Результаты исследований: Научные публикации в периодических изданиях › статья
Lactoferrin, myeloperoxidase, and ceruloplasmin: complementary gearwheels cranking physiological and pathological processes. / Sokolov, A.V.; Zakahrova, E.T.; Kostevich, V.A.; Samygina, V.R.; Vasilyev, V.B.
в: Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine, Том 27, № 5, 2014, стр. 815-828.Результаты исследований: Научные публикации в периодических изданиях › статья
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TY - JOUR
T1 - Lactoferrin, myeloperoxidase, and ceruloplasmin: complementary gearwheels cranking physiological and pathological processes
AU - Sokolov, A.V.
AU - Zakahrova, E.T.
AU - Kostevich, V.A.
AU - Samygina, V.R.
AU - Vasilyev, V.B.
PY - 2014
Y1 - 2014
N2 - Copper-containing plasma protein ceruloplasmin (Cp) forms a complex with lactoferrin (Lf), an iron-binding protein, and with the heme-containing myeloperoxidase (Mpo). In case of inflammation Lf and Mpo are secreted from the granules of neutrophils. Among the plasma proteins Cp seems to be the preferential partner of Lf and Mpo. After an intraperitoneal injection of Lf to rodents the “Cp-Lf” complex has been shown to appear in their bloodstream. Cp prevents the interaction of Lf with protoplasts of Micrococcus luteus. Upon immunoprecipitation of Cp the blood plasma becomes depleted of Lf and in dose-dependent manner loses the capacity to inhibit the peroxidase activity of Mpo, but not the Mpo-catalyzed oxidation of thiocyanate in the (pseudo)halogenating cycle. Antimicrobial effect against E.coli displayed by a synergistic system that includes Lf and Mpo-H2O2-chloride, but not thiocyanate, as the substrate for Mpo is abrogated when Cp is added. Hence, Cp can be regarded as an anti-inflammatory factor that res
AB - Copper-containing plasma protein ceruloplasmin (Cp) forms a complex with lactoferrin (Lf), an iron-binding protein, and with the heme-containing myeloperoxidase (Mpo). In case of inflammation Lf and Mpo are secreted from the granules of neutrophils. Among the plasma proteins Cp seems to be the preferential partner of Lf and Mpo. After an intraperitoneal injection of Lf to rodents the “Cp-Lf” complex has been shown to appear in their bloodstream. Cp prevents the interaction of Lf with protoplasts of Micrococcus luteus. Upon immunoprecipitation of Cp the blood plasma becomes depleted of Lf and in dose-dependent manner loses the capacity to inhibit the peroxidase activity of Mpo, but not the Mpo-catalyzed oxidation of thiocyanate in the (pseudo)halogenating cycle. Antimicrobial effect against E.coli displayed by a synergistic system that includes Lf and Mpo-H2O2-chloride, but not thiocyanate, as the substrate for Mpo is abrogated when Cp is added. Hence, Cp can be regarded as an anti-inflammatory factor that res
KW - ceruloplsamin
KW - lactoferrin
KW - myeloperoxidase
KW - protein-protein interactions
KW - synergism of antimicrobial proteins
KW - inflammation
KW - thiocyanate
KW - halogenative stress.
U2 - 10.1007/s10534-014-9755-2
DO - 10.1007/s10534-014-9755-2
M3 - Article
VL - 27
SP - 815
EP - 828
JO - BioMetals
JF - BioMetals
SN - 0966-0844
IS - 5
ER -
ID: 7017870