Interaction of a Peripheral Protein of the Erythrocyte Membrane, Band 4.1, with Phosphatidylserine‐Containing Liposomes and Erythrocyte Inside‐Out Vesicles

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Abstract
Interactions of band 4,1 with mixed phospholipid membranes [phosphatidylserine (PS), phosphatidylethanolamine, phosphatidylcholine, etc.] and [human] erythrocyte inside-out vesicles were studied. Band 4.1 showed a higher affinity to PS-containing membranes. The amount of binding to PS-containing liposomes was larger than that to PS-lacking liposomes. The amount of binding to inside-out vesicles did not change significantly on a protease treatment of the vesicles. The amount of band 4.1 bound on inside-out vesicles decreased on PS-decarboxylase treatment of the vesicles. Ca2+ acted inhibitory to the binding of 4.1. Band 4.1 together with PS-containing vesicles but not with PS-lacking vesicles induced gelation of spectrin-actin copolymer solution. Ca2+ inhibited the gelation. Fluorescence energy transfer from PS-containing vesicles to band 4.1 was larger than that from PS-lacking vesicles. Band 4.1 caused a marked release of tempocholine from preloaded PS-containing liposomes but not from PS-lacking liposomes. The release was larger from liposomes containing more PS. Ca2+ was inhibitory to the tempocholine release. Band 4.1 may provide another anchoring site for the cytoskeletal spectrin-actin network to PS domains in the inner layer of erythrocyte membrane. This anchoring may be involved in functional regulation since the interaction causes the membrane permeability change that is dependent on Ca2+.

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