Shear stress stimulates phosphorylation of protein kinase A substrate proteins including endothelial nitric oxide synthase in endothelial cells

Experimental & Molecular Medicine
Yong Chool Boo

Abstract

Fluid shear stress plays a critical role in vascular health and disease. While protein kinase A (PKA) has been implicated in shear-stimulated signaling events in endothelial cells, it remains unclear whether and how PKA is stimulated in response to shear stress. This issue was addressed in the present study by monitoring the phosphorylation of endogenous substrates of PKA. Shear stress stimulated the phosphorylation of cAMP responsive element binding protein (CREB) in a PKA-dependent manner. Western blot analysis using the antibody reactive against the consensus motif of PKA substrates detected two proteins, P135 and P50, whose phosphorylation was increased by shear stress. The phosphorylation of P135 was blocked by a PKA inhibitor, H89, but not by a phosphoinositide 3-kinase inhibitor, wortmannin. Expression of a constitutively active PKA subunit stimulated P135 phosphorylation, supporting the potential of P135 as a PKA substrate. P135 was identified as endothelial nitric oxide synthase (eNOS) by immunoprecipitation study. PKA appeared to mediate shear stress-stimulated eNOS activation. Shear stress stimulated intracellular translocation of PKA activity from 'soluble' to 'particulate' fractions without involving cellular cAMP ...Continue Reading

Citations

Apr 12, 2012·Cardiovascular Research·Shyamal C BirJincai Luo
May 29, 2014·The Journal of Clinical Investigation·Jessilyn DunnHanjoong Jo
Feb 18, 2011·Journal of Cellular Biochemistry·Maria Grazia SignorelloGiuliana Leoncini
Feb 6, 2017·Journal of Human Kinetics·Krzysztof Krzeminski
Sep 19, 2009·Circulation Research·Bhama RamkhelawonStéphanie Lehoux
Mar 4, 2008·The Journal of Biological Chemistry·Anne A WooldridgeTimothy A J Haystead
Feb 6, 2015·American Journal of Physiology. Cell Physiology·Mohan NatarajanSumathy Mohan

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