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J Biol Chem, Vol. 274, Issue 1, 143-150, January 1, 1999

Fluid Shear Stress Stimulates Big Mitogen-activated Protein Kinase 1 (BMK1) Activity in Endothelial Cells
DEPENDENCE ON TYROSINE KINASES AND INTRACELLULAR CALCIUM

Chen Yan, Masafumi Takahashi, Masanori Okuda, Jiing-Dwan Lee, and Bradford C. Berk^**

From the  Department of Medicine, Division of Cardiology, University of Washington, Seattle, Washington 98195, the ^** Cardiology Unit, University of Rochester, Rochester, New York 14642, and the  Department of Immunology, Scripps Research Institute, La Jolla, California 92037

Mitogen-activated protein (MAP) kinases including ERK1/2 and JNK play an important role in shear stress-mediated gene expression in endothelial cells (EC). A new MAP kinase termed big MAP kinase 1 (BMK1/ERK5) has been shown to phosphorylate and activate the transcription factor MEF2C, which is highly expressed in EC. To determine the effects of shear stress on BMK1, bovine aortic EC were exposed to steady laminar flow (shear stress = 12 dynes/cm²). Flow activated BMK1 within 10 min with peak activation at 60 min (7.1 ± 0.6-fold) in a force-dependent manner. Flow was the most powerful activator of BMK1, significantly greater than H₂O₂ or sorbitol. An important role for non-Src tyrosine kinases in flow-mediated BMK1 activation was demonstrated by inhibition with herbimycin A, but not with the Src inhibitor PP1 or overexpression of kinase-inactive c-Src. BMK1 activation was calcium-dependent as shown by inhibition with 1,2-bis(2-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid/acetoxymethyl ester or thapsigargin. As shown by specific inhibitors or activators, flow-mediated BMK1 activation was not regulated by the following: intracellular redox state; intracellular NO; protein kinase A, C, or G; calcium/calmodulin-dependent kinase; phosphatidylinositol 3-kinase; or arachidonic acid metabolism. In summary, flow potently stimulates BMK1 in EC by a mechanism dependent on a tyrosine kinase(s) and calcium mobilization, but not on c-Src, redox state, or NO production.

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Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.

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