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J. Biol. Chem., Vol. 277, Issue 35, 31796-31800, August 30, 2002
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From the The red cell membrane derives its elasticity and
resistance to mechanical stresses from the membrane skeleton, a network
composed of spectrin tetramers. These are formed by the head-to-head
association of pairs of heterodimers attached at their ends to
junctional complexes of several proteins. Here we examine the dynamics
of the spectrin dimer-dimer association in the intact membrane. We show
that univalent fragments of spectrin, containing the dimer self-association site, will bind to spectrin on the membrane and thereby disrupt the continuity of the protein network. This results in
impairment of the mechanical stability of the membrane. When, moreover,
the cells are subjected to a continuous low level of shear, even at
room temperature, the incorporation of the fragments and the consequent
destabilization of the membrane are greatly accentuated. It follows
that a modest shearing force, well below that experienced by the red
cell in the circulation, is sufficient to sever dimer-dimer links in
the network. Our results imply 1) that the membrane accommodates the
enormous distortions imposed on it during the passage of the cell
through the microvasculature by means of local dissociation of spectrin
tetramers to dimers, 2) that the network in situ is in a
dynamic state and undergoes a "breathing" action of tetramer
dissociation and re-formation.
Shear-Response of the Spectrin Dimer-Tetramer Equilibrium in the
Red Blood Cell Membrane*
§,
,, and Red Cell Physiology Laboratory, The New York
Blood Center, New York, New York 10021, the ¶ INSERM U409, Faculte
de Medecine Bichat, 75870 Paris cedex 18, France, the Life
Science Division, Lawrence Berkeley National Laboratory, Berkeley,
California 94720, and the ** Medical Council Cell Biophysics
Unit, The Randall Center, King's College, New Hunt House, London
SE1 IUL, United Kingdom
*
This work was supported in part by National Institutes of
Health Grants DK 26263 and DK 32094 (to N. M.).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.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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