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Abstract:

Acute muscle damage, myonecrosis, is one of the main characteristics of envenoming by Bothrops genus. In this invitro study we investigated the role of a metalloproteinase (baltergin) and an acidic phospholipase A2 (Ba SPII RP4) in the cytotoxicity exhibited by Bothrops alternatus venom. Baltergin metalloproteinase purified from the venom exerted a toxic effect on C2C12 myoblast cells (CC50: 583.34μg/mL) which involved morphological alterations compatible with apoptosis/anoikis. On the contrary, the most abundant PLA2 isolated from this venom did not exhibit cytotoxicity at times and doses tested. However, when myoblasts were treated with both enzymes together, synergic activity was demonstrated. Neutralization of the venom with specific antibodies (IgG anti-baltergin and IgG anti-PLA2) confirmed this synergism. © 2011 Elsevier Ltd.

Registro:

Documento: Artículo
Título:Synergism between baltergin metalloproteinase and Ba SPII RP4 PLA2 from Bothrops alternatus venom on skeletal muscle (C2C12) cells
Autor:Bustillo, S.; Gay, C.C.; García Denegri, M.E.; Ponce-Soto, L.A.; Bal de Kier Joffé, E.; Acosta, O.; Leiva, L.C.
Filiación:Facultad de Ciencias Exactas y Naturales y Agrimensura, Universidad Nacional del Nordeste (UNNE), Av. Libertad 5470, CP 3400, Corrientes, Argentina
Facultad de Ciencias Veterinarias, Universidad Nacional del Nordeste (UNNE), Corrientes, Argentina
Area Investigación, Instituto de Oncología Angel H. Roffo, Buenos Aires, Argentina
Departamento de Bioquímica, Instituto de Biología, Universidade Estadual de Campinas, Campinas, SP, Brazil
Idioma: Inglés
Palabras clave:Baltergin; Bothrops alternatus; C2C12; Cytotoxicity; Metalloproteinase; Phospholipase A2; Synergism; acidic phospholipase A2; baltergin; metalloproteinase; phospholipase A2; snake venom; unclassified drug; animal cell; anoikis; apoptosis; article; bothrops alternatus; controlled study; cytotoxicity; enzyme isolation; in vitro study; mouse; myoblast; nonhuman; poisonous snake; priority journal; protein function; Animals; Antibodies, Monoclonal; Bothrops; Cell Line; Crotalid Venoms; Drug Synergism; Metalloproteases; Mice; Mice, Inbred C3H; Muscle, Skeletal; Muscular Diseases; Phospholipases A2; Rabbits; Bothrops; Bothrops alternatus
Año:2012
Volumen:59
Número:2
Página de inicio:338
Página de fin:343
DOI: http://dx.doi.org/10.1016/j.toxicon.2011.11.007
Título revista:Toxicon
Título revista abreviado:Toxicon
ISSN:00410101
CODEN:TOXIA
CAS:metalloproteinase, 81669-70-7; phospholipase A2, 9001-84-7; snake venom, 55230-69-8; Antibodies, Monoclonal; Crotalid Venoms; Metalloproteases, 3.4.-; Phospholipases A2, 3.1.1.4
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00410101_v59_n2_p338_Bustillo

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Citas:

---------- APA ----------
Bustillo, S., Gay, C.C., García Denegri, M.E., Ponce-Soto, L.A., Bal de Kier Joffé, E., Acosta, O. & Leiva, L.C. (2012) . Synergism between baltergin metalloproteinase and Ba SPII RP4 PLA2 from Bothrops alternatus venom on skeletal muscle (C2C12) cells. Toxicon, 59(2), 338-343.
http://dx.doi.org/10.1016/j.toxicon.2011.11.007
---------- CHICAGO ----------
Bustillo, S., Gay, C.C., García Denegri, M.E., Ponce-Soto, L.A., Bal de Kier Joffé, E., Acosta, O., et al. "Synergism between baltergin metalloproteinase and Ba SPII RP4 PLA2 from Bothrops alternatus venom on skeletal muscle (C2C12) cells" . Toxicon 59, no. 2 (2012) : 338-343.
http://dx.doi.org/10.1016/j.toxicon.2011.11.007
---------- MLA ----------
Bustillo, S., Gay, C.C., García Denegri, M.E., Ponce-Soto, L.A., Bal de Kier Joffé, E., Acosta, O., et al. "Synergism between baltergin metalloproteinase and Ba SPII RP4 PLA2 from Bothrops alternatus venom on skeletal muscle (C2C12) cells" . Toxicon, vol. 59, no. 2, 2012, pp. 338-343.
http://dx.doi.org/10.1016/j.toxicon.2011.11.007
---------- VANCOUVER ----------
Bustillo, S., Gay, C.C., García Denegri, M.E., Ponce-Soto, L.A., Bal de Kier Joffé, E., Acosta, O., et al. Synergism between baltergin metalloproteinase and Ba SPII RP4 PLA2 from Bothrops alternatus venom on skeletal muscle (C2C12) cells. Toxicon. 2012;59(2):338-343.
http://dx.doi.org/10.1016/j.toxicon.2011.11.007