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Effects of Recombinant Human Lactoferrin on Calcium Signaling and Functional Responses of Human Neutrophils

Effects of Recombinant Human Lactoferrin on Calcium Signaling and Functional Responses of Human Neutrophils

Daria V Grigorieva, Irina V Gorudko, Ekaterina V Shamova, Maria S Terekhova, Elena V Maliushkova, Igor V Semak, Sergey N Cherenkevich, Alexey V Sokolov, Alexander V Timoshenko

Arch Biochem Biophys. 2019 Oct 30;675:108122.

PMID: 31580874

Abstract:

Lactoferrin is a non-heme iron-binding glycoprotein with multiple health-beneficial functions including antimicrobial, antioxidant, anticarcinogenic, and immunomodulatory effects. There is emerging evidence that neutrophils may serve as targets of lactoferrin in vivo, and here we show how recombinant human lactoferrin (rhLf) can contribute to this regulation. Indeed, our results demonstrate that rhLf binds efficiently to human neutrophils and induces a variety of early cellular responses such as mobilization of intracellular Ca2+, remodeling of actin cytoskeleton, and degranulation (release of lysozyme and myeloperoxidase). In addition, rhLf facilitates lectin-induced H2O2 production and stabilization of lectin-induced cellular aggregates. The role of calcium signaling seems to be essential for rhLf-induced activation of neutrophils, as Ca2+-chelators inhibit degranulation response while lectin-induced H2O2 production correlates significantly with cytoplasmic Ca2+ elevation. Taken together, our findings justify that rhLf can activate neutrophil functions in a calcium-dependent manner and hence, can potentiate innate immune responses.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP9001632-A	Lysozyme from human neutrophils		9001-63-2	Price

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