BaltPLA2: A New Phospholipase A2 from Bothrops Alternatus Snake Venom with Antiplatelet Aggregation Activity.

Autor:	Dias EHV; Federal University of Uberlandia, Molecular and Cellular Biology Laboratory, Uberlandia, Brazil., Dos Santos Paschoal T; Federal University of Uberlandia, Molecular and Cellular Biology Laboratory, Uberlandia, Brazil., da Silva AP; Federal University of Uberlandia, Molecular and Cellular Biology Laboratory, Uberlandia, Brazil., da Cunha Pereira DF; Federal University of Uberlandia, Molecular and Cellular Biology Laboratory, Uberlandia, Brazil., de Sousa Simamoto BB; Federal University of Uberlandia, Molecular and Cellular Biology Laboratory, Uberlandia, Brazil., Matias MS; Federal University of Uberlandia, Molecular and Cellular Biology Laboratory, Uberlandia, Brazil., Santiago FM; Federal University of Uberlandia, Molecular and Cellular Biology Laboratory, Uberlandia, Brazil., Rosa JC; Department of Cellular and Molecular Biology and Pathogenic Bioagents and Center for Protein Chemistry, Sao Paulo Universit, Sao Paulo, Brazil., Soares A; Center for the Study of Biomolecules Applied to Health - CEBio, Oswaldo Cruz Foundation, FIOCRUZ Rondonia and Health Center, Federal University of Rondonia, UNIR, Porto Velho-RO, Brazil., Santos-Filho NA; Institute of Chemistry - UNESP Araraquara, Sao Paulo, Brazil., de Oliveira F; Federal University of Uberlandia, Institute of Biomedical Science, Uberlandia, Brazil., Mamede CCN; Federal University of Uberlandia - Institute of Agricultural Sciences Uberlandia, Uberlandia, Brazil.
Jazyk:	angličtina
Zdroj:	Protein and peptide letters [Protein Pept Lett] 2018; Vol. 25 (10), pp. 943-952.
DOI:	10.2174/0929866525666181004101622
Abstrakt:	Background: In last decades, snake venoms have aroused great interest of the medicine due to the pathophysiological effects caused by their toxins. These include the phospholipases A2, low molecular weight proteins capable of causing haemorrhagic, myotoxic, inflammatory and neurotoxic effects after an ophidian accident. The present work describes the isolation and biochemical characterization of a new PLA2 isolated from the B. alternatus snake venom, which was named BaltPLA2. Method: The rapid and efficient purification of this toxin was performed using only two chromatography steps (anion exchange and hydrophobic chromatography). Results: BaltPLA2 is an acidic protein (pI 4.4) with an apparent molecular mass of 17000 (SDSPAGE) and 14074.74 Da (MALDI TOF/TOF). Analysis of fragments ion by MS / MS showed the following internal amino acid sequence SGVIICGEGTPCEK, which did not exhibit homology with other PLA2 from the same venom. BaltPLA2 is a catalytically active, which displayed an anticoagulant action, inhibition of platelet aggregation induced by epinephrine (~ 80%) and ADP (24%). BaltPLA2 also was able to induce myonecrosis and the release of cytokines (IL-10, IL-12 and TNF- α) in macrophages culture. Conclusion: The results presented in this work greatly contribute to a better understanding of the mechanism of enzymatic and pharmacological actions of PLA2s from snake venoms and they may contribute to its application in medical research. (Copyright© Bentham Science Publishers; For any queries, please email at epub@benthamscience.org.)
Databáze:	MEDLINE
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