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Binding of human myeloperoxidase to red blood cells : Molecular targets and biophysical consequences at the plasma membrane level. / Gorudko, Irina V.; Sokolov, Alexey V.; Shamova, Ekaterina V.; Grigorieva, Daria V.; Mironova, Elena V.; Kudryavtsev, Igor V.; Gusev, Sergey A.; Gusev, Alexander A.; Chekanov, Andrey V.; Vasilyev, Vadim B.; Cherenkevich, Sergey N.; Panasenko, Oleg M.; Timoshenko, Alexander V.

In: Archives of Biochemistry and Biophysics, Vol. 591, 01.02.2016, p. 87-97.

Research output: Contribution to journal › Article › peer-review

Harvard

Gorudko, IV, Sokolov, AV, Shamova, EV, Grigorieva, DV, Mironova, EV, Kudryavtsev, IV, Gusev, SA, Gusev, AA, Chekanov, AV, Vasilyev, VB, Cherenkevich, SN, Panasenko, OM & Timoshenko, AV 2016, 'Binding of human myeloperoxidase to red blood cells: Molecular targets and biophysical consequences at the plasma membrane level', Archives of Biochemistry and Biophysics, vol. 591, pp. 87-97. https://doi.org/10.1016/j.abb.2015.12.007

APA

Gorudko, I. V., Sokolov, A. V., Shamova, E. V., Grigorieva, D. V., Mironova, E. V., Kudryavtsev, I. V., Gusev, S. A., Gusev, A. A., Chekanov, A. V., Vasilyev, V. B., Cherenkevich, S. N., Panasenko, O. M., & Timoshenko, A. V. (2016). Binding of human myeloperoxidase to red blood cells: Molecular targets and biophysical consequences at the plasma membrane level. Archives of Biochemistry and Biophysics, 591, 87-97. https://doi.org/10.1016/j.abb.2015.12.007

Vancouver

Gorudko IV, Sokolov AV, Shamova EV, Grigorieva DV, Mironova EV, Kudryavtsev IV et al. Binding of human myeloperoxidase to red blood cells: Molecular targets and biophysical consequences at the plasma membrane level. Archives of Biochemistry and Biophysics. 2016 Feb 1;591:87-97. https://doi.org/10.1016/j.abb.2015.12.007

Author

Gorudko, Irina V. ; Sokolov, Alexey V. ; Shamova, Ekaterina V. ; Grigorieva, Daria V. ; Mironova, Elena V. ; Kudryavtsev, Igor V. ; Gusev, Sergey A. ; Gusev, Alexander A. ; Chekanov, Andrey V. ; Vasilyev, Vadim B. ; Cherenkevich, Sergey N. ; Panasenko, Oleg M. ; Timoshenko, Alexander V. / Binding of human myeloperoxidase to red blood cells : Molecular targets and biophysical consequences at the plasma membrane level. In: Archives of Biochemistry and Biophysics. 2016 ; Vol. 591. pp. 87-97.

BibTeX

@article{863dece8830c42e2be351c0e5b0cbbb0,
title = "Binding of human myeloperoxidase to red blood cells: Molecular targets and biophysical consequences at the plasma membrane level",
abstract = "Myeloperoxidase (MPO) is an oxidant-producing enzyme that can also bind to cellular surface proteins. We found that band 3 protein and glycophorins A and B were the key MPO-binding targets of human red blood cells (RBCs). The interaction of MPO with RBC proteins was mostly electrostatic in nature because it was inhibited by desialation, exogenic sialic acid, high ionic strength, and extreme pH. In addition, MPO failed to interfere with the lectin-induced agglutination of RBCs, suggesting a minor role of glycan-recognizing mechanisms in MPO binding. Multiple biophysical properties of RBCs were altered in the presence of native (i.e., not hypochlorous acid-damaged) MPO. These changes included transmembrane potential, availability of intracellular Ca2+, and lipid organization in the plasma membrane. MPO-treated erythrocytes became larger in size, structurally more rigid, and hypersensitive to acidic and osmotic hemolysis. Furthermore, we found a significant correlation between the plasma MPO concentration and RBC rigidity index in type-2 diabetes patients with coronary heart disease. These findings suggest that MPO functions as a mediator of novel regulatory mechanism in microcirculation, indicating the influence of MPO-induced abnormalities on RBC deformability under pathological stress conditions.",
keywords = "Cardiovascular diseases, Cell deformability, Erythrocytes, Lectin, Myeloperoxidase, Oxidative/halogenative stress",
author = "Gorudko, {Irina V.} and Sokolov, {Alexey V.} and Shamova, {Ekaterina V.} and Grigorieva, {Daria V.} and Mironova, {Elena V.} and Kudryavtsev, {Igor V.} and Gusev, {Sergey A.} and Gusev, {Alexander A.} and Chekanov, {Andrey V.} and Vasilyev, {Vadim B.} and Cherenkevich, {Sergey N.} and Panasenko, {Oleg M.} and Timoshenko, {Alexander V.}",
note = "Publisher Copyright: {\textcopyright} 2015 Elsevier Inc.",
year = "2016",
month = feb,
day = "1",
doi = "10.1016/j.abb.2015.12.007",
language = "English",
volume = "591",
pages = "87--97",
journal = "Archives of Biochemistry and Biophysics",
issn = "0003-9861",
publisher = "Elsevier",

}

RIS

TY - JOUR

T1 - Binding of human myeloperoxidase to red blood cells

T2 - Molecular targets and biophysical consequences at the plasma membrane level

AU - Gorudko, Irina V.

AU - Sokolov, Alexey V.

AU - Shamova, Ekaterina V.

AU - Grigorieva, Daria V.

AU - Mironova, Elena V.

AU - Kudryavtsev, Igor V.

AU - Gusev, Sergey A.

AU - Gusev, Alexander A.

AU - Chekanov, Andrey V.

AU - Vasilyev, Vadim B.

AU - Cherenkevich, Sergey N.

AU - Panasenko, Oleg M.

AU - Timoshenko, Alexander V.

N1 - Publisher Copyright: © 2015 Elsevier Inc.

PY - 2016/2/1

Y1 - 2016/2/1

N2 - Myeloperoxidase (MPO) is an oxidant-producing enzyme that can also bind to cellular surface proteins. We found that band 3 protein and glycophorins A and B were the key MPO-binding targets of human red blood cells (RBCs). The interaction of MPO with RBC proteins was mostly electrostatic in nature because it was inhibited by desialation, exogenic sialic acid, high ionic strength, and extreme pH. In addition, MPO failed to interfere with the lectin-induced agglutination of RBCs, suggesting a minor role of glycan-recognizing mechanisms in MPO binding. Multiple biophysical properties of RBCs were altered in the presence of native (i.e., not hypochlorous acid-damaged) MPO. These changes included transmembrane potential, availability of intracellular Ca2+, and lipid organization in the plasma membrane. MPO-treated erythrocytes became larger in size, structurally more rigid, and hypersensitive to acidic and osmotic hemolysis. Furthermore, we found a significant correlation between the plasma MPO concentration and RBC rigidity index in type-2 diabetes patients with coronary heart disease. These findings suggest that MPO functions as a mediator of novel regulatory mechanism in microcirculation, indicating the influence of MPO-induced abnormalities on RBC deformability under pathological stress conditions.

AB - Myeloperoxidase (MPO) is an oxidant-producing enzyme that can also bind to cellular surface proteins. We found that band 3 protein and glycophorins A and B were the key MPO-binding targets of human red blood cells (RBCs). The interaction of MPO with RBC proteins was mostly electrostatic in nature because it was inhibited by desialation, exogenic sialic acid, high ionic strength, and extreme pH. In addition, MPO failed to interfere with the lectin-induced agglutination of RBCs, suggesting a minor role of glycan-recognizing mechanisms in MPO binding. Multiple biophysical properties of RBCs were altered in the presence of native (i.e., not hypochlorous acid-damaged) MPO. These changes included transmembrane potential, availability of intracellular Ca2+, and lipid organization in the plasma membrane. MPO-treated erythrocytes became larger in size, structurally more rigid, and hypersensitive to acidic and osmotic hemolysis. Furthermore, we found a significant correlation between the plasma MPO concentration and RBC rigidity index in type-2 diabetes patients with coronary heart disease. These findings suggest that MPO functions as a mediator of novel regulatory mechanism in microcirculation, indicating the influence of MPO-induced abnormalities on RBC deformability under pathological stress conditions.

KW - Cardiovascular diseases

KW - Cell deformability

KW - Erythrocytes

KW - Lectin

KW - Myeloperoxidase

KW - Oxidative/halogenative stress

UR - http://www.scopus.com/inward/record.url?scp=84952360563&partnerID=8YFLogxK

U2 - 10.1016/j.abb.2015.12.007

DO - 10.1016/j.abb.2015.12.007

M3 - Article

C2 - 26714302

AN - SCOPUS:84952360563

VL - 591

SP - 87

EP - 97

JO - Archives of Biochemistry and Biophysics

JF - Archives of Biochemistry and Biophysics

SN - 0003-9861

ER -

ID: 97786365