| Literature DB >> 21690842 |
Ole G Mouritsen1, Thomas L Andresen, Avi Halperin, Per Lyngs Hansen, Ask F Jakobsen, Uffe Bernchou Jensen, Morten O Jensen, Kent Jørgensen, Thomas Kaasgaard, Chad Leidy, Adam Cohen Simonsen, Günther H Peters, Matthias Weiss.
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 A(2) (sPLA(2)), 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 sPLA(2) as derived from a range of different experimental and theoretical investigations.Entities:
Year: 2006 PMID: 21690842 DOI: 10.1088/0953-8984/18/28/S12
Source DB: PubMed Journal: J Phys Condens Matter ISSN: 0953-8984 Impact factor: 2.333