Human serum albumin modified under oxidative/halogenative stress enhances luminol-dependent chemiluminescence of human neutrophils

Mikhalchik, Elena V.; Смолина, Н. В.; Astamirova, T. S.; Gorudko, Irina V.; Grigorieva, Daria V.; Иванов, В. А.; Sokolov, A. V.; Kostevich, Valeria A.; Sn, Cherenkevich; Панасенко, О. М.

doi:10.1134/s0006350913040118

Cited by 9 publications

(4 citation statements)

References 25 publications

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“…Meanwhile it opens the way for studies aimed at analyzing the effects of different conditions (such as the presence of small-molecule antioxidants or the binding of ligands) on the observed oxidation-induced structural transition. We could also speculate that the conformational change of HSA caused by the hypochlorite-induced chemical modification could help rationalize on a structural basis the observations about an apparent implication of the “chlorinated” form of HSA in specific receptor recognitions with potential roles in physiological processes like clearance of the damaged protein or inflammation stimulation. − …”

Section: Discussionmentioning

confidence: 98%

Structural Response of Human Serum Albumin to Oxidation: Biological Buffer to Local Formation of Hypochlorite

et al. 2016

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The most abundant plasma protein, human serum albumin (HSA), plays a key part in the body's antioxidant defense against reactive species. This study was aimed at correlating oxidant-induced chemical and structural effects on HSA. Despite the chemical modification induced by the oxidant hypochlorite, the native shape is preserved up to oxidant/HSA molar ratio <80, above which a structural transition occurs in the critical range 80-120. This conformational variation involves the drifting of one of the end-domains from the rest of the protein and corresponds to the loss of one-third of the α-helix and a net increase of the protein negative charge. The transition is highly reproducible suggesting that it represents a well-defined structural response typical of this multidomain protein. The ability to tolerate high levels of chemical modification in a folded or only partially unfolded state, as well as the stability to aggregation, provides albumin with optimal features as a biological buffer for the local formation of oxidants.

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Section: Discussionmentioning

confidence: 98%

Structural Response of Human Serum Albumin to Oxidation: Biological Buffer to Local Formation of Hypochlorite

et al. 2016

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“…CL is a simple, sensitive, and fast method to study cell response to stimuli and cell‐independent oxidative reactions in biological fluids [Kozlov et al, ; Vlasova et al, ; Mikhalchik et al, ]. In our experiments, the kinetics of luminol‐dependent CL of blood samples showed that ROS generation in blood was due to neutrophil activation rather than luminol oxidation by redox‐active metals and peroxides present in the samples [Robinson et al, ] (Figs.…”

Section: Discussionmentioning

confidence: 55%

“…Our previous studies focused on modulating the functional activity of isolated neutrophils and neutrophils in blood by proteins, phenolic compounds, nanoparticles, and high voltage electric field pulses [Malinin et al, ; Vlasova et al, ,, ,, 2016; Mikhalchik et al, ]. In the present work, we studied the influence of MMW radiation (32.9–39.6 GHz, 100 W/m 2 ) on neutrophil activation by particulate agonists in whole blood samples.…”

Section: Introductionmentioning

confidence: 90%

Extremely high‐frequency electromagnetic radiation enhances neutrophil response to particulate agonists

Vlasova

Mikhalchik²,

Gusev³

et al. 2017

Bioelectromagnetics

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The growing use of extremely high-frequency electromagnetic radiation (EHF EMR) in information and communication technology and in biomedical applications has raised concerns regarding the potential biological impact of millimeter waves (MMWs). Here, we elucidated the effects of MMW radiation on neutrophil activation induced by opsonized zymosan or E. coli in whole blood ex vivo. After agonist addition to blood, two samples were prepared. A control sample was incubated at ambient conditions without any treatment, and a test sample was exposed to EHF EMR (32.9-39.6 GHz, 100 W/m ). We used methods that allowed us to assess the functional status of neutrophils immediately after exposure: oxidant production levels were measured by luminol-dependent chemiluminescence, and morphofunctional changes to neutrophils were observed in blood smears. Results revealed that the response of neutrophils to both agonists was intensified if blood was exposed to MMW radiation for 15 min. Neutrophils were intact in both the control and irradiated samples if no agonist was added to blood before incubation. Similarly, exposing suspensions of isolated neutrophils in plasma to MMW radiation enhanced cell response to both zymosan and E. coli. Heating blood samples was shown to be the primary mechanism underlying enhanced EHF EMR-induced oxidant production by neutrophils in response to particulate agonists. Bioelectromagnetics. 39:144-155, 2018. © 2017 Wiley Periodicals, Inc.

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“…Earlier, in equivalent experiments, we studied the effects of HSA [ 44 , 45 ] and low-density lipoprotein (LDL) [ 43 , 46 ] modified with HOCl, the major product of MPO catalysis on Luc-CL and Lum-CL, and registered the enhancement of both, accompanied by the upregulation of MPO exocytosis. We expected the same results in the present study.…”

Section: Discussionmentioning

confidence: 99%

Methylglyoxal-Modified Human Serum Albumin Binds to Leukocyte Myeloperoxidase and Inhibits its Enzymatic Activity

et al. 2022

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Hyperglycemia in diabetes mellitus induces modification of proteins by glucose and its derivative methylglyoxal (MG). Neutrophils perform their bactericidal activity mainly via reactive halogen (RHS) and oxygen (ROS) species generation catalyzed by myeloperoxidase (MPO) stored in neutrophil azurophilic granules (AGs) and membrane NADPH oxidase, respectively. Herein, we study the binding of human serum albumin (HSA) modified with MG (HSA-MG) to MPO and its effects on MPO activity and release by neutrophils. Peroxidase activity of MPO was registered by oxidation of 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) diammonium salt, and chlorinating activity by decolorization of Celestine blue B dye. Binding of HSA-MG to MPO was studied by affinity chromatography, disc-electrophoresis, ligand Western blotting and enzyme-linked solid phase immunoassay using monoclonal antibodies (mAbs) to MPO. ROS and RHS generation were detected by lucigenin (Luc) and luminol (Lum) chemiluminescence (CL), respectively. Neutrophil degranulation was assessed by flow cytometry using fluorescent labeled antibodies to the marker proteins CD63 from AGs and CD11b from peroxidase-negative granules (PNGs). NETosis was assayed by quantifying DNA network-like structures (NET-like structures) in blood smears stained by Romanowsky. HSA-MG bound to MPO, giving a stable complex (Kd = 1.5 nM) and competing with mAbs, and non-competitively inhibited peroxidase and chlorinating MPO activity and induced degranulation of PNGs but not of AGs. HSA-MG enhanced Luc-CL per se or following PMA, unlike Lum-CL, and did not affect spontaneous or PMA-stimulated NETosis. Thus, HSA modified under hyperglycemia-like conditions stimulated NADPH oxidase of neutrophils but dampened their functions dependent on activity of MPO, with no effect on its release via degranulation or NETosis. This phenomenon could underlie the downregulation of bactericidal activity of MPO and neutrophils, and hence of innate immunity, giving rise to wound healing impairment and susceptibility to infection in patients with hyperglycemia.

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Human serum albumin modified under oxidative/halogenative stress enhances luminol-dependent chemiluminescence of human neutrophils

Cited by 9 publications

References 25 publications

Structural Response of Human Serum Albumin to Oxidation: Biological Buffer to Local Formation of Hypochlorite

Structural Response of Human Serum Albumin to Oxidation: Biological Buffer to Local Formation of Hypochlorite

Extremely high‐frequency electromagnetic radiation enhances neutrophil response to particulate agonists

Methylglyoxal-Modified Human Serum Albumin Binds to Leukocyte Myeloperoxidase and Inhibits its Enzymatic Activity

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