PMID: 6109559Oct 1, 1980Paper

Ordering of bulk membrane lipid or protein promotes activity of plasma membrane Mg2+ATPase

Canadian Journal of Biochemistry
J R Riordan

Abstract

Treatment of liver plasma membranes with phospholipase A2 or high doses of concanavalin A enhances the activity of Mg2+ATPase assayed at temperatures greater than 30 degrees C. The effects of the two treatments are not additive. Both the removal of phospholipids and binding of the lectin increase the degree of polarization of fluorescence of the lipid-soluble fluorophores, diphenylhexatriene and beta-parinaric acid, suggesting that decreased lipid fluidity may activate Mg2+-ATPase. In fact modification of lipid fluidity by reconstitution of phospholipase-treated membranes with phosphatidylcholines of defined fatty acid composition or by addition of cis-vaccenic acid showed a strong inverse correlation between Mg2+ATPase activity and lipid fluidity as monitored by fluorescence polarization. However, despite the ability of concanavalin A to nonspecifically order membrane lipid, its effect on Mg2+ATPase is apparently not mediated in this manner because other enzyme-activating lectins such as Ricinus communis agglutinin and wheat germ agglutinin are without effect on lipid fluidity. The facts that lectins of lower valency than tetravalent native concanavalin A such as divalent succinyl concanavalin A are far less effective in activ...Continue Reading

Citations

Dec 1, 1985·Archives of Biochemistry and Biophysics·T J BeelerS Lee
Jan 1, 1987·Journal of Pharmaceutical Sciences·G M GoldenR O Potts
Jan 1, 1984·Hepatology : Official Journal of the American Association for the Study of Liver Diseases·D Schachter
Jan 1, 1988·Progress in Biophysics and Molecular Biology·N S Dhalla, D Zhao
Feb 15, 1983·Biochimica Et Biophysica Acta·J M LamersN S Dhalla
Jan 1, 1989·Archives of Biochemistry and Biophysics·D Y ZhaoN S Dhalla

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