Abstract
Increasing the cytoplasmic calcium concentration of human erythrocytes with ionophore A23187 drives the transformation from diskocyte to echinocyte morphology1. This transformation is closely linked to the intracellular ATP level, which drops when calcium is introduced across the membrane2,3. The echinocyte morphology reverts to the diskocyte after restoration of normal ATP and calcium levels4,5. ATP control of cell morphology is thought to depend on the action of a protein kinase and phosphatase which reversibly modify the membrane cytoskeleton6–9. The cytoskeleton in turn is in contact with the outside membrane surface via transmembrane proteins10–11. We show here that binding of the lectin, wheat-germ agglutinin (WGA), to the erythrocyte membrane surface blocks the morphological conversions diskocyte ⇄ echinocyte in both directions. WGA seems to work via a mechanism involving the transmembrane glycoprotein, glycophorin13,14.
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Anderson, R., Lovrien, R. Erythrocyte membrane sidedness in lectin control of the Ca2+–A23187-mediated diskocyte ⇄ echinocyte conversion. Nature 292, 158–161 (1981). https://doi.org/10.1038/292158a0
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DOI: https://doi.org/10.1038/292158a0
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