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

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.
PMID: 31754972 [PubMed - as supplied by publisher]

Source: Molecular and Cellular Biochemistry - November 20, 2019 Category: Biochemistry Authors: Shamova EV, Gorudko IV, Grigorieva DV, Sokolov AV, Kokhan AU, Melnikova GB, Yafremau NA, Gusev SA, Sveshnikova AN, Vasilyev VB, Cherenkevich SN, Panasenko OM Tags: Mol Cell Biochem Source Type: research