Conlon, J Michael, Attoub, Samir, Arafat, Hama, Mechkarska, Milena, Casewell, Nicholas ORCID: https://orcid.org/0000-0002-8035-4719, Harrison, Robert and Calvete, Juan J (2013) 'Cytotoxic activities of [Ser⁴⁹]phospholipase A₂ from the venom of the saw-scaled vipers Echis ocellatus, Echis pyramidum leakeyi, Echis carinatus sochureki, and Echis coloratus.'. Toxicon, Vol 71, pp. 96-104.
Full text not available from this repository.Abstract
Fractionation by reversed-phase HPLC of venom from four species of saw-scaled viper: Echis ocellatus, Echis pyramidum leakeyi, Echis carinatus sochureki, and Echis coloratus led to identification in each sample of an abundant protein with cytotoxic activity against human non-small cell lung adenocarcinoma A549 cells. The active component in each case was identified by MALDI-TOF mass fingerprinting of tryptic digests as [Ser⁴⁹]phospholipase A₂ ([Ser⁴⁹]PLA₂). An isoform of [Ser⁴⁹]PLA₂ containing the single Ala¹⁸→ Val substitution and a partially characterized [Asp⁴⁹]PLA₂ were also present in the E. coloratus venom. LC₅₀ values against A549 cells for the purified [Ser⁴⁹]PLA₂ proteins from the four species are in the range 2.9-8.5 μM. This range is not significantly different from the range of LC₅₀ values against human umbilical vein endothelial HUVEC cells (2.5-12.2 μM) indicating that the [Ser⁴⁹]PLA₂ proteins show no differential anti-tumor activity. The LC₅₀ value for [Ser⁴⁹]PLA₂ from E. ocellatus against human erythrocytes is >100 μM and the MIC values against Escherichia coli and Staphylococcus aureus are >100 μM. It is suggested that the [Ser⁴⁹]PLA₂ proteins play a major role in producing local tissue necrosis and hemorrhage at the site of envenomation.
Item Type: | Article |
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Subjects: | QU Biochemistry > Cells and Genetics > QU 350 Cellular structures QU Biochemistry > Proteins. Amino Acids. Peptides > QU 58.5 DNA. QV Pharmacology > Toxicology > General Toxicology > QV 600 General works WD Disorders of Systemic, Metabolic or Environmental Origin, etc > Animal Poisons > WD 410 Reptiles |
Faculty: Department: | Biological Sciences > Department of Tropical Disease Biology |
Digital Object Identifer (DOI): | https://doi.org/10.1016/j.toxicon.2013.05.017 |
Depositing User: | Mary Creegan |
Date Deposited: | 10 Nov 2014 09:37 |
Last Modified: | 06 Feb 2018 13:07 |
URI: | https://archive.lstmed.ac.uk/id/eprint/4534 |
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