دورية أكاديمية

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

التفاصيل البيبلوغرافية
العنوان: Binding of human myeloperoxidase to red blood cells: Molecular targets and biophysical consequences at the plasma membrane level.
المؤلفون: Gorudko IV; Department of Biophysics, Faculty of Physics, Belarusian State University, Minsk 220030, Belarus., Sokolov AV; Institute of Experimental Medicine, St. Petersburg, Russia; Saint-Petersburg State University, St. Petersburg, Russia; Research Institute of Physico-Chemical Medicine, Moscow, Russia., Shamova EV; Department of Biophysics, Faculty of Physics, Belarusian State University, Minsk 220030, Belarus., Grigorieva DV; Department of Biophysics, Faculty of Physics, Belarusian State University, Minsk 220030, Belarus., Mironova EV; Belarusian State Medical University, Minsk, Belarus., Kudryavtsev IV; Institute of Experimental Medicine, St. Petersburg, Russia., Gusev SA; Research Institute of Physico-Chemical Medicine, Moscow, Russia., Gusev AA; Research Institute of Physico-Chemical Medicine, Moscow, Russia., Chekanov AV; Pirogov Russian National Research Medical University, Moscow, Russia., Vasilyev VB; Institute of Experimental Medicine, St. Petersburg, Russia; Saint-Petersburg State University, St. Petersburg, Russia., Cherenkevich SN; Department of Biophysics, Faculty of Physics, Belarusian State University, Minsk 220030, Belarus., Panasenko OM; Research Institute of Physico-Chemical Medicine, Moscow, Russia; Pirogov Russian National Research Medical University, Moscow, Russia. Electronic address: o-panas@mail.ru., Timoshenko AV; Department of Biology, Western University, Ontario, London, N6A 5B7, Canada.
المصدر: Archives of biochemistry and biophysics [Arch Biochem Biophys] 2016 Feb 01; Vol. 591, pp. 87-97. Date of Electronic Publication: 2015 Dec 20.
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: Elsevier Country of Publication: United States NLM ID: 0372430 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1096-0384 (Electronic) Linking ISSN: 00039861 NLM ISO Abbreviation: Arch Biochem Biophys Subsets: MEDLINE
أسماء مطبوعة: Publication: <2000- > : San Diego, CA : Elsevier
Original Publication: New York, NY : Academic Press
مواضيع طبية MeSH: Erythrocyte Membrane/*metabolism , Erythrocytes/*cytology , Erythrocytes/*physiology , Hemolysis/*physiology , Membrane Fluidity/*physiology , Peroxidase/*metabolism, Binding Sites ; Cell Size ; Cells, Cultured ; Erythrocyte Membrane/ultrastructure ; Humans ; Membrane Potentials/physiology ; Protein Binding
مستخلص: 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 Ca(2+), 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.
(Copyright © 2015 Elsevier Inc. All rights reserved.)
فهرسة مساهمة: Keywords: Cardiovascular diseases; Cell deformability; Erythrocytes; Lectin; Myeloperoxidase; Oxidative/halogenative stress
المشرفين على المادة: EC 1.11.1.7 (Peroxidase)
تواريخ الأحداث: Date Created: 20151230 Date Completed: 20160614 Latest Revision: 20160209
رمز التحديث: 20221213
DOI: 10.1016/j.abb.2015.12.007
PMID: 26714302
قاعدة البيانات: MEDLINE
الوصف
تدمد:1096-0384
DOI:10.1016/j.abb.2015.12.007