Dynamic activation of endothelial nitric oxide synthase by Hsp90

Guillermo García-Cardeña, Roger Fan, Vijay Shah, Raffaella Sorrentino, Giuseppe Cirino, Andreas Papapetropoulos and William C. Sessa ()
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Guillermo García-Cardeña: Department of Pharmacology and Molecular Cardiobiology Program
Roger Fan: Department of Pharmacology and Molecular Cardiobiology Program
Vijay Shah: Boyer Center for Molecular Medicine, Yale University School of Medicine
Raffaella Sorrentino: Universita' degli Studi di Napoli Federico II
Giuseppe Cirino: Universita' degli Studi di Napoli Federico II
Andreas Papapetropoulos: Department of Pharmacology and Molecular Cardiobiology Program
William C. Sessa: Department of Pharmacology and Molecular Cardiobiology Program

Nature, 1998, vol. 392, issue 6678, 821-824

Abstract: Abstract Heat-shock protein 90 (Hsp90) coordinates the trafficking and regulation of diverse signalling proteins, but its precise role in regulating specific cellular targets is not known1,2. Here we show that Hsp90 associates with endothelial nitric oxide synthase (eNOS) and is rapidly recruited to the eNOS complex by agonists that stimulate production of nitric oxide, namely vascular endothelial growth factor, histamine and fluid shear stress. Moreover, the binding of Hsp90 to eNOS enhances the activation of eNOS. Inhibition of signalling through Hsp90 attenuates both agonist-stimulated production of nitric oxide and endothelium-dependent relaxation of isolated blood vessels. Our results indicate that Hsp90 facilitates signalling mediated by growth-factor, G-protein and mechanotransduction pathways that lead to the activation of eNOS. These observations indicate that in addition to its role as a molecular chaperone involved in protein folding and maturation, Hsp90 may also be recruited to cellular targets depending on the activation state of the cell.

Date: 1998
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DOI: 10.1038/33934

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