Mouritsen, Ole G.2; Andresen, Thomas Lars3; Halperin, Avi4; Hansen, Per Lyngs2; Jakobsen, Ask F.2; Bernchou Jensen, Uffe2; Jensen, Morten Ø.2; Jørgensen, Kent5; Kaasgaard, Thomas1; Leidy, Chad1; Simonsen, Adam Cohen2; Peters, Günther H.J.1; Weiss, Matthias7
1 Department of Chemistry, Technical University of Denmark2 University of Southern Denmark3 Department of Micro- and Nanotechnology, Technical University of Denmark4 French National Centre for Scientific Research5 Department of Chemistry, Technical University of Denmark6 German Cancer Research Center7 German Cancer Research Center
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.
Journal of Physics: Condensed Matter, 2006, Vol 18, Issue 28