Conférence par Mahmood AMIRY‐MOGHADDAM, MD, PhD

Head, Laboratory of Molecular Neuroscience
Centre for Molecular Biology and Neuroscience (www.cmbn.no)
University of Oslo, Norway

Summary:

The water permeability of biological membranes has been a longstanding problem in physiology, but the proteins responsible for this remained unknown until discovery of the aquaporin 1 (AQP1) water channel protein. Peter Agre received Nobel prize in Chemistry in 2003 for this discovery. AQP1 is selectively permeated by water driven by osmotic gradients. The atomic structure of human AQP1 has recently been defined. Each subunit of the tetramer contains an individual aqueous pore that permits single‐file passage of water molecules but interrupts the hydrogen bonding needed for passage of protons. At least 12 mammalian aquaporins have been identified, and these are selectively permeated by water (aquaporins) or water plus glycerol (aquaglyceroporins). More than 200 members of the aquaporin family have been found in plants, microbials, invertebrates and vertebrates. Research in the past decade has shown that aquaporins are not only involved in important physiological processes such as maintenance of body water homeostasis, but are also involved in pathological conditions such as nephrogenic diabetes insipidus, cataract, metabolic syndrome, brain edema and malaria.

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Horaire : 11H

CONTACT:

Brian B. RUDKIN (bbrudkin@ens‐lyon.fr)