Fr. Poulain et al., KINETICS OF PHOSPHOLIPID MEMBRANE-FUSION INDUCED BY SURFACTANT APOPROTEIN-A AND APOPROTEIN-B, Biochimica et biophysica acta. Biomembranes, 1278(2), 1996, pp. 169-175
Surfactant apoproteins A (SP-A) and B (SP-B) interact with the lipids
of surfactant and such protein-lipid interactions may be of importance
in several of the steps in the surfactant cycle. We analyzed the kine
tics of fusion of ipalmitoylphosphatidylcholine-phosphatidylglycerol (
DPPC:PG; 7:3, w/w) phospholipid vesicles induced by SP-B alone, in the
presence of 5 mM calcium, and in the presence of calcium and SP-A. Me
mbrane fusion was measured by the method of resonance energy transfer
between non-exchangeable fluorophores incorporated in the membrane, Da
ta were analyzed using a mass action kinetic model for membrane fusion
between phospholipid vesicles. We found a SP-B dose-dependent increas
e in lipid mixing within a range of phospholipid concentration of 5 to
100 mu M. Calcium caused a small additive increase in lipid mixing, b
ut calcium and SP-A combined markedly increased lipid mixing induced b
y SP-B. Both aggregation and fusion rate constants increased with an i
ncrease in the SP-B/lipid ratio. In the presence of calcium and SP-A,
the number of vesicles per fusion product markedly increased, as did t
he aggregation rate constants, whereas the fusion rate constants remai
ned essentially unchanged.