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Structural organisation of band 3 in Melanesian ovalocytes |
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| Authors: | Leann Tilley Robert A McPherson Graham L Jones William H Sawyer |
| Institution: | 1. Department of Biochemistry, La Trobe University, Bundoora, Vic., Australia;2. Department of Science, Technology, Mathematics and Engineering, University of New England, Armidale, NSW, Australia;3. Department of Biochemistry, University of Melbourne, Parkville, Vic., Australia |
| Abstract: | The diffusional freedom of human erythrocyte band 3 (anion exchanger 1) has been measured in membranes from normacytic and ovalocytic erythrocytes. A dramatic reorganisation of band 3 in the ovalocyte membranes is indicated by a markedly restricted rotational mobility. Extraction of spectrin from erythrocyte membranes had no effect on normocyte band 3 mobility, but partially relieved the restrictions on ovalocyte band 3 mobility. Further removal of ankyrin and band 4.2 resulted in an increase in the rotational mobility of both ovalocyte and normocyte band 3 to similar levels. The results suggest that the molecular basis of the unusual shape and decreased deformability of ovalocytes resides in an altered interaction of band 3 with one or more of the peripheral proteins. We present a model which illustrates a possible role for band 3 aggregation in controlling erythrocyte deformability. |
| Keywords: | Rotational diffusion Erythrocyte membrane Band 3 Time-resolved phosphorescence anisotropy Ovalocyte Erythrocyte morphology SDS-PAGE sodium dodecylsulphate-polyacrylamide gel electrophoresis CAPS 3-(cyclohexylamino)-1-propanesulfonic acid TPCK L-1-tosyl-2-phenylmethyl chloromethyl ketone |
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