ACP-TX-I and ACP-TX-II, Two Novel Phospholipases A2 Isolated from Trans-Pecos Copperhead Agkistrodon contortrix pictigaster Venom: Biochemical and Functional Characterization
This work reports the purification and biochemical and functional characterization of ACP-TX-I and ACP-TX-II, two phospholipases A2 (PLA2) from Agkistrodon contortrix pictigaster venom. Both PLA2s were highly purified by a single chromatographic step on a C18 reverse phase HPLC column. Various pepti...
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2019
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| author | Huancahuire Vega, Salomon Hollanda, Luciana M. Gomes-Heleno, Mauricio Newball Noriega, Edda Evnet Marangoni, Sergio |
| author_browse | Gomes-Heleno, Mauricio Hollanda, Luciana M. Huancahuire Vega, Salomon Marangoni, Sergio Newball Noriega, Edda Evnet |
| author_facet | Huancahuire Vega, Salomon Hollanda, Luciana M. Gomes-Heleno, Mauricio Newball Noriega, Edda Evnet Marangoni, Sergio |
| author_sort | Huancahuire Vega, Salomon |
| collection | Producción científica |
| description | This work reports the purification and biochemical and functional characterization of ACP-TX-I and ACP-TX-II, two phospholipases A2 (PLA2) from Agkistrodon contortrix pictigaster venom. Both PLA2s were highly purified by a single chromatographic step on a C18 reverse phase HPLC column. Various peptide sequences from these two toxins showed similarity to those of other PLA2 toxins from viperid snake venoms. ACP-TX-I belongs to the catalytically inactive K49 PLA2 class, while ACP-TX-II is a D49 PLA2, and is enzymatically active. ACP-TX-I PLA2 is monomeric, which results in markedly diminished myotoxic and inflammatory activities when compared with dimeric K49 PLA2s, confirming the hypothesis that dimeric structure contributes heavily to the profound myotoxicity of the most active viperid K49 PLA2s. ACP-TX-II exhibits the main pharmacological actions reported for this protein family, including in vivo local myotoxicity, edema-forming activity, and in vitro cytotoxicity. ACP-TX-I PLA2 is cytotoxic to A549 lung carcinoma cells, indicating that cytotoxicity to these tumor cells does not require enzymatic activity. |
| format | Article |
| id | oai:cris.upeu.edu.pe:20.500.15037/491 |
| institution | UPeU |
| language | English |
| publishDate | 2019 |
| publishDateRange | 2019 |
| publishDateSort | 2019 |
| record_format | dspace |
| spelling | oai:cris.upeu.edu.pe:20.500.15037/4912026-11-02T12:57:04ZACP-TX-I and ACP-TX-II, Two Novel Phospholipases A2 Isolated from Trans-Pecos Copperhead Agkistrodon contortrix pictigaster Venom: Biochemical and Functional CharacterizationHuancahuire Vega, SalomonHollanda, Luciana M.Gomes-Heleno, MauricioNewball Noriega, Edda EvnetMarangoni, SergioSnake venomMyotoxinAgkistrodon Contortrix PictigasterD49 Pla2Edema-forming Activity And CytotoxicityHomologous K49 Pla2This work reports the purification and biochemical and functional characterization of ACP-TX-I and ACP-TX-II, two phospholipases A2 (PLA2) from Agkistrodon contortrix pictigaster venom. Both PLA2s were highly purified by a single chromatographic step on a C18 reverse phase HPLC column. Various peptide sequences from these two toxins showed similarity to those of other PLA2 toxins from viperid snake venoms. ACP-TX-I belongs to the catalytically inactive K49 PLA2 class, while ACP-TX-II is a D49 PLA2, and is enzymatically active. ACP-TX-I PLA2 is monomeric, which results in markedly diminished myotoxic and inflammatory activities when compared with dimeric K49 PLA2s, confirming the hypothesis that dimeric structure contributes heavily to the profound myotoxicity of the most active viperid K49 PLA2s. ACP-TX-II exhibits the main pharmacological actions reported for this protein family, including in vivo local myotoxicity, edema-forming activity, and in vitro cytotoxicity. ACP-TX-I PLA2 is cytotoxic to A549 lung carcinoma cells, indicating that cytotoxicity to these tumor cells does not require enzymatic activity.Articlehttps://pubmed.ncbi.nlm.nih.gov/31739403https://www.mdpi.com/2072-6651/11/11/661/pdf?version=1573712119https://doi.org/10.3390/toxins11110661PMC689168710.3390/toxins11110661https://hdl.handle.net/20.500.15037/49131739403W2986921775enToxins2072-66512019-11-142026-06-13T08:14:56Z2026-06-13T08:14:56Z |
| spellingShingle | Snake venom Myotoxin Agkistrodon Contortrix Pictigaster D49 Pla2 Edema-forming Activity And Cytotoxicity Homologous K49 Pla2 Huancahuire Vega, Salomon Hollanda, Luciana M. Gomes-Heleno, Mauricio Newball Noriega, Edda Evnet Marangoni, Sergio ACP-TX-I and ACP-TX-II, Two Novel Phospholipases A2 Isolated from Trans-Pecos Copperhead Agkistrodon contortrix pictigaster Venom: Biochemical and Functional Characterization |
| title | ACP-TX-I and ACP-TX-II, Two Novel Phospholipases A2 Isolated from Trans-Pecos Copperhead Agkistrodon contortrix pictigaster Venom: Biochemical and Functional Characterization |
| title_full | ACP-TX-I and ACP-TX-II, Two Novel Phospholipases A2 Isolated from Trans-Pecos Copperhead Agkistrodon contortrix pictigaster Venom: Biochemical and Functional Characterization |
| title_fullStr | ACP-TX-I and ACP-TX-II, Two Novel Phospholipases A2 Isolated from Trans-Pecos Copperhead Agkistrodon contortrix pictigaster Venom: Biochemical and Functional Characterization |
| title_full_unstemmed | ACP-TX-I and ACP-TX-II, Two Novel Phospholipases A2 Isolated from Trans-Pecos Copperhead Agkistrodon contortrix pictigaster Venom: Biochemical and Functional Characterization |
| title_short | ACP-TX-I and ACP-TX-II, Two Novel Phospholipases A2 Isolated from Trans-Pecos Copperhead Agkistrodon contortrix pictigaster Venom: Biochemical and Functional Characterization |
| title_sort | acp tx i and acp tx ii two novel phospholipases a2 isolated from trans pecos copperhead agkistrodon contortrix pictigaster venom biochemical and functional characterization |
| topic | Snake venom Myotoxin Agkistrodon Contortrix Pictigaster D49 Pla2 Edema-forming Activity And Cytotoxicity Homologous K49 Pla2 |
| topic_facet | Snake venom Myotoxin Agkistrodon Contortrix Pictigaster D49 Pla2 Edema-forming Activity And Cytotoxicity Homologous K49 Pla2 |
| url | https://pubmed.ncbi.nlm.nih.gov/31739403 https://www.mdpi.com/2072-6651/11/11/661/pdf?version=1573712119 https://doi.org/10.3390/toxins11110661 https://hdl.handle.net/20.500.15037/491 |
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