Synergism between baltergin metalloproteinase and Ba SPII RP4 PLA2 from Bothrops alternatus venom on skeletal muscle (C2C12) cells

Acute muscle damage, myonecrosis, is one of the main characteristics of envenoming by Bothrops genus. In this in vitro 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...

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Autores principales: Bustillo, Soledad, Gay, Claudia C., García Denegri, María Emilia, Ponce-Soto, Luis Alberto, Bal de Kier Joffé, Elisa, Acosta, Ofelia Cristina, Leiva, Laura Cristina Ana
Formato: Artículo
Lenguaje:Inglés
Publicado: Elsevier 2025
Materias:
Bothrops alternatus
Cytotoxicity
Phospholipase A2
Metalloproteinase
Baltergin
C2C12
Synergism
Acceso en línea:http://repositorio.unne.edu.ar/handle/123456789/59352
Aporte de:
RIUNNE - Repositorio Institucional de la Universidad Nacional del Nordeste (UNNE) de Universidad Nacional del Nordeste
id I48-R184-123456789-59352
record_format dspace
spelling I48-R184-123456789-593522025-12-15T12:01:35Z Synergism between baltergin metalloproteinase and Ba SPII RP4 PLA2 from Bothrops alternatus venom on skeletal muscle (C2C12) cells Bustillo, Soledad Gay, Claudia C. García Denegri, María Emilia Ponce-Soto, Luis Alberto Bal de Kier Joffé, Elisa Acosta, Ofelia Cristina Leiva, Laura Cristina Ana Bothrops alternatus Cytotoxicity Phospholipase A2 Metalloproteinase Baltergin C2C12 Synergism Acute muscle damage, myonecrosis, is one of the main characteristics of envenoming by Bothrops genus. In this in vitro 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: 583.34 mg/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. 2025-12-15T11:31:17Z 2025-12-15T11:31:17Z 2012-02 Artículo Bustillo, Soledad, et al., 2012. Synergism between baltergin metalloproteinase and Ba SPII RP4 PLA2 from Bothrops alternatus venom on skeletal muscle (C2C12) cells. Toxicon. Oxford: Elsevier, vol. 59, p. 338–343. ISSN 1879-3150 0041-0101 http://repositorio.unne.edu.ar/handle/123456789/59352 eng https://doi.org/10.1016/j.toxicon.2011.11.007 openAccess http://creativecommons.org/licenses/by-nc-nd/2.5/ar/ application/pdf p. 338-343 application/pdf Elsevier Toxicon, 2012, vol. 59, p. 338–343.
institution Universidad Nacional del Nordeste
institution_str I-48
repository_str R-184
collection RIUNNE - Repositorio Institucional de la Universidad Nacional del Nordeste (UNNE)
language Inglés
topic Bothrops alternatus
Cytotoxicity
Phospholipase A2
Metalloproteinase
Baltergin
C2C12
Synergism
spellingShingle Bothrops alternatus
Cytotoxicity
Phospholipase A2
Metalloproteinase
Baltergin
C2C12
Synergism
Bustillo, Soledad
Gay, Claudia C.
García Denegri, María Emilia
Ponce-Soto, Luis Alberto
Bal de Kier Joffé, Elisa
Acosta, Ofelia Cristina
Leiva, Laura Cristina Ana
Synergism between baltergin metalloproteinase and Ba SPII RP4 PLA2 from Bothrops alternatus venom on skeletal muscle (C2C12) cells
topic_facet Bothrops alternatus
Cytotoxicity
Phospholipase A2
Metalloproteinase
Baltergin
C2C12
Synergism
description Acute muscle damage, myonecrosis, is one of the main characteristics of envenoming by Bothrops genus. In this in vitro 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: 583.34 mg/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.
format Artículo
author Bustillo, Soledad
Gay, Claudia C.
García Denegri, María Emilia
Ponce-Soto, Luis Alberto
Bal de Kier Joffé, Elisa
Acosta, Ofelia Cristina
Leiva, Laura Cristina Ana
author_facet Bustillo, Soledad
Gay, Claudia C.
García Denegri, María Emilia
Ponce-Soto, Luis Alberto
Bal de Kier Joffé, Elisa
Acosta, Ofelia Cristina
Leiva, Laura Cristina Ana
author_sort Bustillo, Soledad
title Synergism between baltergin metalloproteinase and Ba SPII RP4 PLA2 from Bothrops alternatus venom on skeletal muscle (C2C12) cells
title_short Synergism between baltergin metalloproteinase and Ba SPII RP4 PLA2 from Bothrops alternatus venom on skeletal muscle (C2C12) cells
title_full Synergism between baltergin metalloproteinase and Ba SPII RP4 PLA2 from Bothrops alternatus venom on skeletal muscle (C2C12) cells
title_fullStr Synergism between baltergin metalloproteinase and Ba SPII RP4 PLA2 from Bothrops alternatus venom on skeletal muscle (C2C12) cells
title_full_unstemmed Synergism between baltergin metalloproteinase and Ba SPII RP4 PLA2 from Bothrops alternatus venom on skeletal muscle (C2C12) cells
title_sort synergism between baltergin metalloproteinase and ba spii rp4 pla2 from bothrops alternatus venom on skeletal muscle (c2c12) cells
publisher Elsevier
publishDate 2025
url http://repositorio.unne.edu.ar/handle/123456789/59352
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