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J. Biol. Chem., Vol. 276, Issue 25, 22223-22230, June 22, 2001
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From the Department of Chemistry, Purdue University,
West Lafayette, Indiana 47907
The band 3-ankyrin-spectrin bridge and the
glycophorin C-protein 4.1-spectrin/actin bridge constitute the two
major tethers between the erythrocyte membrane and its spectrin
skeleton. Although a structural requirement for the band 3-ankyrin
bridge is well established, the contribution of the glycophorin
C-protein 4.1 bridge to red cell function remains to be defined. In
order to explore this latter bridge further, we have identified and/or characterized five stimuli that sever the linkage in intact
erythrocytes and have examined the impact of this rupture on membrane
mechanical properties. We report here that elevation of cytosolic
2,3-bisphosphoglycerate, an increase in intracellular
Ca2+, removal of cell O2, a decrease in
intracellular pH, and activation of erythrocyte protein kinase C all
promote dissociation of protein 4.1 from glycophorin C, leading to
reduced retention of glycophorin C in detergent-extracted
spectrin/actin skeletons. Significantly, where mechanical studies could
be performed, we also observe that rupture of the membrane-to-skeleton
bridge has little or no impact on the mechanical properties of the
cell, as assayed by ektacytometry and nickel mesh filtration. We,
therefore, suggest that, although regulation of the glycophorin
C-protein 4.1-spectrin/actin bridge likely occurs physiologically, the
role of the tether and the associated regulatory changes remain to
be established.
Regulation of the Glycophorin C-Protein 4.1 Membrane-to-Skeleton
Bridge and Evaluation of Its Contribution to Erythrocyte Membrane
Stability*
*
This work was supported in part by National Institutes of
Health Grant GM24417.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.: 765-494-5273;
Fax: 765-494-0239; E-mail: plow@purdue.edu.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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