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Activation of interfacial enzymes at membrane surfaces

Ole G Mouritsen et al 2006 J. Phys.: Condens. Matter 18 S1293-S1304   doi: 10.1088/0953-8984/18/28/S12  Help

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Ole G Mouritsen1,7, Thomas L Andresen2, Avi Halperin3, Per Lyngs Hansen1, Ask F Jakobsen1,4, Uffe Bernchou Jensen1, Morten Ø Jensen1, Kent Jørgensen2, Thomas Kaasgaard5, Chad Leidy5,6, Adam Cohen Simonsen1, Günther H Peters5 and Matthias Weiss4
1 MEMPHYS-Center for Biomembrane Physics, Physics Department, University of Southern Denmark, Campusvej 55, DK-5230 Odense M, Denmark
2 LiPlasome Pharma A/S, Technical University of Denmark, Building 207, DK-2800 Lyngby, Denmark
3 UMR 5819, DRFMC/SI3M, CEA-CENG, 17 Rue des Martyrs, 38054 Grenoble Cedex 9, France
4 Cellular Biophysics Group (BIOMS), German Cancer Research Center, Im Neuenheimer Feld 580, D-69121 Heidelberg, Germany
5 Department of Chemistry, Technical University of Denmark, Building 207, DK-2800 Lyngby, Denmark
6 Physics Department, Universidad de los Andes, Bogota, Colombia
7 Author to whom any correspondence should be addressed
E-mail: ogm@memphys.sdu.dk

Abstract. A host of water-soluble enzymes are active at membrane surfaces and in association with membranes. Some of these enzymes are involved in signalling and in modification and remodelling of the membranes. A special class of enzymes, the phospholipases, and in particular secretory phospholipase A2 (sPLA2), are only activated at the interface between water and membrane surfaces, where they lead to a break-down of the lipid molecules into lysolipids and free fatty acids. The activation is critically dependent on the physical properties of the lipid-membrane substrate. A topical review is given of our current understanding of the physical mechanisms responsible for activation of sPLA2 as derived from a range of different experimental and theoretical investigations.

Print publication: Issue 28 (19 July 2006)
Received 3 November 2005, in final form 1 February 2006
Published 28 June 2006

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