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Fine Regulation of Neutrophil Oxidative Status and Apoptosis by Ceruloplasmin and Its Derivatives

Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow 119234, Russia
FGBU Hematology Research Centre, Russia Federation Ministry of Public Health, Moscow 125167, Russia
FSBSI Institute of Experimental Medicine, St. Petersburg 197376, Russia
Department of Fundamental Problems of Medicine and Medical Technology, Saint-Petersburg State University, St. Petersburg 199034, Russia
Centre of Preclinical Translational Research, Almazov National Medical Research Centre, Saint-Petersburg 197371, Russia
Author to whom correspondence should be addressed.
Received: 7 December 2017 / Revised: 30 December 2017 / Accepted: 10 January 2018 / Published: 12 January 2018
(This article belongs to the Section Cell Signaling and Regulated Cell Death)
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Timely neutrophil apoptosis is an essential part of the resolution phase of acute inflammation. Ceruloplasmin, an acute-phase protein, which is the predominant copper-carrying protein in the blood, has been suggested to have a marked effect on neutrophil life span. The present work is a comparative study on the effects of intact holo-ceruloplasmin, its copper-free (apo-) and partially proteolyzed forms, and synthetic free peptides RPYLKVFNPR (883–892) and RRPYLKVFNPRR (882–893) on polymorphonuclear leukocyte (PMNL, neutrophil) oxidant status and apoptosis. The most pronounced effect on both investigated parameters was found with copper-containing samples, namely, intact and proteolyzed proteins. Both effectively reduced spontaneous and tumor necrosis factor-α (TNF-α)-induced extracellular and intracellular accumulation of superoxide radicals, but induced a sharp increase in the oxidation of intracellular 2′,7′-dichlorofluorescein upon short exposure. Therefore, intact and proteolyzed ceruloplasmin have both anti- and pro-oxidant effects on PMNLs wherein the latter effect is diminished by TNF-α and lactoferrin. Additionally, all compounds investigated were determined to be inhibitors of delayed spontaneous apoptosis. Intact enzyme retained its pro-survival activity, whereas proteolytic degradation converts ceruloplasmin from a mild inhibitor to a potent activator of TNF-α-induced neutrophil apoptosis. View Full-Text
Keywords: apoptosis; neutrophil; ceruloplasmin; superoxide; reactive oxygen species apoptosis; neutrophil; ceruloplasmin; superoxide; reactive oxygen species

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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

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Golenkina, E.A.; Viryasova, G.M.; Galkina, S.I.; Gaponova, T.V.; Sud’ina, G.F.; Sokolov, A.V. Fine Regulation of Neutrophil Oxidative Status and Apoptosis by Ceruloplasmin and Its Derivatives. Cells 2018, 7, 8.

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