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Biophys J, December 1999, p. 3085-3095, Vol. 77, No. 6
MRC Unit of Muscle and Cell Motility, Randall Institute, Kings College London, 26-29 Drury Lane, London WC2B 5RL, United Kingdom
We have used optical tweezers to study the elasticity of
red cell membranes; force was applied to a bead attached to a
permeabilized spherical ghost and the force-extension relation was
obtained from the response of a second bead bound at a diametrically
opposite position. Interruption of the skeletal network by dissociation of spectrin tetramers or extraction of the actin junctions engendered a
fourfold reduction in stiffness at low applied force, but only a
twofold change at larger extensions. Proteolytic scission of the
ankyrin, which links the membrane skeleton to the integral membrane
protein, band 3, induced a similar effect. The modified, unlike the
native membranes, showed plastic relaxation under a prolonged stretch.
Flaccid giant liposomes showed no measurable elasticity. Our
observations indicate that the elastic character is at least as much a
consequence of the attachment of spectrin as of a continuous
membrane-bound network, and they offer a rationale for formation of
elliptocytes in genetic conditions associated with membrane-skeletal
perturbations. The theory of Parker and Winlove for elastic deformation
of axisymmetric shells (accompanying paper) allows us to determine the
function BH2 for the spherical
saponin-permeabilized ghost membranes (where B is the
bending modulus and H the shear modulus); taking the literature value of 2 × 10
19 Nm for
B, H then emerges as 2 × 106 Nm1. This is an order of magnitude
higher than the value reported for intact cells from micropipette
aspiration. Reasons for the difference are discussed.
Biophys J, December 1999, p. 3085-3095, Vol. 77, No. 6
© 1999 by the Biophysical Society 0006-3495/99/12/3085/11 $2.00
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