Effects of proteins on phospholipid vesicle aggregation and lipid vesicle-monolayer interactions.
The effects of proteins on divalent cation-induced phospholipid vesicle aggregation and phospholipid vesicle-monolayer membrane interactions (fusion) were examined. Glycophorin (from human erythrocytes) suppressed the membrane interactions more than N-2 protein (from human brain myelin) when these proteins were incorporated into acidic phospholipid vesicle membranes. The threshold concentrations of divalent cations which induced vesicle aggregation were increased by protein incorporation, and the rate of vesicle aggregation was reduced. A similar inhibitory effect by the proteins, incorporated into lipid vesicle membranes, was observed for Ca2+-induced lipid vesicle-monolayer interactions. However, when these proteins were incorporated only in the acidic phospholipid monolayers, the interaction (fusion) of the lipid vesicle-monolayer membranes, induced by divalent cations, was not appreciably altered by the presence of the proteins. In contrast to these two proteins, the presence of synexin in the solution did enhance the Ca2+-induced aggregation of phosphatidylserine vesicles, but did not seem to affect the degree of Ca2+-induced fusion between phosphatidylserine/phosphatidylcholine (1:1) and phosphatidylserine vesicles and monolayer membranes.
D000818:Animals; D001923:Brain Chemistry; D002417:Cattle; D005614:Freeze Fracturing; D006021:Glycophorins; D006801:Humans; D008081:Liposomes; D008854:Microscopy, Electron; D009185:Myelin Proteins; D009391:Nephelometry and Turbidimetry; D010713:Phosphatidylcholines; D010718:Phosphatidylserines; D011485:Protein Binding; D012795:Sialoglycoproteins; D013500:Surface Tension
D006021:Glycophorins; D008081:Liposomes; D009185:Myelin Proteins; D010713:Phosphatidylcholines; D010718:Phosphatidylserines; D012795:Sialoglycoproteins