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Journal articles on the topic 'Bolesatine'

Author: Grafiati
Published: 4 June 2021
Last updated: 6 February 2022

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1

Gachet, C., R. Ennamany, O. Kretz, et al. "Bolesatine induces agglutination of rat platelets and human erythrocytes and platelets in vitro." Human & Experimental Toxicology 15, no. 1 (1996): 26–29. http://dx.doi.org/10.1177/096032719601500105.

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Bolesatine is a toxic glycoprotein isolated from the mushroom Boletus satanas Lenz, which has been shown to inhibit protein synthesis in cell-free systems and cell culture. It is toxic to rodents, the LD50% 24 h being 1 mg kg-1 (i.p.) and 0.15 mg kg-1 (i.v) in the rat in which it induces hepatic blood stasis. Bolesatine possesses lectinic properties with in parti cular a sugar binding site for D-galactose and mitogenic activity toward lymphocytes. Tested for cell agglutination on red blood cells and platelets, bolesatine agglutinates both human and rat platelets from threshold concentrations o
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2

Ennamany, R., A. Bingen, E. E. Creppy, et al. "Aspirin® and heparin prevent hepatic blood stasis and thrombosis induced by the toxic glycoprotein Bolesatine in mice." Human & Experimental Toxicology 17, no. 11 (1998): 620–24. http://dx.doi.org/10.1177/096032719801701106.

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Bolesatine is a toxic glycoprotein isolated from Boletus satanas Lenz, which inhibits protein synthesis in vivo and in vitro. The LD50 (24 h) is 1 mg /kg bw (i.p.), in mice and rats. When given i.p. to mice (0.1 - 1.0 mg/kg bw) bolesatine induced thrombi and blood stasis in the liver, 5 - 21 h after injection, and modifications of the number of blood corpuscles in peripheral blood. These effects were efficiently reversed by aspirin, ticlopidin and heparin (as attested by histology and electron microscopy) which however failed to prevent death in animals given lethal doses. Together, these resu
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3

Patočka, Jiří. "BOLESATINE, A TOXIC PROTEIN FROM THE MUSHROOM RUBROBOLETUS SATANAS." Military Medical Science Letters 87, no. 1 (2018): 14–20. http://dx.doi.org/10.31482/mmsl.2018.003.

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4

Kretz, O., E. E. Creppy, and G. Dirheimer. "Disposition of the toxic protein, bolesatine, in rats: Its resistance to proteolytic enzymes." Xenobiotica 21, no. 1 (1991): 65–73. http://dx.doi.org/10.3109/00498259109039451.

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5

Ennamay, R. "Mode of Action of Bolesatine, a Glycoprotein from Boletus Satanas Lenz, Mechanistic Approaches." Toxicology Letters 78 (August 1995): 31–32. http://dx.doi.org/10.1016/03784-2749(59)4724u-.

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6

Ennamany, R., O. Kretz, A. Badoc, G. Deffieux, and E. E. Creppy. "Effect of bolesatine, a glycoprotein from Boletus satanas, on rat thymus in vivo." Toxicology 89, no. 2 (1994): 113–18. http://dx.doi.org/10.1016/0300-483x(94)90219-4.

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7

Basset, L., R. Ennamany, J. P. Portail, et al. "Effects of bolesatine on a cell line from the SP2/O thymic lymphosarcoma." Toxicology 103, no. 2 (1995): 121–25. http://dx.doi.org/10.1016/0300-483x(95)03113-t.

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8

Ennamany, R., J. P. Lavergne, J. P. Reboud, G. Dirheimer, and E. E. Creppy. "Mode of action of bolesatine, a cytotoxic glycoprotein from Boletus satanas Lenz. Mechanistic approaches." Toxicology 100, no. 1-3 (1995): 51–55. http://dx.doi.org/10.1016/0300-483x(95)03058-n.

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9

Licastro, Frederico, Maria Cristina Morini, Olivier Kretz, Guy Dirheimer, Edmond Ekue Creppy, and Fiorenzo Stirpe. "Mitogenic activity and immunological properties of bolesatine, a lectin isolated from the mushroom Boletus satanas Lenz." International Journal of Biochemistry 25, no. 5 (1993): 789–92. http://dx.doi.org/10.1016/0020-711x(93)90366-m.

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10

Ennamany, R., O. Kretz, and E. E. Creppy. "Effect of bolesatine on phospholipid/calcium dependent protein kinase in vero cells and in rat thymus." Archives of Toxicology 69, no. 9 (1995): 624–30. http://dx.doi.org/10.1007/s002040050223.

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11

Kretz, O., E. E. Creppy, and G. Dirheimer. "Characterization of bolesatine, a toxic protein from the mushroom Boletus satanas Lenz and it's effects on kidney cells." Toxicology 66, no. 2 (1991): 213–24. http://dx.doi.org/10.1016/0300-483x(91)90220-u.

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12

Ennamany, R., A. Bingen, E. E. Creppy, et al. "Aspirin® and heparin prevent hepatic blood stasis and thrombosis induced by the toxic glycoprotein Bolesatine in mice." Human & Experimental Toxicology 17, no. 11 (1998): 620–24. http://dx.doi.org/10.1191/096032798678908017.

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13

Kretz, Olivier, Joseph Reinbolt, Edmond-Ekue Creppy, and Guy Dirheimer. "Properties of bolesatine, a translational inhibitor from Boletus satanas Lenz. Amino-terminal sequence determination and inhibition of rat mitochondrial protein synthesis." Toxicology Letters 64-65 (December 1992): 763–66. http://dx.doi.org/10.1016/0378-4274(92)90259-m.

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14

Ennamany, R., S. Marzetto, D. Saboureau, and E. E. Creppy. "Lipid peroxidation induced by bolesatine, a toxin ofBoletus satanas: Implication in m5dC variation in Vero cells related to inhibition of cell growth." Cell Biology and Toxicology 11, no. 6 (1995): 347–54. http://dx.doi.org/10.1007/bf01305906.

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15

Kretz, O., L. Barbieri, E. E. Creppy, and G. Dirheimer. "Inhibition of protein synthesis in liver and kidney of mice by bolesatine: mechanistic approaches to the mode of action at the molecular level." Toxicology 73, no. 3 (1992): 297–304. http://dx.doi.org/10.1016/0300-483x(92)90071-l.

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