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J Biol Chem, Vol. 274, Issue 49, 34669-34675, December 3, 1999
,§
From the We previously demonstrated that
lysophosphatidylcholine up-regulated endothelial nitric-oxide synthase
promoter activity by increasing Sp1 binding via the action of protein
serine/threonine phosphatase 2A (Cieslik, K., Zembowicz, A., Tang,
J.-L., and Wu, K.K. (1998) J. Biol. Chem. 273, 14885-14890). To characterize the regulation of basal endothelial
nitric-oxide synthase promoter activity and the signaling pathway
through which lysophosphatidylcholine augments endothelial nitric-oxide
synthase transcription, we used a casein kinase 2 inhibitor coupled
with immunoprecipitation to demonstrate that basal Sp1 binding and
endothelial nitric-oxide synthase promoter activity were controlled by
casein kinase 2 complexed with protein serine/threonine phosphatase 2A.
Casein kinase 2 catalyzed protein serine/threonine
phosphatase 2A phosphorylation thereby inhibiting its
activity. Lysophosphatidylcholine selectively activated p42/p44
mitogen-activated protein kinase. Purified extracellular regulated kinase 2 blocked casein kinase 2 activity and
increased protein serine/threonine phosphatase 2A activity, resulting
in an increased Sp1 binding and endothelial nitric-oxide synthase promoter activity. These results indicate that Sp1 binding to its
cognate site on the endothelial nitric-oxide synthase promoter and its
transactivation of endothelial nitric-oxide synthase is regulated
by post-translational Sp1 phosphorylation and dephosphorylation through
a dynamic interaction between casein kinase 2 and protein serine/threonine phosphatase 2A.
Vascular Biology Research Center and
Division of Hematology, University of Texas-Houston Medical School,
Houston, Texas 77030 and the § Vascular Biology Program,
Institute of Biomedical Sciences, Academia Sinica, Taipei, Taiwan and
National Taiwan University Hospital, College of Medicine,
Taipei, Taiwan 115
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