Research output: Contribution to journal › Article › peer-review
Effects of recombinant human lactoferrin on calcium signaling and functional responses of human neutrophils. / 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.
In: Archives of Biochemistry and Biophysics, Vol. 675, 108122, 30.10.2019.Research output: Contribution to journal › Article › peer-review
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TY - JOUR
T1 - Effects of recombinant human lactoferrin on calcium signaling and functional responses of human neutrophils
AU - Grigorieva, Daria V.
AU - Gorudko, Irina V.
AU - Shamova, Ekaterina V.
AU - Terekhova, Maria S.
AU - Maliushkova, Elena V.
AU - Semak, Igor V.
AU - Cherenkevich, Sergey N.
AU - Sokolov, Alexey V.
AU - Timoshenko, Alexander V.
N1 - Funding Information: This work was partly supported by RFBR (grant 18-515-00004 ), BRFBR (grant B18R-058 ) and Russian President's grant MD-5133.2018.4 . Publisher Copyright: © 2019 Elsevier Inc. Copyright: Copyright 2019 Elsevier B.V., All rights reserved.
PY - 2019/10/30
Y1 - 2019/10/30
N2 - 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.
AB - 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.
KW - Calcium ions
KW - Cell aggregation
KW - Degranulation
KW - Neutrophils
KW - Recombinant human lactoferrin
KW - Respiratory burst
UR - http://www.scopus.com/inward/record.url?scp=85072775669&partnerID=8YFLogxK
U2 - 10.1016/j.abb.2019.108122
DO - 10.1016/j.abb.2019.108122
M3 - Article
C2 - 31580874
AN - SCOPUS:85072775669
VL - 675
JO - Archives of Biochemistry and Biophysics
JF - Archives of Biochemistry and Biophysics
SN - 0003-9861
M1 - 108122
ER -
ID: 75024723