High affinity Concanavalin A binding to sterol-depleted L cells.

Authors

J D. Marshall
H J. Heiniger

Document Type

Article

Publication Date

1979

Keywords

Cell-Membrane: me, Cholesterol, Concanavalin-A: me, Culture-Media, Hydroxycholesterols, L-Cells, Membrane-Lipids: ph, Mevalonic-Acid, Mice, Sterols: ph

First Page

539

Last Page

550

JAX Source

J-Cell-Physiol. 1979 Sep; 100(3):539-50.

Abstract

Binding of Concanavalin A to mouse L cells which were grown in serum free, chemically defined medium and depleted of their membrane sterol by blocking their de novo sterol synthesis was investigated. Kinetic analysis of binding data implied positive cooperativity, with two different affinities for Con A, in both experimental and control cultures. The amount of Con A bound to the cell surface at saturation was approximately 0.5 picomoles per mg cellular protein in controls and approximately 1.0 picomoles per mg cellular protein in 25-hydroxycholesterol treated cultures (which had a reduced sterol concentration of up to 50% in their plasma membranes). This phenomenon was reversed when cholesterol or mevalonate was added to the inhibited cultures to compensate for their inability to synthesize sterol. Our findings indicate that lectin binding to specific glycoprotein receptors is influenced by membrane lipid composition.

Recommended Citation

Marshall JD, Heiniger HJ. High affinity Concanavalin A binding to sterol-depleted L cells. J-Cell-Physiol. 1979 Sep; 100(3):539-50.