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Am J Physiol Heart Circ Physiol 281: H2705-H2713, 2001;
0363-6135/01 $5.00
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Vol. 281, Issue 6, H2705-H2713, December 2001

Endothelial NOS-dependent activation of c-Jun NH2- terminal kinase by oxidized low-density lipoprotein

Young-Mi Go2, Anna-Liisa Levonen2, Douglas Moellering2, Anup Ramachandran2, Rakesh P. Patel1,2, Hanjoong Jo3, and Victor M. Darley-Usmar1,2

1 Center for Free Radical Biology, 2 Department of Pathology, University of Alabama at Birmingham, Birmingham, Alabama 35294; and 3 Georgia Tech/Emory Biomedical Engineering Department, Emory University, Atlanta, Georgia 30322-4600

Oxidized low-density lipoprotein (oxLDL) is known to activate a number of signal transduction pathways in endothelial cells. Among these are the c-Jun NH2-terminal kinase (JNK), also known as stress-activated protein kinase, and extracellular signal-regulated kinase (ERK). These mitogen-activated protein kinases (MAP kinase) determine cell survival in response to environmental stress. Interestingly, JNK signaling involves redox-sensitive mechanisms and is activated by reactive oxygen and nitrogen species derived from both NADPH oxidases, nitric oxide synthases (NOS), peroxides, and oxidized low-density lipoprotein (oxLDL). The role of endothelial NOS (eNOS) in the activation of JNK in response to oxLDL has not been examined. Herein, we show that on exposure of endothelial cells to oxLDL, both ERK and JNK are activated through independent signal transduction pathways. A key role of eNOS activation through a phosphatidylinositol-3-kinase-dependent mechanism leading to phosphorylation of eNOS is demonstrated for oxLDL-dependent activation of JNK. Moreover, we show that activation of ERK by oxLDL is critical in protection against the cytotoxicity of oxLDL.

nitric oxide synthase; NAD(P)H oxidase; nitric oxide; extracellular signal-regulated kinase


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