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Speaker: Dr Joe Burgoyne, The Rayne Institute, School of Cardiovascular Medicine and Sciences

Host: Elisabeth Ehler

As reversible redox-dependent protein disulphides are integral mediators of cellular signalling, they provide rational targets for therapy. The aim of our work is to identify the targets of this modification and to characterise their function within the cardiovascular system. This work has led to the discovery that cGMP-dependent protein kinase 1a (PKG1a) forms a redox-dependent intermolecular disulphide, a modification that increases substrate affinity and subsequent phosphorylation. This novel mode of PKG1a activation was found to underlie the regulation of blood pressure, as mutant mice with redox-insensitive PKG1a (C42S knock-in mice) are hypertensive.

In this talk I will discuss how, resveratrol, a natural polyphenol and antioxidant, was found to lower blood pressure by directly inducing oxidation of PKG1a. Also, how we have identified a lead compound that can activate PKG1a by mediating its disulphide dimerisation. Finally, I will describe our recent work using structural bioinformatics to identify new substrates of redox-dependent disulphide formation, which could provide future targets for therapy.

Event details

Room G8, New Hunt's House.
Guy’s Campus
Great Maze Pond, London SE1 1UL