Lactoferrin modified by hypohalous acids: Partial loss in activation of human neutrophilsстатья
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Дата последнего поиска статьи во внешних источниках: 15 февраля 2024 г.
Аннотация:Previously we have shown that lactoferrin (LTF), a protein of secondary neutrophilic granules, can be efficientlymodified by hypohalous acids (HOCl and HOBr), which are produced at high concentrations during inflammationand oxidative/halogenative stress by myeloperoxidase, an enzyme of azurophilic neutrophilic granules. Herewe compared the effects of recombinant human lactoferrin (rhLTF) and its halogenated derivatives (rhLTF-Cl andrhLTF-Br) on functional responses of neutrophils. Our results demonstrated that after halogenative modification,rhLTF lost its ability to induce mobilization of intracellular calcium, actin cytoskeleton reorganization, andmorphological changes in human neutrophils. Moreover, both forms of the halogenated rhLTF prevented bindingof N-acetylglucosamine-specific plant lectin Triticum vulgaris agglutinin (WGA) to neutrophils and, in contrast tonative rhLTF, inhibited respiratory burst of neutrophils induced by N-formyl-L-methionyl-L-leucyl-L-phenylalanineand by two plant lectins (WGA and PHA-L). However, we observed no differences between the effects ofrhLTF, rhLTF-Cl, and rhLTF-Br on respiratory burst of neutrophils induced by phorbol 12-myristate 13-acetate(PMA), digitonin, and number of plant lectins with different glycan-binding specificity. Furthermore, all rhLTFforms interfered with PMA- and ionomycin-induced formation of neutrophil extracellular traps. Thus, halogenativemodification of LTF is one of the mechanisms involved in modulating a variety of signaling pathways inneutrophils to control their pro-inflammatory activity.