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 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 m...

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Publicado: 2012
Materias:
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
Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00410101_v59_n2_p338_Bustillo
http://hdl.handle.net/20.500.12110/paper_00410101_v59_n2_p338_Bustillo
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
id paper:paper_00410101_v59_n2_p338_Bustillo
record_format dspace
spelling paper:paper_00410101_v59_n2_p338_Bustillo2023-06-08T15:04:45Z Synergism between baltergin metalloproteinase and Ba SPII RP4 PLA2 from Bothrops alternatus venom on skeletal muscle (C2C12) cells 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 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. 2012 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00410101_v59_n2_p338_Bustillo http://hdl.handle.net/20.500.12110/paper_00410101_v59_n2_p338_Bustillo
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic 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
spellingShingle 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
Synergism between baltergin metalloproteinase and Ba SPII RP4 PLA2 from Bothrops alternatus venom on skeletal muscle (C2C12) cells
topic_facet 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
description 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.
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
publishDate 2012
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00410101_v59_n2_p338_Bustillo
http://hdl.handle.net/20.500.12110/paper_00410101_v59_n2_p338_Bustillo
_version_ 1768541837459456000

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