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| Silva,Cássio Prinholato da; Costa,Tássia R.; Paiva,Raquel M. Alves; Cintra,Adélia C. O.; Menaldo,Danilo L.; Antunes,Lusânia M. Greggi; Sampaio,Suely V.. |
| Abstract Background Phospholipases A 2 (PLA 2 s) are abundant components of snake venoms that have been extensively studied due to their pharmacological and pathophysiological effects on living organisms. This study aimed to assess the antitumor potential of BthTX-I, a basic myotoxic PLA 2isolated from Bothrops jararacussu venom, by evaluating in vitro processes of cytotoxicity, modulation of the cell cycle and induction of apoptosis in human (HL-60 and HepG2) and murine (PC-12 and B16F10) tumor cell lines. Methods The cytotoxic effects of BthTX-I were evaluated on the tumor cell lines HL-60 (promyelocytic leukemia), HepG2 (human hepatocellular carcinoma), PC-12 (murine pheochromocytoma) and B16F10 (murine melanoma) using the MTT method. Flow cytometry... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Bothrops jararacussu; BthTX-I; Antitumor potential; Apoptosis; Cell cycle alterations. |
| Ano: 2015 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992015000100348 |
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| Cedro,Rafhaella C. A.; Menaldo,Danilo L.; Costa,Tássia R.; Zoccal,Karina F.; Sartim,Marco A.; Santos-Filho,Norival A.; Faccioli,Lúcia H.; Sampaio,Suely V.. |
| Abstract Background: Snake venom phospholipases A2 (PLA2s) have been reported to induce myotoxic, neurotoxic, hemolytic, edematogenic, cytotoxic and proinflammatory effects. This work aimed at the isolation and functional characterization of a PLA2 isolated from Bothrops jararaca venom, named BJ-PLA2-I. Methods and Results: For its purification, three consecutive chromatographic steps were used (Sephacryl S-200, Source 15Q and Mono Q 5/50 GL). BJ-PLA2-I showed acidic characteristics, with pI~4.4 and molecular mass of 14. 2 kDa. Sequencing resulted in 60 amino acid residues that showed high similarity to other Bothrops PLA2s, including 100% identity with BJ-PLA2, an Asp49 PLA2 previously isolated from B. jararaca venom. Being an Asp49 PLA2, BJ-PLA2-I... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Snake venom; Bothrops jararaca; Phospholipase A2; Inflammation; Cytotoxicity. |
| Ano: 2018 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992018000100324 |
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| Costa,Tássia R.; Carone,Sante E. I.; Tucci,Luiz F. F.; Menaldo,Danilo L.; Rosa-Garzon,Nathalia G.; Cabral,Hamilton; Sampaio,Suely V.. |
| Abstract Background: L-amino acid oxidases isolated from snake venoms (SV-LAAOs) are enzymes that have great therapeutic potential and are currently being investigated as tools for developing new strategies to treat various diseases, including cancer and bacterial infections. The main objective of this study was to make a brief evaluation of the enzymatic stability of two Bothrops LAAOs, one isolated from Bothrops jararacussu (BjussuLAAO-II) and the other from Bothrops moojeni (BmooLAAO-I) venoms. Methods and results: The enzymatic activity and stability of both LAAOs were evaluated by microplate colorimetric assays, for which BjussuLAAO-II and BmooLAAO-I were incubated with different L-amino acid substrates, in the presence of different ions, and at... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Snake venom; Bothrops; L-amino acid oxidase; Enzymatic stability. |
| Ano: 2018 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992018000100327 |
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| Menaldo,Danilo L.; Jacob-Ferreira,Anna L.; Bernardes,Carolina P.; Cintra,Adélia C. O.; Sampaio,Suely V.. |
| Background Snake venoms are complex mixtures of inorganic and organic components, mainly proteins and peptides. Standardization of methods for isolating bioactive molecules from snake venoms is extremely difficult due to the complex and highly variable composition of venoms, which can be influenced by factors such as age and geographic location of the specimen. Therefore, this study aimed to standardize a simple purification methodology for obtaining a P-I class metalloprotease (MP) and an acidic phospholipase A2 (PLA 2 ) from Bothrops atroxvenom, and biochemically characterize these molecules to enable future functional studies.Methods To obtain the toxins of interest, a method has been standardized using consecutive isolation steps. The purity level of... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Snake venoms; Bothrops atrox; Toxins; Metalloprotease; Phospholipase A2; Isolation; Characterization; Chromatography. |
| Ano: 2015 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992015000100337 |
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