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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; in revised form: 19 March 2010 / Accepted: 22 March 2010 / Published: 26 March 2010
Abstract: 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
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MDPI and ACS Style
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.
Burgoyne JR, Eaton P. Oxidant Sensing by Protein Kinases A and G Enables Integration of Cell Redox State with Phosphoregulation. Sensors. 2010; 10(4):2731-2751.
Burgoyne, Joseph R.; Eaton, Philip. 2010. "Oxidant Sensing by Protein Kinases A and G Enables Integration of Cell Redox State with Phosphoregulation." Sensors 10, no. 4: 2731-2751.