Binding of human myeloperoxidase to red blood cells: Molecular targets and biophysical consequences at the plasma membrane

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.

Авторы: 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.
Журнал: Archives of Biochemistry and Biophysics
Том: 591
Год издания: 2016
Издательство: Academic Press
Местоположение издательства: United States
Первая страница: 87
Последняя страница: 97
DOI: 10.1016/j.abb.2015.12.007
Аннотация: 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 glycanrecognizing 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 Ca2þ, 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.
Добавил в систему: Панасенко Олег Михайлович

	ИСТИНА	Войти в систему Регистрация
	Интеллектуальная Система Тематического Исследования НАукометрических данных
	Главная Поиск Статистика О проекте Помощь

ИСТИНА

Интеллектуальная Система Тематического Исследования НАукометрических данных

Binding of human myeloperoxidase to red blood cells: Molecular targets and biophysical consequences at the plasma membraneстатья