Interaction of lens crystallins with lipid vesicles.
Previous studies have demonstrated that alpha-crystallin, but not beta or gamma-crystallin, can bind to lens membrane in a specific and saturable manner. To determine which components of the lens membrane might be involved in this interaction, each of these crystallins was incubated with reconstituted vesicles containing either phosphatidylethanolamine (PE), phosphatidylcholine (PC), or sphingomyelin (SPH). Alpha-crystallin, but not beta- or gamma-crystallin, bound to these vesicles in a saturable manner, in similar amounts as lens membrane. Together, these results suggest that the lipid moiety of the lens membrane may be involved in recognition of the alpha-crystallin molecule.
Ifeanyi
F
F
Division of Biology, Kansas State University, Manhattan 66506.
Takemoto
L
L
D000818:Animals; D015153:Blotting, Western; D002417:Cattle; D002462:Cell Membrane / Q000378:metabolism; D003459:Crystallins / Q000378:metabolism*; D007904:Lens Cortex, Crystalline / Q000378:metabolism*; D050356:Lipid Metabolism; D010713:Phosphatidylcholines / Q000378:metabolism; D010714:Phosphatidylethanolamines / Q000378:metabolism; D013109:Sphingomyelins / Q000378:metabolism
D003459:Crystallins; D010713:Phosphatidylcholines; D010714:Phosphatidylethanolamines; D013109:Sphingomyelins