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. 1990 Nov 1;271(3):831–834. doi: 10.1042/bj2710831

Restricted diffusion of integral membrane proteins and polyphosphoinositides leads to their depletion in microvesicles released from human erythrocytes.

C Hagelberg 1, D Allan 1
PMCID: PMC1149640  PMID: 2173910

Abstract

The protein and phospholipid composition of microvesicles released from normal human erythrocytes after ATP depletion, on aging or by treatment with merocyanine 540, dimyristoyl phosphatidylcholine or Ca2+/ionophore A23187 has been compared with the composition of the original cell membrane. It has been shown that these microvesicles are depleted of band 3, glycophorin and phosphatidylinositol 4,5-bisphosphate relative to phospholipid by 40% or more. These data are interpreted to mean that less than half of these membrane components are free to diffuse laterally in the lipid bilayer. Acetylcholinesterase was found to be enriched 2-3-fold in microvesicles, possibly because the removal of non-diffusing proteins from the vesiculating region of the lipid bilayer allows more space for freely diffusing proteins like acetylcholinesterase to enter the microvesicle membrane.

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Selected References

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