|Tel||01865 279631, 01865 272451|
UV Uncaging of H+ ions
- Vaughan-Jones Group Research Group
Professor of Cellular Physiology
- Official Fellow and Tutor for Medicine and Physiology, Exeter College, Oxford.
- Joint-Director of The Burdon-Sanderson Cardiac Science Centre.
- BHF Programme Director, 2015-2020; "H+ ion control and signalling in cardiac hypertrophy and heart failure".
- President, Physiological Society 2014-2016
- Visiting Professor, Cardiovascular Research and Training Institute, University of Utah, Salt Lake City, Utah.
Richard Vaughan-Jones is Professor of Cellular Physiology at Oxford. He is co-founder and Joint-Director of the Burdon Sanderson Cardiac Science Centre, in the Department of Physiology, Anatomy & Genetics, and Tutorial Fellow in Medicine & Biomedical Sciences at Exeter College, Oxford. He studied Physiology at the University of Bristol (BSc, PhD), subsequently specialising in membrane ion-transport. He researches the mechanism and function of intracellular H+ ion sensing, signalling and regulation. His work centres on the heart, but also cancer and arterial chemoreception. He was the first to identify Cl/HCO3 exchange activity in non-erythroid tissue, Na-HCO3 and Cl/OH transporter activity in heart, and the role of gap-junctions and carbonic anhydrase enzymes in the spatial control of pH in the heart and in tumours.
Richard Vaughan-Jones was elected to the Physiological Society in 1978, and is currently serving as its President. He has served as an Editor of The Journal of Physiology and as a Trustee of the Society. For three years, he was Deputy Head of Exeter College, Oxford. He firmly believes in the importance of Physiology as an essential life-sciences/medical discipline, and in the pre-eminence of the Society for growing and sustaining a dynamic, research community.
Journal of Physiology Cover
The cover shows a confocal image of an enzymically isolated rat ventricular myocyte (~125 μm long), treated with 10 μM 8 di-ANEPPS, a fluorescent surface-membrane marker. The dye illuminates lateral sarcolemma, intercalated disks (at ends of cell), and transverse tubules (radial striations). Selective removal of transverse tubules (by osmotic shock) removes radial staining, and reduces the cell’s Na+–HCO3– cotransporter (NBC) activity by 40%, suggesting that NBC proteins are sited partly in tubular membranes. See Garciarena et al. pp. . 2287–2306.