ArticleThe Biochemical journal2003
The requirement of cytosolic phospholipase A2 for the PMA activation of proton efflux through the N-terminal 230-amino-acid fragment of gp91phox.
Article in The Biochemical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 14 citations in OpenAlex.
- The phospholipase A2 activity of peroxiredoxin 6 modulates NADPH oxidase 2 activation via lysophosphatidic acid receptor signaling in the pulmonary endothelium and alveolar macrophages.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2016Article
- NADPH oxidase-2: linking glucose, acidosis, and excitotoxicity in stroke.Antioxidants & redox signaling · 2015Article
- Ceramide kinase regulates TNFα-stimulated NADPH oxidase activity and eicosanoid biosynthesis in neuroblastoma cells.Cellular signalling · 2012Article
- Voltage-gated proton channels.Comprehensive Physiology · 2012Review
- Native LDL-induced oxidative stress in human proximal tubular cells: multiple players involved.Journal of cellular and molecular medicine · 2011Article
- Cytokine generation, promoter activation, and oxidant-independent NF-kappaB activation in a transfectable human neutrophilic cellular model.BMC immunology · 2008Article
- Sustained activation of proton channels and NADPH oxidase in human eosinophils and murine granulocytes requires PKC but not cPLA2 alpha activity.The Journal of physiology · 2007Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The absolute requirement for the 85 kDa cytosolic phospholipase A(2) (cPLA(2)) in the PMA stimulation of proton efflux through the NADPH-oxidase-associated proton channel, has previously been demonstrated using a PLB-985 cell line deficient in cPLA(2) (PLB-D). The flux of protons in Chinese-Hamster ovary (CHO) cells that express the N-terminal 230-amino-acid (NT) fragment of gp91(phox) is activated by arachidonic acid (AA) added externally. To investigate the physiological role of cPLA(2), and the intracellular AA that it releases, in the activation of proton flux through the NT fragment of gp91(phox), this fragment was stably expressed in PLB-985 cells (PLB-985 NT) and in PLB-D cells (PLB-D NT). The expression of the NT fragment of gp91(phox) by itself in PLB-985 did not initiate differentiation and did not alter their ability to undergo differentiation after the addition of DMSO. Addition of PMA induced a proton efflux from undifferentiated PLB-985 NT cells expressing the NT fragment of gp91(phox), which was inhibited by zinc. In contrast, PMA failed to activate proton efflux in undifferentiated PLB-D NT cells, lacking the expression of cPLA(2); however, addition of AA restored the efflux of protons in these cells. These results establish an essential and specific physiological requirement of cPLA(2)-generated AA in the activation of proton flux through the NT fragment of gp91(phox).
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