Effect of Lactoferrin on Consequences of Acute Experimental Hemorrhagic Anemia in Rats

Pulina, M. O.; Sokolov, A. V.; Захарова, Е. М.; Kostevich, Valeria A.; Vasilyev, V. B.

doi:10.1007/s10517-010-0911-6

Cited by 14 publications

(13 citation statements)

References 10 publications

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“…2 -form TFe 465 = 4446 M -1 cm -1 (Masson 1970), Fe 2? -ferrozine-e 564 = 27,900 M -1 cm -1 (Pulina et al 2010). …”

Section: Methodsmentioning

confidence: 97%

“…Hemoglobin content was assayed by reading A 492 absorption of the animals' whole blood samples subjected to hemolysis and diluted 1:20 with 0.04 % ammonia in 96-well plates (Pulina et al 2010). …”

Section: Hemoglobin Contentmentioning

confidence: 99%

“…and its release from transferrin. Absorption of samples was measured at A 564 and iron content in lM was calculated using coefficient 442 deduced from the calibration curve (Pulina et al 2010).…”

Section: Serum Iron Contentmentioning

confidence: 99%

“…ions faster than serum transferrin (TF) (Sokolov et al 2005a(Sokolov et al , 2009). Apo-LF provided faster recovery of rats that underwent acute post-hemorrhagic anemia (Pulina et al 2010). One of the likely mechanisms of the antianemic effect of LF can be ferroportin stabilization (Cutone et al 2014).…”

Section: Introductionmentioning

confidence: 98%

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Functional link between ferroxidase activity of ceruloplasmin and protective effect of apo-lactoferrin: studying rats kept on a silver chloride diet

Kostevich¹,

Sokolov

Kozlov³

et al. 2016

Biometals

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Strongly pronounced argyrosis caused by adding AgCl to the feed of laboratory rats efficiently mimics the deficiency of ceruloplasmin (CP) ferroxidase activity. Bringing the concentration of AgCl in the feedstuff of lactating rats to 250 mg % and keeping their progeny (Ag-rats) for 3 months on the same silver-containing feed provided the serum iron content 1.4 times lower than that in the control group. Besides, the ferroxidase activity of CP dropped to zero. In CP purified from sera of Ag-rats two copper ions were substituted with two silver ions. Using rat models of both post-hemorrhagic and hemolytic anemia we showed that the deficiency of CP ferroxidase activity in Ag-rats affects the iron content in serum, though does not prevent the recovery of hemoglobin level accompanied by exhaustion of iron caches in liver and spleen. When apo-lactoferrin (apo-LF) was administered to Ag-rats suffering from either post-hemorrhagic or hemolytic anemia, both hemoglobin and serum iron were restored more rapidly than in the control animals. In independent experiments Ag-rats were compared with those fed on regular diet and the former displayed a prolonged 3-day stabilization of hypoxia-inducible factors 1 and 2 alpha (HIF-1a and HIF-2a) along with an increased serum concentration of erythropoietin. Introduction to Ag-rats of active CP separately or together with apo-LF reduced that effect to 1 day only. It is concluded that saturation of apo-LF with iron, provided by active CP, can strongly affect its protective capacity.

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“…2 -form TFe 465 = 4446 M -1 cm -1 (Masson 1970), Fe 2? -ferrozine-e 564 = 27,900 M -1 cm -1 (Pulina et al 2010). …”

Section: Methodsmentioning

confidence: 97%

Section: Hemoglobin Contentmentioning

confidence: 99%

Section: Serum Iron Contentmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 98%

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Functional link between ferroxidase activity of ceruloplasmin and protective effect of apo-lactoferrin: studying rats kept on a silver chloride diet

Kostevich¹,

Sokolov

Kozlov³

et al. 2016

Biometals

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“…Ferroxidase activity was assayed in reaction of 15 nM CP with 150 µM Fe(NH 4 ) 2 (SO 4 ) 2 ×6H 2 O in 0.4 Na-acetate buffer, pH 5.5. After 10 min incubation, ferrozin was added to the reaction mixture to the final concentration of 150 µM, and A 564 was monitored vs. the control aliquot with NaN 3 (Pulina et al 2010).…”

Section: R a F Tmentioning

confidence: 99%

Capacity of ceruloplasmin to scavenge products of the respiratory burst of neutrophils is not altered by the products of reactions catalyzed by myeloperoxidase

Sokolov

Kostevich

Varfolomeeva

et al. 2018

Biochem. Cell Biol.

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CP is a copper-containing ferroxidase of blood plasma, which acts as an acute phase reactant during inflammation. The effect of oxidative modification of CP induced by oxidants produced by MPO, such as HOCl, HOBr, and HOSCN, on its spectral, enzymatic, and anti-inflammatory properties was studied. We monitored the chemiluminescence of lucigenin and luminol along with fluorescence of hydroethidine and scopoletin to assay the inhibition by CP of the neutrophilic respiratory burst induced by PMA or fMLP. Superoxide dismutase activity of CP and its capacity to reduce the production of oxidants in respiratory burst of neutrophils remained virtually unchanged upon modifications caused by HOCl, HOBr, and HOSCN. Meanwhile, the absorption of type I copper ions at 610 nm became reduced, along with a drop in the ferroxidase and amino oxidase activities of CP. Likewise, its inhibitory effect on the halogenating activity of MPO was diminished. Sera of either healthy donors or patients with Wilson disease were co-incubated with neutrophils from healthy volunteers. In these experiments, we observed an inverse relationship between the content of CP in sera and the rate of HO production by activated neutrophils. In conclusion, CP is likely to play a role of an anti-inflammatory factor tempering the neutrophil respiratory burst in the bloodstream despite the MPO-mediated oxidative modifications.

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Human apo-lactoferrin as a physiological mimetic of hypoxia stabilizes hypoxia-inducible factor-1 alpha

et al. 2012

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Apo-form of human lactoferrin (LF) is a potent iron chelator, this feature being similar to the iron-binding properties of a synthetic chelator desferoxamine (DFO). The latter stabilizes the principal adaptive transcriptional hypoxia-inducible factor-1 alpha (HIF-1α). Since DFO is known as a pharmacological mimetic of hypoxia it was decided to test whether apo-LF is able to perform as such. Mice either injected intraperitoneally or given per os apo-LF displayed HIF-1α in liver, lungs, heart, brain, spleen and kidneys, as judged by results of Western blotting. Similar administration of iron-saturated LF (75 mg/kg) did not bring forth such effect. Synthesis of erythropoietin and ceruloplasmin became increased in the first case, which is explained by the respective genes being targets for HIF-1α. Apo-LF, but not Fe-LF, injected intraperitoneally to hypoxia low-resistant mice 24 h before animals were subjected to normobaric hypoxia with hypercapnia caused a significant increase of life-time by 40 %. The results obtained show that, like DFO, apo-LF performs as a normoxic mimetic of hypoxia, capable of stabilizing HIF-1α. Protective features of LF and DFO and their pharmacological properties involving HIF-1α are discussed.

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Effect of Lactoferrin on Consequences of Acute Experimental Hemorrhagic Anemia in Rats

Cited by 14 publications

References 10 publications

Functional link between ferroxidase activity of ceruloplasmin and protective effect of apo-lactoferrin: studying rats kept on a silver chloride diet

Functional link between ferroxidase activity of ceruloplasmin and protective effect of apo-lactoferrin: studying rats kept on a silver chloride diet

Capacity of ceruloplasmin to scavenge products of the respiratory burst of neutrophils is not altered by the products of reactions catalyzed by myeloperoxidase

Human apo-lactoferrin as a physiological mimetic of hypoxia stabilizes hypoxia-inducible factor-1 alpha

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