Abstract
Publisher Summary This chapter discusses the regulation of red cell membrane skeleton organization. The principal associations responsible for maintaining the integrity of the erythrocyte-membrane skeleton have been known and characterized for some time. The membrane skeleton is an interconnected network of proteins whose major constituents are spectrin, F-actin, band 4.1, and band 4.9. The spectrin molecules that are composed of two nonidentical polypeptide chains (α and β) exist principally in the form of α 2 β 2 tetramers. The protein-denoted band 4.1 plays a central role in membrane skeletal organization. The best understood role of this multifunctional protein is to promote or strengthen the association between spectrin and F-actin, one of the key skeletal interconnections. The proteins of the membrane skeleton that form a flexible two-dimensional lattice laminating the cytoplasmic membrane surface are responsible for the remarkable flexibility and resiliency of the red-cell membrane and for maintaining the shape of the normal red-blood cell. Abnormally shaped or fragile red cells that are characteristic of several types of inherited hemolytic anemias may, in some cases be the result of a genetic defect of one of the major membrane skeletal proteins.
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