Erythrocyte membrane deformability and stability: two distinct membrane properties that are independently regulated by skeletal protein associations

Skeletal proteins play an important role in determining erythrocyte membrane biophysical properties. To study whether membrane deformability and stability are regulated by the same or different skeletal protein interactions, we measured these two properties, by means of ektacytometry, in biochemical...

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Format: Online
Language:English
Published: The Rockefeller University Press 1986
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2113818/
id pubmed-2113818
recordtype oai_dc
spelling pubmed-21138182008-05-01 Erythrocyte membrane deformability and stability: two distinct membrane properties that are independently regulated by skeletal protein associations Articles Skeletal proteins play an important role in determining erythrocyte membrane biophysical properties. To study whether membrane deformability and stability are regulated by the same or different skeletal protein interactions, we measured these two properties, by means of ektacytometry, in biochemically perturbed normal membranes and in membranes from individuals with known erythrocyte abnormalities. Treatment with 2,3-diphosphoglycerate resulted in membranes with decreased deformability and decreased stability, whereas treatment with diamide produced decreased deformability but increased stability. N- ethylmaleimide induced time-dependent changes in membrane stability. Over the first minute, the stability increased; but with continued incubation, the membranes became less stable than control. Meanwhile, the deformability of these membranes decreased with no time dependence. Biophysical measurements were also carried out on pathologic erythrocytes. Membranes from an individual with hereditary spherocytosis and a defined abnormality in spectrin-protein 4.1 association showed decreased stability but normal deformability. In a family with hereditary elliptocytosis and an abnormality in spectrin self-association, the membranes had decreased deformability and stability. Finally, membranes from several individuals with Malaysian ovalocytosis had decreased deformability but increased stability. Our data from both pathologic membranes and biochemically perturbed membranes show that deformability and stability change with no fixed relationship to one another. These findings imply that different skeletal protein interactions regulate membrane deformability and stability. In light of these data, we propose a model of the role of skeletal protein interactions in deformability and stability. The Rockefeller University Press 1986-08-01 /pmc/articles/PMC2113818/ /pubmed/3733870 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
repository_type Open Access Journal
institution_category Foreign Institution
institution US National Center for Biotechnology Information
building NCBI PubMed
collection Online Access
language English
format Online
title Erythrocyte membrane deformability and stability: two distinct membrane properties that are independently regulated by skeletal protein associations
spellingShingle Erythrocyte membrane deformability and stability: two distinct membrane properties that are independently regulated by skeletal protein associations
title_short Erythrocyte membrane deformability and stability: two distinct membrane properties that are independently regulated by skeletal protein associations
title_full Erythrocyte membrane deformability and stability: two distinct membrane properties that are independently regulated by skeletal protein associations
title_fullStr Erythrocyte membrane deformability and stability: two distinct membrane properties that are independently regulated by skeletal protein associations
title_full_unstemmed Erythrocyte membrane deformability and stability: two distinct membrane properties that are independently regulated by skeletal protein associations
title_sort erythrocyte membrane deformability and stability: two distinct membrane properties that are independently regulated by skeletal protein associations
description Skeletal proteins play an important role in determining erythrocyte membrane biophysical properties. To study whether membrane deformability and stability are regulated by the same or different skeletal protein interactions, we measured these two properties, by means of ektacytometry, in biochemically perturbed normal membranes and in membranes from individuals with known erythrocyte abnormalities. Treatment with 2,3-diphosphoglycerate resulted in membranes with decreased deformability and decreased stability, whereas treatment with diamide produced decreased deformability but increased stability. N- ethylmaleimide induced time-dependent changes in membrane stability. Over the first minute, the stability increased; but with continued incubation, the membranes became less stable than control. Meanwhile, the deformability of these membranes decreased with no time dependence. Biophysical measurements were also carried out on pathologic erythrocytes. Membranes from an individual with hereditary spherocytosis and a defined abnormality in spectrin-protein 4.1 association showed decreased stability but normal deformability. In a family with hereditary elliptocytosis and an abnormality in spectrin self-association, the membranes had decreased deformability and stability. Finally, membranes from several individuals with Malaysian ovalocytosis had decreased deformability but increased stability. Our data from both pathologic membranes and biochemically perturbed membranes show that deformability and stability change with no fixed relationship to one another. These findings imply that different skeletal protein interactions regulate membrane deformability and stability. In light of these data, we propose a model of the role of skeletal protein interactions in deformability and stability.
publisher The Rockefeller University Press
publishDate 1986
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2113818/
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