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ACP-TX-I and ACP-TX-II, Two Novel Phospholipases A2 Isolated from Trans-Pecos Copperhead Agkistrodon contortrix pictigaster Venom: Biochemical and Functional Characterization.
Toxins (Basel). 2019 11 14; 11(11)T

Abstract

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.

Authors+Show Affiliations

Departamento de Ciencias Básicas, Facultad de Ciencias de la Salud, Escuela de Medicina Humana, Universidad Peruana Unión (UPeU), Lima 15, Peru.Instituto de Tecnologia e Pesquisa, Universidade Tiradentes (UNIT), Aracaju 49032-490, SE, Brazil.Departamento de Bioquímica, Instituto de Biologia, Universidade Estadual de Campinas (UNICAMP), Campinas 13083-970, SP, Brazil.Departamento de Ciencias Básicas, Facultad de Ciencias de la Salud, Escuela de Medicina Humana, Universidad Peruana Unión (UPeU), Lima 15, Peru.Departamento de Bioquímica, Instituto de Biologia, Universidade Estadual de Campinas (UNICAMP), Campinas 13083-970, SP, Brazil.

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

31739403

Citation

Huancahuire-Vega, Salomón, et al. "ACP-TX-I and ACP-TX-II, Two Novel Phospholipases A2 Isolated From Trans-Pecos Copperhead Agkistrodon Contortrix Pictigaster Venom: Biochemical and Functional Characterization." Toxins, vol. 11, no. 11, 2019.
Huancahuire-Vega S, Hollanda LM, Gomes-Heleno M, et al. ACP-TX-I and ACP-TX-II, Two Novel Phospholipases A2 Isolated from Trans-Pecos Copperhead Agkistrodon contortrix pictigaster Venom: Biochemical and Functional Characterization. Toxins (Basel). 2019;11(11).
Huancahuire-Vega, S., Hollanda, L. M., Gomes-Heleno, M., Newball-Noriega, E. E., & Marangoni, S. (2019). ACP-TX-I and ACP-TX-II, Two Novel Phospholipases A2 Isolated from Trans-Pecos Copperhead Agkistrodon contortrix pictigaster Venom: Biochemical and Functional Characterization. Toxins, 11(11). https://doi.org/10.3390/toxins11110661
Huancahuire-Vega S, et al. ACP-TX-I and ACP-TX-II, Two Novel Phospholipases A2 Isolated From Trans-Pecos Copperhead Agkistrodon Contortrix Pictigaster Venom: Biochemical and Functional Characterization. Toxins (Basel). 2019 11 14;11(11) PubMed PMID: 31739403.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - ACP-TX-I and ACP-TX-II, Two Novel Phospholipases A2 Isolated from Trans-Pecos Copperhead Agkistrodon contortrix pictigaster Venom: Biochemical and Functional Characterization. AU - Huancahuire-Vega,Salomón, AU - Hollanda,Luciana M, AU - Gomes-Heleno,Mauricio, AU - Newball-Noriega,Edda E, AU - Marangoni,Sergio, Y1 - 2019/11/14/ PY - 2019/09/26/received PY - 2019/10/30/revised PY - 2019/11/06/accepted PY - 2019/11/20/entrez PY - 2019/11/20/pubmed PY - 2019/11/20/medline KW - Agkistrodon contortrix pictigaster KW - D49 PLA2 KW - edema-forming activity and cytotoxicity KW - homologous K49 PLA2 KW - myotoxin KW - snake venom JF - Toxins JO - Toxins (Basel) VL - 11 IS - 11 N2 - 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. SN - 2072-6651 UR - https://www.unboundmedicine.com/medline/citation/31739403/ACP-TX-I_and_ACP-TX-II,_Two_Novel_Phospholipases_A2_Isolated_from_Trans-Pecos_Copperhead_Agkistrodon_contortrix_pictigaster_Venom:_Biochemical_and_Functional_Characterization L2 - https://www.mdpi.com/resolver?pii=toxins11110661 DB - PRIME DP - Unbound Medicine ER -
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