The effect of myeloperoxidase isoforms on biophysical properties of red blood cellsстатья
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Дата последнего поиска статьи во внешних источниках: 15 февраля 2024 г.
Аннотация:Myeloperoxidase (MPO), an oxidant-producing enzyme, stored in azurophilic granules of neutrophils has been recently shown to infuence 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 disulfde bond but in infammatory foci as a result of disulfde cleavage monomeric MPO (hemi-MPO) can also be produced. This study investigated if two MPO isoforms have distinct efects on biophysical properties of RBCs. We have found that hemi-MPO, as well as thedimeric 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, signifcant changes in cell volume, morphology, and the conductance of RBC plasma membrane ion channels. Furthermore, we have shown for the frst time that both dimeric and hemi-MPO lead to hosphatidylserine (PS) exposure on the outer leafet of RBC membrane. However, the efects of hemiMPO on the structural and functional properties of RBCs were lower compared to those of dimeric MPO. These fndingssuggest that the ability of MPO protein to infuence RBC’s biophysical properties depends on its conformation (dimeric or monomeric isoform). It is intriguing to speculate that hemi-MPO appearance in blood during infammation can serve as a regulatory mechanism addressed to reduce abnormalities on RBC response, induced by dimeric MPO.