Identification of leukocyte cationic proteins that interact with ceruloplasmin

Sokolov, A. V.; Pulina, M. O.; Ageeva, K. V.; Runova, O. L.; Захарова, Е. М.; Vasilyev, V. B.

doi:10.1134/s0006297907080093

Cited by 25 publications

(18 citation statements)

References 25 publications

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“…thrombin, serprocidins, and matrix metalloproteinases 2 and 12 (Sokolov et al 2007(Sokolov et al , 2009b(Sokolov et al , 2010a(Sokolov et al , 2015a. Plasma concentration of the socalled ''free copper'' grows in Alzheimer's disease concommittantly with the proteolytic degradation of CP (Squitti et al 2008).…”

Section: Discussionmentioning

confidence: 99%

“…Pro-inflammatory activity of some enzymes is suppressed as CP forms complexes with them. Among such are myeloperoxidase Samygina et al 2013), the members of the serprocidin family (elastase, cathepsin G, proteinase 3) (Sokolov et al 2007), matrix metalloproteinases 2 and 12 (Sokolov et al 2009b), 5-lipoxygenase (Sokolov et al 2010b) and eosinophil peroxidase (Sokolov et al 2015b). Importantly, the inhibition of the inflammation mediators listed is not directly linked with the oxidase activity of CP.…”

Section: Introductionmentioning

confidence: 99%

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Interaction of macrophage migration inhibitory factor with ceruloplasmin: role of labile copper ions

et al. 2015

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Macrophage migration inhibitory factor (MIF), a pro-inflammatory cytokine, is a target for pharmacological treatment of sepsis and malignant tumors. Inhibition of tautomerase activity of MIF in reaction with p-hydroxyphenylpyruvate (HPP) was observed in the presence of ceruloplasmin (CP), a copper-containing plasma protein. Binding labile copper ions to CP (CP+Cu(II)) is a prerequisite for MIF inhibiting. CP+Cu(II) is shown to be an uncompetitive inhibitor of MIF (Ki ~ 37 nM), which suggests formation of a complex 'MIF-HPP-CP-Cu(II)'. Filtration of CP+Cu(II) on a column with Chelex-100, otherwise the presence of high concentrations of histidine, cysteine or methionine abrogated the inhibitory effect of CP. Adding salts of Co(II) and Ni(II) that replace copper ions in the labile sites prevented the inhibitory effect of CP+Cu(II). Limited proteolysis of CP by thrombin diminished its oxidase activity in reaction with p-phenylenediamine, but endowed it with the capacity of inhibiting MIF. Covalent modification of MIF by phenylmethylsulfonyl fluoride (PMSF) resulted in binding of MIF-PMSF to CP immobilized on CM5 chip, the dissociation constant being 4.2 μM. In D-galactosamine-sensitized mice CP+Cu(II) increased the LPS-induced lethality from 54 to 100%, while administration of antibodies against MIF prevented the lethal effect. The enhancement by CP+Cu(II) of the pro-inflammatory signal of MIF is discussed.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Interaction of macrophage migration inhibitory factor with ceruloplasmin: role of labile copper ions

et al. 2015

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“…[21][22][23]. In recent years, interest for synthesis and application of styrylcyanine dyes has grown due to their use as a fluorescent probes in bioanalytical methods for DNA or RNA analyses [24,25].…”

Section: Introductionmentioning

confidence: 99%

Crystal structure and synthesis of benzimidazole substituted acrylonitriles and benzimidazo[1, 2-a]quinolines

2009

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The benzimidazole compounds and benzoannulated cyclic benzimidazole analogues, such as benzimidazo[1,2-a]quinolines, are a part of our wider investigation on biologically active compounds, potential antitumor drugs. Here, we present the synthesis of two compounds,[2-(1H-benzimidazol-2-yl)-3-(4-bromophenyl)-acrylonitrile, 5] and [2-bromo-benzimidazo[1,2-a]quinoline-6-carbonitrile, 7] and their crystal structures revealed by X-ray single crystal diffractometry. We also report the molecular and crystal structures of two additional compounds [2-(1H-benzimidazol-2-yl)-3-(4-cyanophenyl)-acrylonitrile, 4] and [benzimidazo[1,2-a]quinoline-2,6-dicarbonitrile, 6], whose synthesis and spectroscopic characterization have been published earlier by us too (Hranjec and Karminski-Zamola, Molecules 12:1817, 2007). The compounds 4 and 5 crystallize as monohydrates. The dihedral angles calculated between phenyl and benzimidazole ring reflect not significant deviation from molecular planarity in the crystalline state for 4 and 5, while benzoannulated cyclic benzimidazole derivatives 6 and 7 are essentially planar. The crystal structures of 4 and 5 are characterized by O-HÁÁÁN and N-HÁÁÁO hydrogen bonds between water molecule of crystallization and imidazole NH group as well as CN group, while in 6 and 7 only weak C-HÁÁÁN intermolecular hydrogen bonds exist. Although, crystal packings are analogous in 4 and 5, the molecular conformations differ slightly. In 6 there is one C-HÁÁÁN hydrogen bond that do not exist in 7.

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“…Two peptide fragments Lys50-Gln55, Ile65-Leu71-Pro76-Lys79-Lys109 and Asp929-Glu931-Glu932-Glu935-His940-Phe947-Arg1012 may be important for the interactions of ceruloplasmin with lactoferrin and myeloperoxidaze [63]. Fagments Arg883-Arg892 [64], His667-Trp669 [65] and loop Cys699-Leu710 [39] are probably involved in interactions of cerruloplasmin with myeloperoxidaze.…”

Section: Methodsmentioning

confidence: 99%

Rapid insight into C60 influence on biological functions of proteins

et al. 2017

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Experimental methods of investigations of nanoparticle (NP)-protein interactions are limited, because they require a high amount of samples and the NPs tend to interfere with spectral results. Therefore, molecular modeling is a commonly accepted tool in such kind of investigations. Examining the molecule toxicity on the molecular level, we usually want to know, mainly, the location of the ligand on the protein surface and what is an influence of such a contact on the biological functions of the protein. In the presented work, we demonstrate that multiple-docking of the ligand from a random start and with large grid volume, to let the ligand search the whole protein surface, allows to find the best binding sites and gives reliable results considering ligand-protein interactions. In the present work, we have constructed six models of bronchoalveolar lavage fluids proteins: α1-antitripsin, albumin, ceruloplasmin, lactoferrin, lysozyme, and transferrin with fullerene, C 60 utilizing molecular docking methods. The most probable results were examined with steered molecular dynamics (SMD) to see, if the simple docking method is able to predict the fullerene binding affinity. Albumin and lysozyme were already widely investigated and literature data is available for their complexes with fullerene C 60 and/or its derivatives. Thus, we used these two models as a reference set to validate the used molecular modeling methods. With our best knowledge, interactions of the remaining four proteins with NPs have never been investigated in detail before. Our results indicate that fullerene C 60 readily interacts with all studied proteins and may have a large impact on their biological functions.

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Identification of leukocyte cationic proteins that interact with ceruloplasmin

Cited by 25 publications

References 25 publications

Interaction of macrophage migration inhibitory factor with ceruloplasmin: role of labile copper ions

Interaction of macrophage migration inhibitory factor with ceruloplasmin: role of labile copper ions

Crystal structure and synthesis of benzimidazole substituted acrylonitriles and benzimidazo[1, 2-a]quinolines

Rapid insight into C60 influence on biological functions of proteins

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