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Sensors 2010, 10(4), 2731-2751; doi:10.3390/s100402731

Oxidant Sensing by Protein Kinases A and G Enables Integration of Cell Redox State with Phosphoregulation

Department of Cardiology, The Rayne Institute, King’s College London, St. Thomas’ Hospital, London, SE1 7EH, UK
* Author to whom correspondence should be addressed.
Received: 11 January 2010 / Revised: 19 March 2010 / Accepted: 22 March 2010 / Published: 26 March 2010
(This article belongs to the Special Issue State-of-the-Art Sensors Technology in the UK)
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The control of vascular smooth muscle contractility enables regulation of blood pressure, which is paramount in physiological adaptation to environmental challenges. Maintenance of stable blood pressure is crucial for health as deregulation (caused by high or low blood pressure) leads to disease progression. Vasotone is principally controlled by the cyclic nucleotide dependent protein kinases A and G, which regulate intracellular calcium and contractile protein calcium sensitivity. The classical pathways for activation of these two kinases are well established and involve the formation and activation by specific cyclic nucleotide second messengers. Recently we reported that both PKA and PKG can be regulated independently of their respective cyclic nucleotides via a mechanism whereby the kinases sense cellular oxidant production using redox active thiols. This novel redox regulation of these kinases is potentially of physiological importance, and may synergise with the classical regulatory mechanisms.
Keywords: protein kinase A; protein kinase G; oxidation protein kinase A; protein kinase G; oxidation
This is an open access article distributed under the Creative Commons Attribution License (CC BY) which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Burgoyne, J.R.; Eaton, P. Oxidant Sensing by Protein Kinases A and G Enables Integration of Cell Redox State with Phosphoregulation. Sensors 2010, 10, 2731-2751.

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