Red Blood Cell Deformability Is Expressed by a Set of Interrelated Membrane Proteins

Red blood cell (RBC) deformability, expressing their ability to change their shape, allows them to minimize their resistance to flow and optimize oxygen delivery to the tissues. RBC with reduced deformability may lead to increased vascular resistance, capillary occlusion, and impaired perfusion and...

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Main Authors: Gregory Barshtein, Alexander Gural, Dan Arbell, Refael Barkan, Leonid Livshits, Ivana Pajic-Lijakovic, Saul Yedgar
Format: Article
Language:English
Published: MDPI AG 2023-08-01
Series:International Journal of Molecular Sciences
Subjects:
Online Access:https://www.mdpi.com/1422-0067/24/16/12755
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author Gregory Barshtein
Alexander Gural
Dan Arbell
Refael Barkan
Leonid Livshits
Ivana Pajic-Lijakovic
Saul Yedgar
author_facet Gregory Barshtein
Alexander Gural
Dan Arbell
Refael Barkan
Leonid Livshits
Ivana Pajic-Lijakovic
Saul Yedgar
author_sort Gregory Barshtein
collection DOAJ
description Red blood cell (RBC) deformability, expressing their ability to change their shape, allows them to minimize their resistance to flow and optimize oxygen delivery to the tissues. RBC with reduced deformability may lead to increased vascular resistance, capillary occlusion, and impaired perfusion and oxygen delivery. A reduction in deformability, as occurs during RBC physiological aging and under blood storage, is implicated in the pathophysiology of diverse conditions with circulatory disorders and anemias. The change in RBC deformability is associated with metabolic and structural alterations, mostly uncharacterized. To bridge this gap, we analyzed the membrane protein levels, using mass spectroscopy, of RBC with varying deformability determined by image analysis. In total, 752 membrane proteins were identified. However, deformability was positively correlated with the level of only fourteen proteins, with a highly significant inter-correlation between them. These proteins are involved in membrane rafting and/or the membrane–cytoskeleton linkage. These findings suggest that the reduction of deformability is a programmed (not arbitrary) process of remodeling and shedding of membrane fragments, possibly mirroring the formation of extracellular vesicles. The highly significant inter-correlation between the deformability-expressing proteins infers that the cell deformability can be assessed by determining the level of a few, possibly one, of them.
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spelling doaj.art-d5e5c76b31da4e6b99d18fef0681d4392023-11-19T01:28:53ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672023-08-0124161275510.3390/ijms241612755Red Blood Cell Deformability Is Expressed by a Set of Interrelated Membrane ProteinsGregory Barshtein0Alexander Gural1Dan Arbell2Refael Barkan3Leonid Livshits4Ivana Pajic-Lijakovic5Saul Yedgar6Department of Biochemistry, The Faculty of Medicine, The Hebrew University of Jerusalem, Jerusalem 9112001, IsraelBlood Bank, Hadassah University Hospital, Jerusalem 9112001, IsraelPediatric Surgery, Hadassah University Hospital, Jerusalem 9112001, IsraelDepartment of Digital Medical Technologies, Holon Institute of Technology, Holon 5810201, IsraelRed Blood Cell Research Group, Vetsuisse Faculty, Institute of Veterinary Physiology, University of Zurich, 8057 Zürich, SwitzerlandDepartment of Chemical Engineering, University of Belgrade, 11120 Belgrade, SerbiaDepartment of Biochemistry, The Faculty of Medicine, The Hebrew University of Jerusalem, Jerusalem 9112001, IsraelRed blood cell (RBC) deformability, expressing their ability to change their shape, allows them to minimize their resistance to flow and optimize oxygen delivery to the tissues. RBC with reduced deformability may lead to increased vascular resistance, capillary occlusion, and impaired perfusion and oxygen delivery. A reduction in deformability, as occurs during RBC physiological aging and under blood storage, is implicated in the pathophysiology of diverse conditions with circulatory disorders and anemias. The change in RBC deformability is associated with metabolic and structural alterations, mostly uncharacterized. To bridge this gap, we analyzed the membrane protein levels, using mass spectroscopy, of RBC with varying deformability determined by image analysis. In total, 752 membrane proteins were identified. However, deformability was positively correlated with the level of only fourteen proteins, with a highly significant inter-correlation between them. These proteins are involved in membrane rafting and/or the membrane–cytoskeleton linkage. These findings suggest that the reduction of deformability is a programmed (not arbitrary) process of remodeling and shedding of membrane fragments, possibly mirroring the formation of extracellular vesicles. The highly significant inter-correlation between the deformability-expressing proteins infers that the cell deformability can be assessed by determining the level of a few, possibly one, of them.https://www.mdpi.com/1422-0067/24/16/12755red blood cellsRBC deformabilitymembrane proteinslipid raftsmembrane vesiclesmembrane remodeling
spellingShingle Gregory Barshtein
Alexander Gural
Dan Arbell
Refael Barkan
Leonid Livshits
Ivana Pajic-Lijakovic
Saul Yedgar
Red Blood Cell Deformability Is Expressed by a Set of Interrelated Membrane Proteins
International Journal of Molecular Sciences
red blood cells
RBC deformability
membrane proteins
lipid rafts
membrane vesicles
membrane remodeling
title Red Blood Cell Deformability Is Expressed by a Set of Interrelated Membrane Proteins
title_full Red Blood Cell Deformability Is Expressed by a Set of Interrelated Membrane Proteins
title_fullStr Red Blood Cell Deformability Is Expressed by a Set of Interrelated Membrane Proteins
title_full_unstemmed Red Blood Cell Deformability Is Expressed by a Set of Interrelated Membrane Proteins
title_short Red Blood Cell Deformability Is Expressed by a Set of Interrelated Membrane Proteins
title_sort red blood cell deformability is expressed by a set of interrelated membrane proteins
topic red blood cells
RBC deformability
membrane proteins
lipid rafts
membrane vesicles
membrane remodeling
url https://www.mdpi.com/1422-0067/24/16/12755
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