Role of l-amino acid oxidase isolated from Calloselasma rhodostoma venom on neutrophil NADPH oxidase complex activation. (April 2018)

• Record Type: Journal Article
• Authors: Paloschi, Mauro Valentino; Boeno, Charles Nunes; Lopes, Jéssica Amaral; Eduardo dos Santos da Rosa, André; Pires, Weverson Luciano; Pontes, Adriana Silva; da Silva Setúbal, Sulamita; Soares, Andreimar Martins; Zuliani, Juliana Pavan
• Is Part Of: Toxicon. Volume 145(2018)
• Page Start: 48
• Page End: 55
• Publication Date: 2018-04
• Subjects: Snake venom -- LAAO -- Neutrophils -- NADPH oxidase -- Signaling; Toxins -- Periodicals; Venom -- Periodicals; 615.9
• DOI: 10.1016/j.toxicon.2018.02.046
• Languages: English
• ISSNs: 0041-0101

Abstract

Abstract: The action of Cr-LAAO, anl -amino acid oxidase isolated from Calloselasma rhodosthoma snake venom, on NADPH oxidase activation in isolated human neutrophil function was investigated. This enzyme has an intrinsic activity of hydrogen peroxide production. Cr-LAAO, in its native form, induces the ROS production in neutrophil and migration of cytosolic NADPH oxidase components p40 phox, p47 phox and p67 phox to the membrane, and Rac, a GTPase protein member, with the involvement of intracellular signaling mediated by phospho PKC-α. In its inactive form, iCr-LAAO does not induce NADPH oxidase activation in neutrophil showing that the intrinsic enzymatic activity does not have a role in this process, suggesting that its primary structure is essential for the cell's stimulation. Accordingly, the data showed for the first time that the Cr-LAAO has a role in NADPH oxidase complex activation triggering relevant proinflammatory events in human neutrophils. Graphical abstract: Highlights: Cr-LAAO induced NADPH oxidase activation in neutrophils. Cr-LAAO induced migration of p40 phox, p47 phox and p67 phox and Rac to the membrane. Cr-LAAO induced PKC-α phosphorylation. Cr-LAAO induces the ROS production in neutrophil.