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Journal articles on the topic 'Toxine alpha de scorpion'

Author: Grafiati

Published: 4 June 2021

Last updated: 17 February 2022

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1

Strichartz, G. R., and G. K. Wang. "Rapid voltage-dependent dissociation of scorpion alpha-toxins coupled to Na channel inactivation in amphibian myelinated nerves." Journal of General Physiology 88, no. 3 (1986): 413–35. http://dx.doi.org/10.1085/jgp.88.3.413.

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The voltage-dependent action of several scorpion alpha-toxins on Na channels was studied in toad myelinated nerve under voltage clamp. These toxins slow the declining phase of macroscopic Na current, apparently by inhibiting an irreversible channel inactivation step and thus permitting channels to reopen from a closed state in depolarized membranes. In this article, we describe the rapid reversal of alpha-toxin action by membrane depolarizations more positive than +20 mV, an effect not achieved by extensive washing. Depolarizations that were increasingly positive and of longer duration caused

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2

GREEN, Daniel, Suzi PACE, Suzanne M. CURTIS, et al. "The three-dimensional structural surface of two beta-sheet scorpion toxins mimics that of an alpha-helical dihydropyridine receptor segment." Biochemical Journal 370, no. 2 (2003): 517–27. http://dx.doi.org/10.1042/bj20021488.

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An α-helical II—III loop segment of the dihydropyridine receptor activates the ryanodine receptor calcium-release channel. We describe a novel manipulation in which this agonist's activity is increased by modifying its surface structure to resemble that of a toxin molecule. In a unique system, native β-sheet scorpion toxins have been reported to activate skeletal muscle ryanodine receptor calcium channels with high affinity by binding to the same site as the lower-affinity α-helical dihydropyridine receptor segment. We increased the alignment of basic residues in the α-helical peptide to mimic

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3

Kirsch, G. E., A. Skattebøl, L. D. Possani, and A. M. Brown. "Modification of Na channel gating by an alpha scorpion toxin from Tityus serrulatus." Journal of General Physiology 93, no. 1 (1989): 67–83. http://dx.doi.org/10.1085/jgp.93.1.67.

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The effects of TsIV-5, a toxin isolated from the Brazilian scorpion Tityus serrulatus, on whole-cell and single-channel Na currents were determined in N18 neuroblastoma cells. In whole-cell records at a test potential of -10 mV, external application of 500 nM TsIV-5 slowed inactivation 20-fold and increased peak current by about one-third without changing time-to-peak. Both the steady-state activation and inactivation curves were shifted to more negative potentials. Other alpha scorpion toxins produce similar effects but the single-channel mechanism is not known. TsIV-5 caused a voltage-depend

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4

Wang, G. K., and G. Strichartz. "Kinetic analysis of the action of Leiurus scorpion alpha-toxin on ionic currents in myelinated nerve." Journal of General Physiology 86, no. 5 (1985): 739–62. http://dx.doi.org/10.1085/jgp.86.5.739.

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The effects of a neurotoxin, purified from the venom of the scorpion Leiurus quinquestriatus, on the ionic currents of toad single myelinated fibers were studied under voltage-clamp conditions. Unlike previous investigations using crude scorpion venom, purified Leiurus toxin II alpha at high concentrations (200-400 nM) did not affect the K currents, nor did it reduce the peak Na current in the early stages of treatment. The activation of the Na channel was unaffected by the toxin, the activation time course remained unchanged, and the peak Na current vs. voltage relationship was not altered. I

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5

Delabre, M. L., P. Pasero, M. Marilley, and P. E. Bougis. "Promoter structure and intron-exon organization of a scorpion .alpha.-toxin gene." Biochemistry 34, no. 20 (1995): 6729–36. http://dx.doi.org/10.1021/bi00020a018.

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6

Stankiewicz, Maria, Françoise Grolleau, Hervé Rochat, Eliahu Zlotkin, Marcel Pelhate, and Bruno Lapied. "Insect background sodium channel as a new target for scorpion alpha toxin." Pesticide Science 55, no. 10 (1999): 1021–26. http://dx.doi.org/10.1002/(sici)1096-9063(199910)55:10<1021::aid-ps58>3.0.co;2-8.

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7

Bouhaouala-Zahar, B., R. Ben Khalifa, I. Zanouaki, et al. "Immunochemical and electrophysiological properties of a novel recombinant scorpion alpha insect toxin." Toxicon 34, no. 10 (1996): 1084. http://dx.doi.org/10.1016/0041-0101(96)83804-9.

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8

Bouhaouala-Zahar, Balkiss, Frederique Ducancel, Ilham Zenouaki, et al. "A Recombinant Insect-Specific alpha-Toxin of Buthus occitanus tunetanus Scorpion Confers Protection Against Homologous Mammal Toxins." European Journal of Biochemistry 238, no. 3 (1996): 653–60. http://dx.doi.org/10.1111/j.1432-1033.1996.0653w.x.

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9

Hahin, Richard, Ziyi Chen, Danhui Wang, Giridher Reddy, and Long Mao. "Scorpion Toxins from Buthus martensii Karsch All Possess a Predicted alpha-Tight-Turn." Cell Biochemistry and Biophysics 37, no. 3 (2002): 169–86. http://dx.doi.org/10.1385/cbb:37:3:169.

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10

Tejedor, F. J., and W. A. Catterall. "Site of covalent attachment of alpha-scorpion toxin derivatives in domain I of the sodium channel alpha subunit." Proceedings of the National Academy of Sciences 85, no. 22 (1988): 8742–46. http://dx.doi.org/10.1073/pnas.85.22.8742.

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11

Martin-Eauclaire, M. F., M. Alami, A. Giamarchi, V. Missimilli, J. P. Rosso, and P. E. Bougis. "A natural anatoxin, Amm VIII, induces neutralizing antibodies against the potent scorpion alpha-toxins." Vaccine 24, no. 12 (2006): 1990–96. http://dx.doi.org/10.1016/j.vaccine.2005.11.016.

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12

KHARRAT, Riadh, Herve DARBON, Herve ROCHAT, and Claude GRANIER. "Structure/activity relationships of scorpion alpha-toxins. Multiple residues contribute to the interaction with receptors." European Journal of Biochemistry 181, no. 2 (1989): 381–90. http://dx.doi.org/10.1111/j.1432-1033.1989.tb14735.x.

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13

KHARRAT, Riadh, Herve DARBON, Herve ROCHAT, and Claude GRANIER. "Structure/activity relationships of scorpion alpha-toxins. Multiple residues contribute to the interaction with receptors." European Journal of Biochemistry 181, no. 2 (1989): 388–90. http://dx.doi.org/10.1111/j.1432-1033.1989.tb14736.x.

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14

Kuldyushev, Nikita A., Antonina A. Berkut, Steve Peigneur, Jan Tytgat, Eugene V. Grishin, and Alexander A. Vassilevski. "Design of sodium channel ligands with defined selectivity - a case study in scorpion alpha-toxins." FEBS Letters 591, no. 20 (2017): 3414–20. http://dx.doi.org/10.1002/1873-3468.12839.

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15

Gordon, D., M. F. Martin-Eauclaire, S. Cestele, Ch Kopeyan, E. Zoltkin, and H. Rochat. "Alpha scorpion toxins as tools for the study of homologous receptor sites in neuronal sodium channels." Toxicon 33, no. 3 (1995): 268. http://dx.doi.org/10.1016/0041-0101(95)99263-3.

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16

AYEB, Mohamed EL, Herve DARBON, El Mostafa BAHRAOUI, Orietta VARGAS, and Herve ROCHAT. "Differential effects of defined chemical modifications on antigenic and pharmacological activities of scorpion alpha and beta toxins." European Journal of Biochemistry 155, no. 2 (1986): 289–94. http://dx.doi.org/10.1111/j.1432-1033.1986.tb09488.x.

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17

Thomsen, W. J., and W. A. Catterall. "Localization of the receptor site for alpha-scorpion toxins by antibody mapping: implications for sodium channel topology." Proceedings of the National Academy of Sciences 86, no. 24 (1989): 10161–65. http://dx.doi.org/10.1073/pnas.86.24.10161.

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18

Paillart, C., J. L. Boudier, J. A. Boudier, H. Rochat, F. Couraud, and B. Dargent. "Activity-induced internalization and rapid degradation of sodium channels in cultured fetal neurons." Journal of Cell Biology 134, no. 2 (1996): 499–509. http://dx.doi.org/10.1083/jcb.134.2.499.

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A regulatory mechanism for neuronal excitability consists in controlling sodium channel density at the plasma membrane. In cultured fetal neurons, activation of sodium channels by neurotoxins, e.g., veratridine and alpha-scorpion toxin (alpha-ScTx) that enhance the channel open state probability induced a rapid down-regulation of surface channels. Evidence that the initial step of activity-induced sodium channel down-regulation is mediated by internalization was provided by using 125I-alpha-ScTx as both a channel probe and activator. After its binding to surface channels, the distribution of 1

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19

Kem, W. R., V. M. Mahnir, and M. W. Pennington. "Type 2 sea anemone toxins compete with type 1 sea anemone and scorpion alpha-toxins for binding to nerve sodium channels." Toxicon 33, no. 3 (1995): 268–69. http://dx.doi.org/10.1016/0041-0101(95)99265-5.

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20

Cestele, S., R. B. Khalifa, M. Pelhate, H. Rochat, and D. Gordon. "Alpha scorpion toxins binding on rat brain and insect sodium channels reveal divergent allosteric modulations by brevetoxin and veratridine." Toxicon 34, no. 3 (1996): 303–4. http://dx.doi.org/10.1016/0041-0101(96)80911-1.

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21

Griene, L., P. Mansuelle, R. Oughideni, M. Pelhate, F. Sampieri, and C. Kopeyan. "Characterization of a new anti-insect toxin of alpha type isolated from the venom of the scorpion Buthacus arenicola." Toxicon 35, no. 12 (1997): 1665. http://dx.doi.org/10.1016/s0041-0101(97)90097-0.

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22

Wang, Jinti, Vladimir Yarov-Yarovoy, Roy Kahn, et al. "Molecular Determinants for Alpha-Scorpion Toxin Binding to the Resting State of a Voltage Sensor of Brain Sodium Channels." Biophysical Journal 100, no. 3 (2011): 422a. http://dx.doi.org/10.1016/j.bpj.2010.12.2498.

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23

Gurevitz, M., D. Urbach, E. Zlotkin, and N. Zilberberg. "Nucleotide sequence and structure analysis of a cDNA encoding an alpha insect toxin from the scorpion Leiurus quinquestriatus hebraeus." Toxicon 29, no. 10 (1991): 1270–72. http://dx.doi.org/10.1016/0041-0101(91)90200-b.

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24

Massensini, André R., Tasso Moraes-Santos, Marcus V. Gomez, and Marco A. Romano-Silva. "Alpha- and beta-scorpion toxins evoke glutamate release from rat cortical synaptosomes with different effects on [Na+]i and [Ca2+]i." Neuropharmacology 37, no. 3 (1998): 289–97. http://dx.doi.org/10.1016/s0028-3908(98)00025-2.

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25

Bayatzadeh, Mohammad Ali, Abbas Zare Mirakabadi, Nahid Babaei, Abdolhassan Doulah, and Abbas Doosti. "Expression and purification of recombinant alpha-toxin AnCra1 from the scorpion Androctonus crassicauda and its functional characterization on mammalian sodium channels." Molecular Biology Reports 48, no. 9 (2021): 6303–12. http://dx.doi.org/10.1007/s11033-021-06624-2.

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26

Grolleau, F., M. Stankiewicz, L. Birinyi-Strachan, et al. "Electrophysiological analysis of the neurotoxic action of a funnel-web spider toxin, delta-atracotoxin-HV1a, on insect voltage-gated Na+ channels." Journal of Experimental Biology 204, no. 4 (2001): 711–21. http://dx.doi.org/10.1242/jeb.204.4.711.

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The effects of delta-ACTX-Hv1a, purified from the venom of the funnel-web spider Hadronyche versuta, were studied on the isolated giant axon and dorsal unpaired median (DUM) neurones of the cockroach Periplaneta americana under current- and voltage-clamp conditions using the double oil-gap technique for single axons and the patch-clamp technique for neurones. In parallel, the effects of the toxin were investigated on the excitability of rat dorsal root ganglion (DRG) neurones. In both DRG and DUM neurones, delta-ACTX-Hv1a induced spontaneous repetitive firing accompanied by plateau potentials.

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27

Devaux, Christiane, Besma Jouirou, Mohamed Naceur Krifi, Olivier Clot-Faybesse, Mohamed El Ayeb, and Hervé Rochat. "Quantitative variability in the biodistribution and in toxinokinetic studies of the three main alpha toxins from the Androctonus australis hector scorpion venom." Toxicon 43, no. 6 (2004): 661–69. http://dx.doi.org/10.1016/j.toxicon.2004.02.021.

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28

Legros, Christian, Brigitte Céard, Hélène Vacher, Pascale Marchot, Pierre E. Bougis, and Marie-France Martin-Eauclaire. "Expression of the standard scorpion alpha-toxin AaH II and AaH II mutants leading to the identification of some key bioactive elements." Biochimica et Biophysica Acta (BBA) - General Subjects 1723, no. 1-3 (2005): 91–99. http://dx.doi.org/10.1016/j.bbagen.2005.01.008.

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29

Brône, B., J. Tytgat, D. C. Wang, and E. Van Kerkhove. "Characterization of Na+ currents in isolated dorsal unpaired median neurons of Locusta migratoria and effect of the alpha-like scorpion toxin BmK M1." Journal of Insect Physiology 49, no. 2 (2003): 171–82. http://dx.doi.org/10.1016/s0022-1910(02)00263-9.

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30

El Ayeb, Mohamed, El Mostafa Bahraoui, Claude Granier, and Herve Rochat. "Use of antibodies specific to defined regions of scorpion .alpha.-toxin to study its interaction with its receptor site on the sodium channel." Biochemistry 25, no. 21 (1986): 6671–78. http://dx.doi.org/10.1021/bi00369a052.

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31

Boudier, JL, T. Le Treut, and E. Jover. "Autoradiographic localization of voltage-dependent sodium channels on the mouse neuromuscular junction using 125I-alpha scorpion toxin. II. Sodium distribution on postsynaptic membranes." Journal of Neuroscience 12, no. 2 (1992): 454–66. http://dx.doi.org/10.1523/jneurosci.12-02-00454.1992.

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32

Benkhadir, Khadija, Riadh Kharrat, Sandrine Cestèle, et al. "Molecular cloning and functional expression of the alpha-scorpion toxin BotIII: pivotal role of the C-terminal region for its interaction with voltage-dependent sodium channels." Peptides 25, no. 2 (2004): 151–61. http://dx.doi.org/10.1016/j.peptides.2004.01.009.

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33

del Rio-Portilla, Federico, Elizabeth Hernandez-Marin, Genaro Pimienta, et al. "NMR solution structure of Cn12, a novel peptide from the Mexican scorpion Centruroides noxius with a typical beta-toxin sequence but with alpha-like physiological activity." European Journal of Biochemistry 271, no. 12 (2004): 2504–16. http://dx.doi.org/10.1111/j.1432-1033.2004.04181.x.

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34

Boudier, JL, E. Jover, and P. Cau. "Autoradiographic localization of voltage-dependent sodium channels on the mouse neuromuscular junction using 125I-alpha scorpion toxin. I. Preferential labeling of glial cells on the presynaptic side." Journal of Neuroscience 8, no. 5 (1988): 1469–78. http://dx.doi.org/10.1523/jneurosci.08-05-01469.1988.

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35

Sabatier, J. M., H. Zerrouk, H. Darbon, et al. "P05, a new leiurotoxin I-like scorpion toxin: Synthesis and structure-activity relationships of the .alpha.-amidated analog, a ligand of calcium-activated potassium channels with increased affinity." Biochemistry 32, no. 11 (1993): 2763–70. http://dx.doi.org/10.1021/bi00062a005.

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36

Gonoi, T., and B. Hille. "Gating of Na channels. Inactivation modifiers discriminate among models." Journal of General Physiology 89, no. 2 (1987): 253–74. http://dx.doi.org/10.1085/jgp.89.2.253.

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Macroscopic Na currents were recorded from N18 neuroblastoma cells by the whole-cell voltage-clamp technique. Inactivation of the Na currents was removed by intracellular application of proteolytic enzymes, trypsin, alpha-chymotrypsin, papain, or ficin, or bath application of N-bromoacetamide. Unlike what has been reported in squid giant axons and frog skeletal muscle fibers, these treatments often increased Na currents at all test pulse potentials. In addition, removal of inactivation gating shifted the midpoint of the peak Na conductance-voltage curve in the negative direction by 26 mV on av

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37

Loret, Erwann P., Marie France Martin-Eauclaire, Pascal Mansuelle, Francois Sampieri, Claude Granier, and Herve Rochat. "An anti-insect toxin purified from the scorpion Androctonus australis Hector also acts on the .alpha.- and .beta.-sites of the mammalian sodium channel: sequence and circular dichroism study." Biochemistry 30, no. 3 (1991): 633–40. http://dx.doi.org/10.1021/bi00217a007.

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38

Wang, G. K., and S. Y. Wang. "Inactivation of batrachotoxin-modified Na+ channels in GH3 cells. Characterization and pharmacological modification." Journal of General Physiology 99, no. 1 (1992): 1–20. http://dx.doi.org/10.1085/jgp.99.1.1.

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Batrachotoxin (BTX)-modified Na+ currents were characterized in GH3 cells with a reversed Na+ gradient under whole-cell voltage clamp conditions. BTX shifts the threshold of Na+ channel activation by approximately 40 mV in the hyperpolarizing direction and nearly eliminates the declining phase of Na+ currents at all voltages, suggesting that Na+ channel inactivation is removed. Paradoxically, the steady-state inactivation (h infinity) of BTX-modified Na+ channels as determined by a two-pulse protocol shows that inactivation is still present and occurs maximally near -70 mV. About 45% of BTX-mo

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39

Lakhkar, Bhavana Bhushan, M. M. Patil, and S. V. Patil. "Scorpion Sting Envenomation." Journal of Nepal Paediatric Society 36, no. 3 (2017): 284–87. http://dx.doi.org/10.3126/jnps.v36i3.14875.

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Scorpion sting envenomation is very common problem in rural India especially where the climate is hot and dry. Management techniques have improved tremendously over the time leading to reduced morbidity and mortality. Mortality is mainly when ignorant patients go to the traditional faith healers (Tantrics) and come late to the facility where better management is available. Indian red scorpion (Mesobhuthustamulus) is the main species in India. Autonomic storm caused by venom acting on sodium gated and other channels is the main cause of manifestations in a scorpion sting victim. Cardio-myopathy

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40

Peker, Erdal, Suleyman Oktar, Murat Dogan, Ergun Kaya, and Mehmet Duru. "Prazosin treatment in the management of scorpion envenomation." Human & Experimental Toxicology 29, no. 3 (2010): 231–33. http://dx.doi.org/10.1177/0960327109359639.

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Scorpion stings represent an important and serious public health problem worldwide due to their high incidence and potentially severe and often fatal clinical manifestations. Children are at greater risk of developing severe cardiac, respiratory, and neurological complications due to lesser body surface area. Alpha receptor stimulation plays important role in the pathogenesis of pulmonary edema. Prazosin, a post synaptic alpha blocker, can be recommended as an effective drug in the treatment of serious scorpion envenomations with significant sympathetic symptoms. Oral prazosin is fast acting,

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41

Sigrist, N. E., and K. N. Adamik. "Alpha-Chloralose-Intoxikation bei zwei Chihuahuas." Tierärztliche Praxis Ausgabe K: Kleintiere / Heimtiere 37, no. 02 (2009): 102–6. http://dx.doi.org/10.1055/s-0038-1622778.

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Zusammenfassung Gegenstand und Ziel: Darstellung einer Vergiftung mit Alpha-Chloralose anhand von zwei Fällen sowie Zusammenstellung der diesbezüglichen Literatur. Patienten: Zwei Chihuahua-Hündinnen (3- bzw. 12-jährig) wurden nach Aufnahme von mit Alpha-Chloralose präparierten Fleischwürstchen vorgestellt. Ergebnisse: Beide Tiere zeigten Hypoventilation und neurologische Symptome, wobei sich eine Hündin mit Koma und Hypothermie präsentierte, die andere mit Koma, Krämpfen und normaler Temperatur. Initial stand die Aufrechterhaltung und Überwachung der Vitalfunktionen sowie die Dekontamination

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42

Zilberberg, Noam, Dalia Gordon, Marcel Pelhate, et al. "Functional Expression and Genetic Alteration of an Alpha Scorpion Neurotoxin†." Biochemistry 35, no. 31 (1996): 10215–22. http://dx.doi.org/10.1021/bi9528309.

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43

Monastyrnaya M.M., Kalina R. S. "Neuro- and Cardiotoxins from Sea Anemones: Structure, Function and Potential of Application in Research and Medical Practice." Journal of NBC Protection Corps 3, no. 2 (2019): 117–36. http://dx.doi.org/10.35825/2587-5728-2019-3-2-117-136.

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Sea anemones are well-spread everywhere in the World Ocean and represent the most ancient active poisonous organisms. Their main instrument of attack on other animals are the nematocysts – stinging organelles with the curtailed hollow thread with poisonous edge on the end. In order to attract their potential victims, they use fluorescent proteins. These proteins became a separate object of research as genetically coded markers for the observation of activity of promotors of genes. The poisonous secret of sea anemones is characterized by the presence of maximum number of peptides of various str

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44

Sifi, Amina, Sonia Adi-Bessalem, and Fatima Laraba-Djebari. "Involvement of the Endothelin Receptor Type A in the Cardiovascular Inflammatory Response Following Scorpion Envenomation." Toxins 12, no. 6 (2020): 389. http://dx.doi.org/10.3390/toxins12060389.

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Elevated levels of endothelin-1 (ET-1) were recorded in sera of scorpion sting patients. However, no studies focused on the mechanism of ET-1 involvement in the pathogenesis of scorpion envenomation, particularly in the cardiovascular system which is seriously affected in severe cases of scorpion stings. Inflammation induced by Androctonus australis hector (Aah) scorpion venom in the heart together with the aorta was studied in mice pretreated with a specific endothelin A receptor (ETA-R) inhibitor. ETA-R inhibition resulted in the attenuation of the high amounts of cytokine (tumor necrosis fa

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45

Romero-Imbachi, Margarita Rosa, Nelson Cupitra, Karen Ángel, et al. "Centruroides margaritatus scorpion complete venom exerts cardiovascular effects through alpha-1 adrenergic receptors." Comparative Biochemistry and Physiology Part C: Toxicology & Pharmacology 240 (February 2021): 108939. http://dx.doi.org/10.1016/j.cbpc.2020.108939.

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46

Ait-Lounis, Aouatef, and Fatima Laraba-Djebari. "TNF-alpha modulates adipose macrophage polarization to M1 phenotype in response to scorpion venom." Inflammation Research 64, no. 11 (2015): 929–36. http://dx.doi.org/10.1007/s00011-015-0876-z.

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47

Chejanovsky, Nor, Noam Zilberberg, Hadasah Rivkin, Eliahu Zlotkin, and Michael Gurevitz. "Functional expression of an alpha anti-insect scorpion neurotoxin in insect cells and lepidopterous larvae." FEBS Letters 376, no. 3 (1995): 181–84. http://dx.doi.org/10.1016/0014-5793(95)01263-4.

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48

Chejanovsky, N., N. Zilberberg, H. Rivkin, E. Zlotkin, and M. Gurevitz. "Baculovirus-directed expression of an alpha anti-insect neuroloxin derived from the Israeli yellow scorpion." Toxicon 33, no. 3 (1995): 270. http://dx.doi.org/10.1016/0041-0101(95)99268-8.

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49

Nakib, Imene, Marie-France Martin-Eauclaire, and Fatima Laraba-Djebari. "Involvement of Cholinergic and Adrenergic Receptors in Pathogenesis and Inflammatory Response Induced by Alpha-Neurotoxin Bot III of Scorpion Venom." Inflammation 39, no. 5 (2016): 1670–80. http://dx.doi.org/10.1007/s10753-016-0401-8.

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50

Chen, Tianbao, Ronan Folan, HangFai Kwok, Edmund J. O'Kane, Anthony J. Bjourson, and Chris Shaw. "Isolation of scorpion (Androctonus amoreuxi) putative alpha neurotoxins and parallel cloning of their respective cDNAs from a single sample of venom." Regulatory Peptides 115, no. 2 (2003): 115–21. http://dx.doi.org/10.1016/s0167-0115(03)00146-0.

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