Effects of recombinant human lactoferrin on calcium signaling and functional responses of human neutrophils

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 recombinan...

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Published in:	Archives of biochemistry and biophysics Vol. 675; p. 108122
Main Authors:	Grigorieva, Daria V., Gorudko, Irina V., Shamova, Ekaterina V., Terekhova, Maria S., Maliushkova, Elena V., Semak, Igor V., Cherenkevich, Sergey N., Sokolov, Alexey V., Timoshenko, Alexander V.
Format:	Journal Article
Language:	English
Published:	United States Elsevier Inc 30-10-2019
Subjects:	Calcium - metabolism Calcium ions Calcium Signaling Cell aggregation Cell Degranulation Degranulation Humans Hydrogen Peroxide - metabolism Lactoferrin - metabolism Neutrophils Neutrophils - metabolism Protein Binding Recombinant human lactoferrin Recombinant Proteins - metabolism Respiratory burst PHA-L STA PNA CABA fMLP HRP SNA Recombinant human lactoferrin MPO SBA Lf GlcNAc PBS [Ca2+]i rhLf PMA VSA Neutrophils Con A o-DA EDTA WGA HSR contacts Cell aggregation ROS Degranulation Respiratory burst Calcium ions BAPTA-AM
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Summary:	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.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0003-9861 1096-0384
DOI:	10.1016/j.abb.2019.108122