Celestine blue B as a sensor for hypochlorous acid and HOCL-modified proteins registration

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Abstract

Objective — the study of hypochlorous acid (HOCl) and its derivatives production, which catalyzed by human neutrophil myeloperoxidase, using “turn-on” fluorescent sensor — celestine blue B.

Materials and methods. Neutrophils were isolated from the venous blood of healthy donors. Phorbol 12-myristate 13-acetate, N-formyl-methionyl-leucyl-phenylalanine, plant lectins, HOCl-modified proteins were used as agonists. N-acetylcysteine, 4-aminobenzoic acid hydrazide, isoniazid and ceruloplasmin were used as regulators of neutrophil myeloperoxidase activity and/or HOCl scavengers.

Results. Using a wide range of agonists and inhibitors, it has been shown that celestine blue B is oxidized in vitro by HOCl and its derivatives as a result of neutrophil myeloperoxidase activity. The oxidation of celestine blue B by HOCl-modified human serum albumin (HSA-Cl) and inhibition of this process by monoclonal antibody against HSA-Cl (IgM class) was also found.

Conclusion. Based on the developed method using celestine blue B, it is possible to conduct a sensitive analysis for the presence of HOCl-modified proteins (chloramines, etc.), to investigate the effect of various agonists and drugs on myeloperoxidase activity and exocytosis from the neutrophil granules.

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About the authors

Veronika E. Lutsenko

Belarusian State University

Author for correspondence.
Email: nika.lutsenko@tut.by
SPIN-code: 1647-2893

PhD student, Department of Biophysics, Physics Faculty

Belarus, Minsk

Daria V. Grigorieva

Belarusian State University

Email: dargr@tut.by
ORCID iD: 0000-0003-0210-5474
SPIN-code: 2479-7785

PhD (Biology), Senior Researcher, Research Laboratory of Biophysics and Biotechnology, Department of Biophysics, Physics Faculty

Belarus, Minsk

Irina V. Gorudko

Belarusian State University

Email: irinagorudko@gmail.com
SPIN-code: 8968-3125

PhD (Biology), Associate Professor, Associate Professor of the Department of Biophysics, Physics Faculty

Belarus, Minsk

Sergey N. Cherenkevich

Belarusian State University

Email: cherenkevich@bsu.by
SPIN-code: 6493-9551

Doctor of Sciences (Biology), Professor, Academician of the NAS of Belarus, Professor of the Department of Biophysics, Physics Faculty

Belarus, Minsk

Nikolay N. Gorbunov

Research Institute of Experimental Medicine

Email: niko_laygo@mail.ru
ORCID iD: 0000-0003-4636-0565
SPIN-code: 6289-7281

PhD student, Research fellow of the Department of Molecular Genetics

Russian Federation, Saint Petersburg

Valeria A. Kostevich

Research Institute of Experimental Medicine; Federal Research and Clinical Center of Physical-Chemical Medicine of Federal Medical Biological Agency

Email: hfa-2005@yandex.ru
ORCID iD: 0000-0002-1405-1322
SPIN-code: 2726-2921

PhD (Biology), Senior Researcher of the Department of Molecular Genetics; Research fellow of Department of Biophysics

Russian Federation, Saint Petersburg; Moscow

Oleg M. Panasenko

Federal Research and Clinical Center of Physical-Chemical Medicine of Federal Medical Biological Agency; Pirogov Russian National Research Medical University

Email: o-panas@mail.ru
ORCID iD: 0000-0001-5245-2285
SPIN-code: 3035-6808

Doctor of Sciences (Biology), Professor, Head of Department of Biophysics; Senior Researcher of Department of Medical Physics

Russian Federation, Moscow

Alexey V. Sokolov

Research Institute of Experimental Medicine; Federal Research and Clinical Center of Physical-Chemical Medicine of Federal Medical Biological Agency; Saint Petersburg State University

Email: biochemsokolov@gmail.com
ORCID iD: 0000-0001-9033-0537
SPIN-code: 7427-7395

Doctor of Biological Sciences, Head of the Laboratory of Biochemical Genetics of the Department of Molecular Genetics; Senior Researcher of Department of Biophysics; Professor of Chair of Fundamental Problems of Medicine and Medical Technology 

Russian Federation, Saint Petersburg; Moscow; Saint Petersburg

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2. Fig. 1. Typical kinetic curves of CB oxidation (a) and parameters characterizing this process (b) in suspension of neutrophils activated by phorbol ester (PMA, 50 nM) or chemotactic peptide (fMLP, 1 μM) in the absence and presence of cytochalasin b (cyth b, 2.5 mg/L)

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3. Fig. 2. The effect of lectins from wheat germ (WGA, 100 mg/L), jack bean seeds (Con A, 100 mg/L), bean seeds (PHA-L, 100 mg/L), caragana tree (CABA, 100 mg/L), mistletoe (VAA, 50 mg/L), soy (SBA, 100 mg/L) in the absence and in the presence of cytochalasin b (cyth b, 2.5 mg/L) on the CB oxidation in neutrophils suspension. * p < 0.05

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4. Fig. 3. The effect of HSA-Cl (1 g/L) on CB oxidation in the neutrophils suspension (a) and in PBS (b)

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5. Fig. 4. The effect of monoclonal antibodies against HSA-Cl (1H2, 0.168 g/L, curve 2) on CB oxidation in HSA-Cl solution (0.125 g/L, curve 1). Negative control on the background of HSA (0.168 g/L and 0.336 g/L, curves 3 and 4)

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Copyright (c) 2019 Lutsenko V.E., Grigorieva D.V., Gorudko I.V., Cherenkevich S.N., Gorbunov N.N., Kostevich V.A., Panasenko O.M., Sokolov A.V.

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