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Evidence that red blood cell protein p55 may participate in the
skeleton-membrane linkage that involves protein 4.1 and glycophorin C
N Alloisio, N Dalla Venezia, A Rana, K Andrabi, P Texier, F Gilsanz, JP Cartron, J Delaunay and AH Chishti
CNRS URA 1171, Faculte de Medecine Grange-Blanche, Lyon, France.
Human erythrocyte p55 is a peripheral membrane protein that contains three
distinct domains in its primary structure: an N-terminal domain, an SH3
motif, and a C-terminal guanylate kinase domain. We used naturally mutated
red blood cells (RBCs) with primary genetic defects resulting in the
absence of protein 4.1 (4.1[-] hereditary elliptocytosis) or glycophorin C
(Leach elliptocytosis). The absence of either protein was associated with
the absence of p55. On a stoichiometric basis, the reduction in glycophorin
C (about 80%) was concomitant to the lack of p55 in RBCs devoid of protein
4.1. Similarly, the reduction of protein 4.1 (about 20%) was equivalent to
the absence of p55 in RBCs devoid of glycophorin C. These correlations
suggest that p55 is associated, in precise proportions, with the protein
4.1-glycophorin-C complex, linking the skeleton and the membrane. The
protein 4.1-glycophorin-C cross-bridge is known to be critically important
for the stability and mechanical properties of human RBC plasma membrane.
Because isoforms of protein 4.1, glycophorin C, and p55 exist in many
tissues, these results provide evidence of a linkage between the skeleton
and the membrane that may have implications in many nonerythroid cells.
Volume 82,
Issue 4,
pp. 1323-1327,
08/15/1993
Copyright © 1993 by The American Society of Hematology
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