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Am J Physiol Cell Physiol 280: C1233-C1241, 2001;
0363-6143/01 $5.00
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Vol. 280, Issue 5, C1233-C1241, May 2001

Pertussis toxin directly activates endothelial cell p42/p44 MAP kinases via a novel signaling pathway

Joe G. N. Garcia1, Peiyi Wang1, Feng Liu1, Marc B. Hershenson2, Talaibek Borbiev1, and Alexander D. Verin1

1 Division of Pulmonary and Critical Care Medicine, Department of Medicine, Johns Hopkins University School of Medicine, Baltimore, Maryland 21224; and 2 Department of Pediatrics, University of Chicago School of Medicine, Chicago, Illinois 60637

Bordetella pertussis generates a bacterial toxin utilized in signal transduction investigation because of its ability to ADP ribosylate specific G proteins. We previously noted that pertussis toxin (PTX) directly activates endothelial cells, resulting in disruption of monolayer integrity and intercellular gap formation via a signaling pathway that involves protein kinase C (PKC). We studied the effect of PTX on the activity of the 42- and 44-kDa extracellular signal-regulated kinases (ERK), members of a kinase family known to be activated by PKC. PTX caused a rapid time-dependent increase in bovine pulmonary artery endothelial cell ERK activity that was significantly attenuated by 1) pharmacological inhibition of MEK, the upstream ERK activating kinase, 2) an MEK dominant-negative construct, and 3) PKC inhibition with bisindolylmaleimide. There was little evidence for the involvement of either Gbeta gamma -subunits, Ras GTPases, Raf-1, p60src, or phosphatidylinositol 3'-kinases in PTX-mediated ERK activation. Both the purified beta -oligomer binding subunit of the PTX holotoxin and a PTX holotoxin mutant genetically engineered to eliminate intrinsic ADP ribosyltransferase activity completely reproduced PTX effects on ERK activation, suggesting that PTX-induced ERK activation involves a novel PKC-dependent signaling mechanism that is independent of either Ras or Raf-1 activities and does not require G protein ADP ribosylation.

signal transduction; endothelium; bacterial toxin; adenosine 5'-diphosphate ribosylation; extracellular signal-regulated kinases; beta -oligomer; Raf-1 activation; p21 Ras activity


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