A redox switch in angiotensinogen modulates angiotensin release

Aiwu Zhou (), Robin W. Carrell (), Michael P. Murphy, Zhenquan Wei, Yahui Yan, Peter L. D. Stanley, Penelope E. Stein, Fiona Broughton Pipkin and Randy J. Read
Additional contact information
Aiwu Zhou: Cambridge Institute for Medical Research, University of Cambridge
Robin W. Carrell: Cambridge Institute for Medical Research, University of Cambridge
Michael P. Murphy: MRC Mitochondrial Biology Unit
Zhenquan Wei: Cambridge Institute for Medical Research, University of Cambridge
Yahui Yan: Cambridge Institute for Medical Research, University of Cambridge
Peter L. D. Stanley: Cambridge Institute for Medical Research, University of Cambridge
Penelope E. Stein: Cambridge Institute for Medical Research, University of Cambridge
Fiona Broughton Pipkin: University of Nottingham, City Hospital
Randy J. Read: Cambridge Institute for Medical Research, University of Cambridge

Nature, 2010, vol. 468, issue 7320, 108-111

Abstract: A blood pressure control point A 20-year effort has succeeded in identifying the initiating step in the molecular interactions that release the vasopressor peptide angiotensin, and hence control blood pressure. Angiotensins are generated by cleavage of a larger protein, angiotensinogen, by the enzyme renin. Crystal structures of angiotensinogen alone and bound to renin now show that a large conformational change is required to expose the renin cleavage site. This transition is regulated by oxidation, and women with pre-eclampsia — which is associated with high blood pressure — have higher levels of the more active oxidized form.

Date: 2010
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DOI: 10.1038/nature09505

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