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Calcium‐dependence of laminin binding to phospholipid membranes
Author(s) -
Ramsden Jeremy J.
Publication year - 1993
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360330313
Subject(s) - chemistry , laminin , membrane , calcium , lipid bilayer , biophysics , bilayer , phospholipid , absorption (acoustics) , biochemistry , organic chemistry , materials science , biology , composite material , cell
Laminin is the most abundant noncollagenous protein in basement membranes. Its selfassembly 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. © 1993 John Wiley & Sons, Inc.