Complex effects of papain on function and inhibitor sensitivity of the red cell anion exchanger AE1 suggest the presence of different transport subsites.

Band 3 (AE1), the anion exchanger of the human erythrocyte membrane, mediates not only fluxes of small hydrophilic anions (e.g., chloride, oxalate), but also the flip-flop of long-chain amphiphilic anions (e.

Chemical and physical in vitro alterations of the erythrocyte membrane: a model for its pathophysiological states?

Plasmodia induce conspicuous structural and functional changes in the erythrocyte membrane. Besides the insertion and apposition of 'xenoproteins', and alterations of lipid composition (fatty acid pattern) and dynamics (transbilayer mobility and disposition of phospholipids, or related probes), new permeation pathways (NPP) are formed, which are still ill-defined in terms of their molecular origin. A remarkable ion selectivity and a high and complete sensitivity of the NPP to inhibitors indicate a rather specific nature.

Extensive electroporation abolishes experimentally induced shape transformations of erythrocytes: a consequence of phospholipid symmetrization?

As shown in earlier work (M.M. Henszen et al.

Passive transmembrane redistributions of phospholipids as a determinant of erythrocyte shape change. Studies on electroporated cells.

Echinocytes formed from discocytic erythrocytes by electric field pulses at 0 degree C return to the discoytic shape upon incubation at 37 degrees C and subsequently turn into stomatocytes. Active and passive components of phospholipid translocation are involved in this shape recovery. Following low-field-strength pulses (5 kV cm-1), shape recovery is fully suppressed by ATPase inhibitors, such as vanadate.

Band 3-mediated flip-flop and phosphatase-catalyzed cleavage of a long-chain alkyl phosphate anion in the human erythrocyte membrane.

In pursuit of the characterization of the recently discovered flippase mode of operation of the anion transporter (band 3, AE1) of the human erythrocyte membrane, the transbilayer translocation (flip) of a fluorescently labeled, membrane-intercalated long-chain alkyl phosphate, 10-(alpha-napthyl)-1-decyl-phosphate (NDP) was investigated. In contrast to the alkyl sulfonates and esters of phosphatidic acid studied as yet, NDP moves exclusively via band 3. NDP is, however, dephosphorylated at the inner membrane surface by a cytoplasmic phosphatase likely to interact specifically with endofacial membrane structures of the erythrocyte.