Ceruloplasmin-derived peptide is the strongest regulator of oxidative stress and leukotriene synthesis in neutrophils

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Ceruloplasmin-derived peptide is the strongest regulator of oxidative stress and leukotriene synthesis in neutrophils. / Golenkina, Ekaterina A.; Livenskyi, Alexey D.; Viryasova, Galina M.; Romanova, Yulia M.; Sud'Ina, Galina F.; Sokolov, Alexey V.

In: Biochemistry and Cell Biology, Vol. 95, No. 3, 2017, p. 445-449.

Research output: Contribution to journal › Article › peer-review

Author

Golenkina, Ekaterina A. ; Livenskyi, Alexey D. ; Viryasova, Galina M. ; Romanova, Yulia M. ; Sud'Ina, Galina F. ; Sokolov, Alexey V. / Ceruloplasmin-derived peptide is the strongest regulator of oxidative stress and leukotriene synthesis in neutrophils. In: Biochemistry and Cell Biology. 2017 ; Vol. 95, No. 3. pp. 445-449.

BibTeX

@article{0f8de99ddaed4e5aaa503cbfd61a98ea,

title = "Ceruloplasmin-derived peptide is the strongest regulator of oxidative stress and leukotriene synthesis in neutrophils",

abstract = "Ceruloplasmin, an acute-phase protein, can affect the activity of leukocytes through its various enzymatic activities and protein-protein interactions (with lactoferrin, myeloperoxidase, eosinophil peroxidase, serprocidins, and 5-lipoxygenase (5-LOX), among others). However, the molecular mechanisms of ceruloplasmin activity are not clearly understood. In this study, we tested the ability of two synthetic peptides, RPYLKVFNPR (883-892) (P1) and RRPYLKVFNPRR (882-893) (P2), corresponding to the indicated fragments of the ceruloplasmin sequence, to affect neutrophil activation. Leukotriene (LT) B4 is the primary eicosanoid product of polymorphonuclear leukocytes (PMNLs, neutrophils). We studied leukotriene synthesis in PMNLs upon interaction with Salmonella enterica serovar Typhimurium. Priming of neutrophils with phorbol 12-myristate 13-acetate (PMA) elicited the strong regulatory function of P2 peptide as a superoxide formation inducer and leukotriene synthesis inhibitor. Ceruloplasmin-derived P2 peptide appeared to be a strong inhibitor of 5-LOX product synthesis under conditions of oxidative stress.",

keywords = "5-lipoxygenase, Ceruloplasmin, Myeloperoxidase, Neutrophil, Superoxide",

author = "Golenkina, {Ekaterina A.} and Livenskyi, {Alexey D.} and Viryasova, {Galina M.} and Romanova, {Yulia M.} and Sud'Ina, {Galina F.} and Sokolov, {Alexey V.}",

note = "Publisher Copyright: {\textcopyright} 2017 Published by NRC Research Press.",

year = "2017",

doi = "10.1139/bcb-2016-0180",

language = "English",

volume = "95",

pages = "445--449",

journal = "Biochemistry and Cell Biology",

issn = "0829-8211",

publisher = "National Research Council of Canada",

number = "3",

}

RIS

TY - JOUR

T1 - Ceruloplasmin-derived peptide is the strongest regulator of oxidative stress and leukotriene synthesis in neutrophils

AU - Golenkina, Ekaterina A.

AU - Livenskyi, Alexey D.

AU - Viryasova, Galina M.

AU - Romanova, Yulia M.

AU - Sud'Ina, Galina F.

AU - Sokolov, Alexey V.

PY - 2017

Y1 - 2017

N2 - Ceruloplasmin, an acute-phase protein, can affect the activity of leukocytes through its various enzymatic activities and protein-protein interactions (with lactoferrin, myeloperoxidase, eosinophil peroxidase, serprocidins, and 5-lipoxygenase (5-LOX), among others). However, the molecular mechanisms of ceruloplasmin activity are not clearly understood. In this study, we tested the ability of two synthetic peptides, RPYLKVFNPR (883-892) (P1) and RRPYLKVFNPRR (882-893) (P2), corresponding to the indicated fragments of the ceruloplasmin sequence, to affect neutrophil activation. Leukotriene (LT) B4 is the primary eicosanoid product of polymorphonuclear leukocytes (PMNLs, neutrophils). We studied leukotriene synthesis in PMNLs upon interaction with Salmonella enterica serovar Typhimurium. Priming of neutrophils with phorbol 12-myristate 13-acetate (PMA) elicited the strong regulatory function of P2 peptide as a superoxide formation inducer and leukotriene synthesis inhibitor. Ceruloplasmin-derived P2 peptide appeared to be a strong inhibitor of 5-LOX product synthesis under conditions of oxidative stress.

AB - Ceruloplasmin, an acute-phase protein, can affect the activity of leukocytes through its various enzymatic activities and protein-protein interactions (with lactoferrin, myeloperoxidase, eosinophil peroxidase, serprocidins, and 5-lipoxygenase (5-LOX), among others). However, the molecular mechanisms of ceruloplasmin activity are not clearly understood. In this study, we tested the ability of two synthetic peptides, RPYLKVFNPR (883-892) (P1) and RRPYLKVFNPRR (882-893) (P2), corresponding to the indicated fragments of the ceruloplasmin sequence, to affect neutrophil activation. Leukotriene (LT) B4 is the primary eicosanoid product of polymorphonuclear leukocytes (PMNLs, neutrophils). We studied leukotriene synthesis in PMNLs upon interaction with Salmonella enterica serovar Typhimurium. Priming of neutrophils with phorbol 12-myristate 13-acetate (PMA) elicited the strong regulatory function of P2 peptide as a superoxide formation inducer and leukotriene synthesis inhibitor. Ceruloplasmin-derived P2 peptide appeared to be a strong inhibitor of 5-LOX product synthesis under conditions of oxidative stress.

KW - 5-lipoxygenase

KW - Ceruloplasmin

KW - Myeloperoxidase

KW - Neutrophil

KW - Superoxide

UR - http://www.scopus.com/inward/record.url?scp=85020007835&partnerID=8YFLogxK

U2 - 10.1139/bcb-2016-0180

DO - 10.1139/bcb-2016-0180

M3 - Article

C2 - 28177760

AN - SCOPUS:85020007835

VL - 95

SP - 445

EP - 449

JO - Biochemistry and Cell Biology

JF - Biochemistry and Cell Biology

SN - 0829-8211

IS - 3

ER -

ID: 97809171