title: Calcium-dependence of laminin binding to phospholipid membranes.
abstract: Laminin is the most abundant noncollagenous protein in basement membranes. Its self-assembly has been studied in solution, and it has been established that calcium ions induce partially reversible aggregation. The behavior at a lipid membrane surface is of greater biological significance, but it is difficult to study quantitatively binding kinetics at a surface. The present work uses a powerful new integrated optics technique to measure the absorption and aggregation of the laminin-nidogen at a bilayer lipid membrane surface. It is found that the binding of a single layer of laminin at the lipid membrane is independent of the presence of calcium, but that the building up of multilayer laminin membranes requires calcium, and that these may not be destroyed by a calcium-complexing agent.
authors: Department of Biophysical Chemistry, Biozentrum, Basle, Switzerland.
authors: J J
authors: JJ
authors: Ramsden
mesh_terms: D002118:Calcium / Q000378:metabolism; D066298:In Vitro Techniques; D007797:Laminin / Q000378:metabolism*; D008051:Lipid Bilayers / Q000378:metabolism; D008563:Membrane Lipids / Q000378:metabolism; D010743:Phospholipids / Q000378:metabolism*; D011485:Protein Binding
chemical_list: D007797:Laminin; D008051:Lipid Bilayers; D008563:Membrane Lipids; D010743:Phospholipids; D002118:Calcium