It was established that recombinant human lactoferrin (rhLf), isolated from transgenic goats milk, binds to human neutrophils. This binding leads to an increase in intracellular Ca2+ due to the mobilization of Ca2+ from the endoplasmic reticulum and influx of extracellular Ca2+ through the store-operating calcium channels and T-type calcium channels. It was found that expose of neutrophils to rhLf lead to actin cytoskeleton reorganization and increase in intracellular protein tyrosine phosphorylation. RhLf augmented fMLP-induced respiratory burst of neutrophils. Together, these finding indicate that rhLf has a modulating effect on the functional neutrophil properties. Obtained results can be used to regulate the body's immune response, aimed to enhance the functional activity of neutrophils in pathologies associated with decreased killer capacity of these cells.
recombinant human lactoferrin, neutrophils, respiratory burst, calcium ions, tyrosine kinases, actin cytoskeleton
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