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Biophys J, March 1999, p. 1153-1165, Vol. 76, No. 3

Calculation of a Gap Restoration in the Membrane Skeleton of the Red Blood Cell: Possible Role for Myosin II in Local Repair

C. Cibert,* G. Prulière,# C. Lacombe,§ C. Deprette, and R. Cassoly

 *Laboratoire de Biologie du Développement, Institut Jacques Monod, UMR 7592, CNRS, Universités Paris VI et Paris VII, F-75005 Paris;  #URA671 CNRS Station de Zoologie Marine, BP28 F-06234 Villefranche-sur-Mer Cedex;  §Laboratoire de Bioactivation des Peptides, Institut Jacques Monod, UMR 7592, CNRS, Universités Paris VI et Paris VII, F-75005 Paris; and  Laboratoire de Biologie Cellulaire des Membranes, Institut Jacques Monod, UMR 7592, CNRS, Universités Paris VI et Paris VII, F-75005 Paris, France

Human red blood cells contain all of the elements involved in the formation of nonmuscle actomyosin II complexes (V. M. Fowler. 1986. J. Cell. Biochem. 31:1-9; 1996. Curr. Opin. Cell Biol. 8:86-96). No clear function has yet been attributed to these complexes. Using a mathematical model for the structure of the red blood cell spectrin skeleton (M. J. Saxton. 1992. J. Theor. Biol. 155:517-536), we have explored a possible role for myosin II bipolar minifilaments in the restoration of the membrane skeleton, which may be locally damaged by major mechanical or chemical stress. We propose that the establishment of stable links between distant antiparallel actin protofilaments after a local myosin II activation may initiate the repair of the disrupted area. We show that it is possible to define conditions in which the calculated number of myosin II minifilaments bound to actin protofilaments is consistent with the estimated number of myosin II minifilaments present in the red blood cells. A clear restoration effect can be observed when more than 50% of the spectrin polymers of a defined area are disrupted. It corresponds to a significant increase in the spectrin density in the protein free region of the membrane. This may be involved in a more complex repair process of the red blood cell membrane, which includes the vesiculation of the bilayer and the compaction of the disassembled spectrin network.

Biophys J, March 1999, p. 1153-1165, Vol. 76, No. 3
© 1999 by the Biophysical Society   0006-3495/99/03/1153/13  $2.00




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Copyright © 1999 by the Biophysical Society.