Effect of interfacial pressure on the binding and phospholipase A2 activity of recombinant human lecithin-cholesterol acyltransferase.
We examined the effect of surface pressure on the interfacial binding and phospholipase A2 activity of lecithin-cholesterol acyltransferase. The enzyme bound to phosphatidylcholine monolayers with an apparent dissociation constant of 1.5 nM was excluded from the interface at pressures > 29 mN/m and exhibited maximal phospholipase activity at pressures between 29-28 mN/m. These data suggest that lipoprotein surface pressure may regulate lecithin-cholesterol acyltransferase activity in vivo.
Weinberg
R B
RB
Department of Internal Medicine, Bowman Gray School of Medicine, Winston-Salem, North Carolina 27257-1048, USA.
Jones
J B
JB
Pritchard
P H
PH
Lacko
A G
AG
D006801:Humans; D006868:Hydrolysis; D006874:Hydrostatic Pressure; D008567:Membranes, Artificial; D007862:Phosphatidylcholine-Sterol O-Acyltransferase / Q000378:metabolism*; D010713:Phosphatidylcholines / Q000378:metabolism; D010741:Phospholipases A / Q000378:metabolism*; D054467:Phospholipases A2; D011994:Recombinant Proteins / Q000378:metabolism; D013499:Surface Properties
D008567:Membranes, Artificial; D010713:Phosphatidylcholines; D011994:Recombinant Proteins; D007862:Phosphatidylcholine-Sterol O-Acyltransferase; D010741:Phospholipases A; D054467:Phospholipases A2