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The effect of myeloperoxidase isoforms on biophysical properties of red blood cells

  • Ekaterina V. ShamovaEmail author
  • Irina V. Gorudko
  • Daria V. Grigorieva
  • Alexey V. Sokolov
  • Anatoli U. Kokhan
  • Galina B. Melnikova
  • Nikolai A. Yafremau
  • Sergey A. Gusev
  • Anastasia N. Sveshnikova
  • Vadim B. Vasilyev
  • Sergey N. Cherenkevich
  • Oleg M. Panasenko
Article
  • 28 Downloads

Abstract

Myeloperoxidase (MPO), an oxidant-producing enzyme, stored in azurophilic granules of neutrophils has been recently shown to influence red blood cell (RBC) deformability leading to abnormalities in blood microcirculation. Native MPO is a homodimer, consisting of two identical protomers (monomeric MPO) connected by a single disulfide bond but in inflammatory foci as a result of disulfide cleavage monomeric MPO (hemi-MPO) can also be produced. This study investigated if two MPO isoforms have distinct effects on biophysical properties of RBCs. We have found that hemi-MPO, as well as the dimeric form, bind to the glycophorins A/B and band 3 protein on RBC’s plasma membrane, that lead to reduced cell resistance to osmotic and acidic hemolysis, reduction in cell elasticity, significant changes in cell volume, morphology, and the conductance of RBC plasma membrane ion channels. Furthermore, we have shown for the first time that both dimeric and hemi-MPO lead to phosphatidylserine (PS) exposure on the outer leaflet of RBC membrane. However, the effects of hemi-MPO on the structural and functional properties of RBCs were lower compared to those of dimeric MPO. These findings suggest that the ability of MPO protein to influence RBC’s biophysical properties depends on its conformation (dimeric or monomeric isoform). It is intriguing to speculate that hemi-MPO appearance in blood during inflammation can serve as a regulatory mechanism addressed to reduce abnormalities on RBC response, induced by dimeric MPO.

Keywords

Monomeric myeloperoxidase Dimeric myeloperoxidase Inflammation RBC Phosphatidylserine 

Notes

Acknowledgements

This work was partly supported by Russian Foundation for Basic Research (Grant 18-515-00004, Grant 17-54-04009), Belarusian Republican Foundation for Fundamental Research (Grant B18R-058) and Russian President’s grant MD-5133.2018.4.

Compliance with ethical standards

Conflict of interest

The authors declare no competing financial and nonfinancial interests.

Ethical approval

This work was approved by the protocol of the Local Ethics Committee at Federal State Budgetary Scientific Institution “Institute of Experimental Medicine”.

Supplementary material

11010_2019_3654_MOESM1_ESM.doc (83 kb)
Supplementary material 1 (DOC 83 kb)

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Copyright information

© Springer Science+Business Media, LLC, part of Springer Nature 2019

Authors and Affiliations

  • Ekaterina V. Shamova
    • 1
    Email author
  • Irina V. Gorudko
    • 1
  • Daria V. Grigorieva
    • 1
  • Alexey V. Sokolov
    • 2
    • 3
    • 4
  • Anatoli U. Kokhan
    • 1
  • Galina B. Melnikova
    • 5
  • Nikolai A. Yafremau
    • 6
  • Sergey A. Gusev
    • 4
  • Anastasia N. Sveshnikova
    • 7
  • Vadim B. Vasilyev
    • 2
    • 3
  • Sergey N. Cherenkevich
    • 1
  • Oleg M. Panasenko
    • 4
    • 8
  1. 1.Belarusian State UniversityMinskBelarus
  2. 2.FSBSI “Institute of Experimental Medicine”St. PetersburgRussia
  3. 3.Saint-Petersburg State UniversitySt. PetersburgRussia
  4. 4.Federal Research and Clinical Center of Physical–Chemical Medicine of Federal Medical Biological AgencyMoscowRussia
  5. 5.A.V. Luikov Heat and Mass Transfer Institute of the National Academy of Sciences of BelarusMinskBelarus
  6. 6.State Institution “N.N. Alexandrov Republican Scientific and Practical Center of Oncology and Medical Radiology”MinskBelarus
  7. 7.Lomonosov Moscow State UniversityMoscowRussia
  8. 8.Pirogov Russian National Research Medical UniversityMoscowRussia

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