Modulation of the activities of membrane enzymes by cereal grain resorcinolic lipids.
Resorcinolic lipids, amphiphilic compounds from cereal grains show strong effects upon the activity of membrane enzymes. The concentrations for 50% inhibition of erythrocyte membrane acetylcholinesterase were in the range of 18-90 microM and were dependent on the length of the aliphatic side chain of the homologue and on the modification of hydroxyl groups in the benzene ring. Sulfonation of OH groups resulted in a drastic decrease of the inhibitory potency. The effect of resorcinolic lipids on the activity of Ca2+(calmodulin)-ATPase was the opposite. Up to concentrations of 50 microM alk(en)ylresorcinols stimulated the activity of this enzyme and only slight inhibition (approx. 30%) was observed above 100 microM. The results suggest that the effect of resorcinolic lipids might depend on their ability to alter the bilayer properties. Most probably these compounds decrease the mobility of membrane phospholipid molecules.
Kozubek
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Instytut Biochemii Uniwersytetu Wrocławskiego, Wrocław, Poland.
Nietubyc
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Sikorski
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AF
D000110:Acetylcholinesterase / Q000097:blood*; D002800:Cholinesterase Inhibitors / Q000302:isolation & purification / Q000494:pharmacology*; D002523:Edible Grain; D004910:Erythrocyte Membrane / Q000201:enzymology; D006801:Humans; D007700:Kinetics; D008962:Models, Theoretical; D012118:Resorcinols / Q000302:isolation & purification / Q000494:pharmacology*; D013329:Structure-Activity Relationship; D013816:Thermodynamics
D002800:Cholinesterase Inhibitors; D012118:Resorcinols; D000110:Acetylcholinesterase