Nigel Hooper, BSc Hons PhD

JAD profile

Affiliation(s): 

University of Manchester

Areas of Interest: 

Alzeimer's Disease, amyloid, amyloid precursor protein processing, secretases, lipid rafts, prion protein, secreted amyloid precursor protein, tau proteolysis, proteases

Biography & Research: 

Nigel Hooper received his Ph.D. in biochemistry at the University of Leeds in 1987. He was then awarded a Mr and Mrs John Jaffé Donation Research Fellowship from the Royal Society to work on the proteolysis and membrane anchorage of mammalian cell surface peptidases. In 1989 he was appointed as lecturer in the Department of Biochemistry at Leeds, followed by promotions to senior lecturer, reader and in 2001 to Professor of Biochemistry. He served as Director of the Institute of Molecular and Cellular Biology (2007-2011), Pro-Dean for Research (2011) and Dean (2012-2014) of the Faculty of Biological Sciences at the University of Leeds. In 2014 he was appointed to the Chair in Cell Biology in the Faculty of Medical and Human Sciences at the University of Manchester. He is currently Vice Dean for Research and Innovation in the Faculty of Biology, Medicine and Health at the University of Manchester. His research has focused on neurodegenerative and cardiovascular diseases. He applies a range of experimental approaches (biochemical, biophysical, molecular biological and cell biological techniques on individual proteins, cells in culture, animal models and human tissues) to probe normal biology and elucidate disease processes, with a common theme of proteolytic mechanisms and protein-membrane interactions. He has led a productive programme of research targeting the GPI-anchored prion protein (PrP) which has contributed to elucidation of the normal cell biology of PrP and provided insights into how loss of function (e.g. zinc uptake) contributes to its pathogenic role in prion disease. He was the first to report a molecular link between PrP and Alzheimer’s disease, when he showed that PrP inhibits the β-secretase-mediated cleavage of APP and thus amyloid-β production. He has also shown that PrP must be localized in rafts in order to mediate amyloid-β binding and subsequent toxic intracellular signalling.