Previous Article in Journal
Effect of shRNA Mediated Silencing of YB-1 Protein on the Expression of Matrix Collagenases in Malignant Melanoma Cell In Vitro
Article Menu

Export Article

Open AccessFeature PaperArticle
Cells 2018, 7(1), 8; doi:10.3390/cells7010008

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 Programmed Cell Death)
View Full-Text   |   Download PDF [2604 KB, uploaded 12 January 2018]   |  


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

Figure 1

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).

Supplementary material

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

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.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics



[Return to top]
Cells EISSN 2073-4409 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top