Effect of anti-spectrin antibody and ATP on deformability of resealed erythrocyte membranes.
Deformability of resealed erythrocyte membranes was measured by using an ektacytometer. Divalent anti-spectrin antibody, but not monovalent anti-spectrin Fab fragments, decreased membrane deformability. Membranes resealed with MgATP were more deformable than those without MgATP. Exogenous alkaline phosphatase, which dephosphorylates spectrin, decreased membrane deformability. These results suggest that spectrin is an essential component of the system that determines erythrocyte deformability. They are consistent with the view that the role of ATP in membrane deformability is mediated through phosphorylation of the spectrin.
D000255:Adenosine Triphosphate / Q000494:pharmacology*; D000469:Alkaline Phosphatase / Q000494:pharmacology; D000906:Antibodies; D004910:Erythrocyte Membrane / Q000187:drug effects*; D004912:Erythrocytes / Q000187:drug effects*; D006801:Humans; D007140:Immunoglobulin Fab Fragments; D008565:Membrane Proteins / Q000276:immunology*; D013049:Spectrin / Q000276:immunology*
D000906:Antibodies; D007140:Immunoglobulin Fab Fragments; D008565:Membrane Proteins; D013049:Spectrin; D000255:Adenosine Triphosphate; D000469:Alkaline Phosphatase