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Professor Anthony J Turner
School of Biochemistry and Microbiology
University of Leeds
Leeds LS2 9JT, U.K.
Email: a.j.turner@leeds.ac.uk
Tel: (+44) 113 343 3131
Fax: (+44) 113 242 3187
Homepage: http://www.bmb.leeds.ac.uk/?staff=AJT

Membrane Metalloproteases in Health and Disease. Proteinases play a key role in many aspects of cell regulation - from fertilisation and embryogenesis to cell death. The main focus of our research is understanding the molecular and cell biology of critical metalloproteinase targets in brain, cardiovascular system and reproductive tissue. A primary focus involves the neprilysin (NEP)/endothelin converting enzyme (ECE) family, which now numbers seven in humans but is over twenty in both C. elegans and Drosophila. We are using functional genomics approaches to understand the multiple roles of these NEP homologues in terminating neuropeptide signalling events in vertebrate and invertebrate organisms. In particular, we have projects in the areas of atherosclerosis, neurodegeneration and cancer. We have also recently cloned and characterized a novel human homologue (ACE2) of the blood pressure regulating peptidase, angiotensin converting enzyme (ACE). We are currently exploring the structure and physiological roles of ACE2 and whether it might constitute a therapeutic target. To date it has been implicated in cardiovascular and renal disease, diabetes and obesity. Most recently, it has been identified as a receptor for the SARS coronavirus on the cell surface. A third topic area involves an understanding of the proteolytic events involved in the production and removal of the beta-amyloid peptide, involved in Alzheimer's disease. Remarkably, NEP and its homologue ECE both appear to play key roles in disposing of the toxic amyloid and therefore serve multiple roles in the body. We also have projects relating to the cell biology of the proteinases regulating the amyloidogenic (beta-secretase) and non-amyloidogenic (alpha-secretase) pathways of amyloid precursor protein metabolism. The involvement of lipid rafts as proteolytic ?hot spots? in the cell membrane is also under investigation.
Professor Ravi Acharya (University of Bath, Bath, U.K.)
Professor Toshihiro Ansai (Kyushi Dental College, Kitakyushu, Japan)
Professor Nigel Hooper (University of Leeds, Leeds, U.K.)
Dr Ari Huovila (University Tampere, Tampere, Finland)
Professor Norman Maitland (University of York, York, U.K.)
Professor H.S. Park (College of Pharmacy, Chonnam National University, Kwangju,
Professor A. Ian Smith (Baker Medical Research Institute, Melbourne, Australia)
Professor Ed Sturrock (University of Cape Town, South Africa)
Dr Igor Zhuravin (Institute of Evolutionary Biochemistry & Physiology, St Petersburg, Russia)
Dawson, L.A., Maitland, N.J., Turner, A.J. and Usmani, B.A. (2004) Stromal-epithelial interactions influence prostate cancer cell invasion by altering the balance of metallopeptidase expression. Brit. J. Cancer, in press.

Parkin, E.T., Watt, N.T., Turner, A.J. and Hooper, N.M. (2004) Dual mechanisms for shedding of the cellular prion protein. J. Biol. Chem. 279, [Jan 7, Epub ahead of print]
PMID: 14711812.

Guy, J.L., Jackson, R.M., Acharya, K.R., Sturrock, E.D., Hooper, N.M. and Turner, A.J. (2003) Angiotensin-converting enzyme-2 (ACE2): comparative modeling of the active site, specificity requirements, and chloride dependence. Biochemistry 42, 13185-13192.

Cordy, J.M., Hussain, I., Dingwall, C., Hooper, N.M. and Turner, A.J. (2003) Exclusively targeting beta-secretase to lipid rafts by GPI-anchor addition up-regulates beta-site processing of the amyloid precursor protein. Proc. Natl. Acad. Sci. U.S.A. 100, 11735-11740.

Parkin, E.T., Tan, F., Skidgel, R.A., Turner, A.J. and Hooper, N.M. (2003) The ectodomain shedding of angiotensin-converting enzyme is independent of its localisation in lipid rafts. J. Cell Sci. 116, 3079-3087.

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