Palladin Institute of Biochemistry NAS of Ukraine

Ukraine

Palladin Institute of Biochemistry NAS of Ukraine

Ukraine
SEARCH FILTERS
Time filter
Source Type

Zholobak N.M.,Ukrainian Academy of Sciences | Popov A.L.,Institute of Theoretical and Experimental Physics | Shcherbakov A.B.,Ukrainian Academy of Sciences | Popova N.R.,Institute of Theoretical and Experimental Physics | And 7 more authors.
Beilstein Journal of Nanotechnology | Year: 2016

Luminescent organic dots (O-dots) were synthesized via a one-pot, solvent-free thermolysis of citric acid in urea melt. The influence of the ratio of the precursors and the duration of the process on the properties of the O-dots was established and a mechanism of their formation was hypothesized. The multicolour luminescence tunability and toxicity of synthesized O-dots were extensively studied. The possible applications of O-dots for alive/fixed cell staining and labelling of layer-by-layer polyelectrolyte microcapsules were evaluated. © 2016 Zholobak et al.


Chernyshenko V.,Palladin Institute of biochemistry NAS of Ukraine | Petruk N.,Taras Shevchenko National University | Korolova D.,Palladin Institute of biochemistry NAS of Ukraine | Kasatkina L.,Palladin Institute of biochemistry NAS of Ukraine | And 7 more authors.
Croatian Medical Journal | Year: 2017

Aim To purify the platelet aggregation inhibitor from Echis multisquamatis snake venom (PAIEM) and characterize its effect on platelet aggregation and HeLa cell proliferation. Methods Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and matrix assisted laser desorption/ ionization time-of-flight (MALDI-TOF) were used for PAIEM identification. Platelet aggregation in the presence of PAIEM was studied on aggregometer Solar-AP2110. The changes of shape and granularity of platelets in the presence of PAIEM were studied on flow cytometer COULTER EPICS XL, and degranulation of platelets was estimated using spectrofluorimetry. Indirect enzyme-linked immunosorbent assay was used for the determination of target of PAIEM on platelet surface. An assay based on 3-(4,5-dimethylthiazol- 2-yl)-2,5-diphenyltetrazolium bromide was used to evaluate the effect of PAIEM on the proliferation of HeLa cells in cell culture. Results The molecular weight of the protein purified from Echis multisquamatis venom was 14.9 kDa. Half-maximal inhibitory concentration (IC50) of PAIEM needed to inhibit adenosine diphosphate (ADP)-induced platelet aggregation was 7 μM. PAIEM did not affect thrombin- or ADP-induced platelet activation, but it did prevent binding of the anti- IIb antibody to glycoprotein IIb/IIIa (GPIIbIIIa)-receptor of adhered platelets and inhibited the viability of HeLa cells by 54%. Conclusion As a member of the disintegrin family, PAIEM inhibited platelet aggregation and cell proliferation possibly by blocking integrin-mediated interactions. However, it did not impair cellular signaling causing any changes in platelet shape and granularity and did not affect ADP-induced platelet degranulation. This disintegrin was shown to be a potent inhibitor of integrin-mediated cellular interactions including platelet aggregation or cancer cell proliferation.


Uspenska K.,Palladin Institute of Biochemistry NAS of Ukraine | Lykhmus O.,Palladin Institute of Biochemistry NAS of Ukraine | Gergalova G.,Palladin Institute of Biochemistry NAS of Ukraine | Chernyshov V.,Palladin Institute of Biochemistry NAS of Ukraine | And 2 more authors.
Neuroscience Letters | Year: 2017

Several nicotinic acetylcholine receptor (nAChR) subtypes are expressed in mitochondria to regulate the internal pathway of apoptosis in ion channel-independent manner. However, the mechanisms of nAChR activation in mitochondria and targeting to mitochondria are still unknown. Nicotine has been shown to favor nAChR pentamer assembly, folding, and maturation on the way of biosynthesis. The idea of the present work was to determine whether nicotine affects the content, glycosylation, and function of mitochondrial nAChRs. Experiments were performed in isolated liver mitochondria from mice, that either consumed or not nicotine with the drinking water (200 μL/L) for 7 days. Mitochondria detergent lysates were studied by sandwich or lectin ELISA for the presence and carbohydrate composition of different nAChR subunits. Intact mitochondria were examined by flow cytometry for the binding of fluorescently labeled α-cobratoxin and were tested in functional assay of cytochrome c release under the effect of either Ca2+ or wortmannin in the presence or absence of nAChR-selective ligands, including PNU-282987 (1 nM), dihydro-β-erythroidine (DhβE, 1 μM), PNU-120596 (0.3, 3, or 10 μM) and desformylflustrabromine hydrochloride (dFBr, 0.001, 0.3, or 1 μM). It was found that nicotine consumption increased the ratio of mitochondrial vs non-mitochondrial nAChRs in the liver, enhanced fucosylation of mitochondrial nAChRs, but prevented the binding of α-cobratoxin and the cytochrome c release-attenuating effects of nAChR-specific agonists, antagonists, or positive allosteric modulators. It is concluded that nicotine consumption in vivo favors nAChR glycosylation and trafficking to mitochondria but makes them less susceptible to the effects of specific ligands. © 2017 Elsevier B.V.


Chernyshenko V.,Palladin Institute of Biochemistry NAS of Ukraine | Platonova T.,Palladin Institute of Biochemistry NAS of Ukraine | Makogonenko Y.,Palladin Institute of Biochemistry NAS of Ukraine | Rebriev A.,Palladin Institute of Biochemistry NAS of Ukraine | And 3 more authors.
Biochimie | Year: 2014

The variety of enzymes including serine proteases that possess fibrin(ogen)olytic and platelet modulating activity have been discovered in different snake venoms. In our work the fibrin(ogen)olytic and platelet modulating activity of a new protease from Echis multisquamatis snake venom was studied. It was shown that purified enzyme cleaved the BβR42-A43 bond of fibrinogen during first contact with the substrate following much slower hydrolysis of C-terminus of fibrinogen Aα-chain. Protease hydrolysed fibrin clot too, but at much slower rate and cleaved both C-terminus of Aα-chain and BβR42-A43 bond of Bβ-chain simultaneously. Preincubation of fibrinogen with protease dramatically elongated thrombin clotting time and the clot formed from a mixture of native fibrinogen and fibrinogen desBβ(1-42)2 digested by plasmin much faster than a native fibrin clot. The protease did not activate platelets nor cause changes in their shape and granularity, but it reduced platelets aggregation induced by ADP. © 2014 Elsevier Masson SAS. All rights reserved.

Loading Palladin Institute of Biochemistry NAS of Ukraine collaborators
Loading Palladin Institute of Biochemistry NAS of Ukraine collaborators