].
• A study was made on the venom of a single specimen of the rattlesnake Crotalus molossus molossus, utilizing isoelectric focusing in polyacrylamide gels, to determine what effects various commonly employed preparative procedures might have on the chemical properties of the venom [36].
• Venoms from Bothrops asper, B. godmani, B. lateralis, B. nasutus, B. ophryomegas, B. schlegelii, B. nummifer, B. picadoi, Crotalus durissus durissus and Lachesis muta stenophrys were separated by SDS-PAGE, transferred to cellulose nitrate membrane and reacted against five different antivenoms [37].

References