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18 results on '"I. M. Kolesnikova"'

1. Features of the intestinal microbiome in athletes engaged in martial arts

Author

A. V. Shestopalov, R. F. Fatkhullin, T. V. Grigorieva, D. S. Martykanova, N. H. Davletova, I. M. Kolesnikova, A. A. Ivanova, and S. A. Roumiantsev

Subjects
microbiome, lactate, prebiotics, mucin, muscle fibers, Sports medicine, RC1200-1245
Abstract

The purpose of the study: the study of the characteristics of the intestinal microbiome in young men who are professionally engaged in sports.Materials and methods: the study involved 36 young men aged 18 to 26 years. Fecal samples were taken from the study participants and then bacterial DNA was isolated from the obtained samples.Results: comparing the intestinal microbe of athletes with the control group, it is possible to trace the positive effect of sports on the overall diversity of representatives of the intestinal microbiota. When analyzing the taxonomic composition, it is worth separately noting the increase in representatives of lactate-producing bacteria and the increased content of Akkermansia muciniphila in athletes.Conclusions: the results of the study indicate the effects of sports training on the human gut microbiota and suggest the presence of a close two-way relationship “microbiome — muscle tissue”.

Published
2024
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2. Novel monoclonal antibody to fibrin(ogen) αC-region for detection of the earliest forms of soluble fibrin

Author

N. E. Lugovska, I. M. Kolesnikova, Ye. M. Stohnii, V. O. Chernyshenko, A. V. Rebriev, O. P. Kostiuchenko, G .K. Gogolinska, N. A. Dziubliuk, L. D. Varbanets, T. M. Platonova, and S. V. Komisarenko

Subjects
fibrin, fibrinogen, hemostasis, immunodiagnostics, monoclonal antibody, αc-region of the molecule fibrin(ogen), Biochemistry, QD415-436, Medicine, Biology (General), QH301-705.5
Abstract

Obtaining new monoclonal antibodies (mAbs) towards fibrin(ogen) and its fragments is an important task for studying mechanisms of blood clot formation, searching for novel antithrombotic agents and developing immunodiagnostics. The aim of the present work was to create and characterize a new mAb towards the fibrin(ogen) αС-region. We surmise that having a specific mAb towards this flexible part of the molecule will allow us to study the role of the αС-region in fibrin polymerization and also to develop an approach for detecting the earliest forms of soluble fibrin by sandwich ELISA. Using hybridoma technology we оbtained mAb 1-5A to the αC-region of fibrinogen.. It was characterized using several variations of ELISA and Western blot. Application of specific proteases together with MALDI-TOF analysis allowed us to localize its epitope that is located in fragment 537-595 of the Aα-chain of fibrin(ogen). МAb 1-5A can be used as a detecting tag-antibody in sandwich ELISA for the quantification of the earliest forms of soluble fibrin which are uncleaved by plasmin and preserved C-terminal portions of αC-regions. These earliest forms of soluble fibrin are direct evidence of blood coagulation system activation, thrombin generation and the danger of intravascular thrombus formation. Their determination will provide additional, more accurate information about the state of the blood coagulation system and the risk of blood clotting, which is very important for the timely and correct selection of adequate antithrombotic therapy. MAb 1-5A effectively binds the αC-containing molecules of fibrinogen and fibrin in blood plasma. It also can be used for studying protein-protein and protein-cellular interactions of the αC-regions of fibrin(ogen).

Published
2020
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3. Comparative analysis of the influence of chlorine and fluorine anions on the fibrin polymerization

Author

L. V. Pyrogova, G. K. Bereznitsky, G. K. Gogolinskaya, T. M. Platonova, I. M. Kolesnikova, O. O. Masenko, R. Yu. Marunich, P. Yu. Tsap, Yu. V. Ushenin, Y. M. Makogonenko, and E. V. Lugovskoi

Subjects
chlorine and fluorine anions, fibrin, fibrinogen, polymerization, Biochemistry, QD415-436, Medicine, Biology (General), QH301-705.5
Abstract

The effect of NaCl and NaF salts in the range of 0.1-0.225 M concentrations on individual stages of fibrin polymerization was investigated, namely: the rate of fibrinogen activation by thrombin, the rate of protofibrils formation, the rate of lateral association of protofibrils, and the maximum clot absorbance value at 350 nm. It was found that the chlorine and fluorine anions equally inhibit the rate of formation of fibrin from fibrinogen and the formation of protofibrils activated with thrombin. Chlorine anions were shown to be significantly more effective than fluorine anions, inhibiting the rate of lateral association and maximal clot absorban­ce level from fibrin desA and desAB. A component of the inhibitory action of chlorine anions, not related to the ionic strength of the solution, was identified and its effect on the individual polymerization steps was shown. Chlorine anions were found to bind to a fibrin clot. Using the surface plasmon resonance method and fibrin-specific mAb FnI-3c, it was established that the rate of exposure of neoantigenic determinants of mAb in the hinge regions of the fibrinogen molecule during its transformation into fibrin under the action of thrombin is inhibited by chlorine anions in correlation with inhibition of the protofibril lateral association rate. It has been suggested that the inhibitory effect of chlorine anions consists of an ionic component and a component that blocks the conformational mobility of the molecule by the chlorine anions binding to its hinge regions and polymerization sites.

Published
2019
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4. Overall hemostasis potential of the blood plasma and its relation to some molecular markers of the hemostasis system in patients with chronic renal disease of stage VD

Author

B. G. Storozhuk, L. V. Pyrogova, T. M. Chernyshenko, O. P. Kostiuchenko,, I. M. Kolesnikova, T. M. Platonova, O. B. Storozhuk, L. O. Storozhuk, G. K. Bereznitsky, P. Yu. Tsap, O. O. Masenko, E. M. Makogonenko, and E. V. Lugovskoy

Subjects
D-dimer, fibrinogen, hemostasis potential of plasma, protein C, soluble fibrin, Biochemistry, QD415-436, Medicine, Biology (General), QH301-705.5
Abstract

The values of the coagulation, overall and fibrinolysis potentials were estimated by the method of the global potential of Blomback M., as well as the values of concentrations of molecular markers of the hemostasis system: soluble fibrin (sf), D-dimer, fibrinogen (Fg) and protein C (88 patients, 52 of them men, 36 women). It was shown that hemostasis system activity in women plasma is higher than that in men plasma. The division of patients into 3 groups, depending on the concentration of sf: less than normal – sf ≤ 3, about norm – 3 < sf < 4 and more than norm – sf > 4 μg/ml, allowed establishing the growth of the parameters of both the hemostatic potential and concentrations of molecular markers in accordance with concentration of sf in the groups of patients. Paerson’s correlation analysis of the relationship between the parameters of the hemostasis potential and concentrations of molecular markers revealed an increase in the correlation relationship to the strong and very strong between the parameters of coagulation, fibrinolysis and protein C systems with an increase in the concentration of soluble fibrin in plasma of patients.

Published
2018
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5. Mapping of residues of fibrinogen cleaved by protease II of Bacillus thuringiensis var. israelensis IMV B-7465

Author

E. M. Stohniy, V. O. Chernyshenko, N. A. Nidialkova, A. V. Rebriev, L. D. Varbanets, V. E. Hadzhynova, T. M. Chernyshenko, I. M. Kolesnikova, and E. V. Lugovskoy

Subjects
Biochemistry, QD415-436, Medicine, Biology (General), QH301-705.5
Abstract

The limited proteolysis of macromolecules allows obtaining the fragments that preserve the structure and functional properties of the whole molecule and could be used in the study of proteins structure and function. Proteases targeted to fibrinogen and fibrin are of interest as the tool for obtaining of functionally active fragments of fibrin(ogen) and for the direct defibrination in vivo. That is why the aim of the present work was to study the proteolytic action of Protease II (PII) purified from Bacillus thuringiensis var. israelensis IMV B-7465 on fibrinogen. Hydrolysis products of fibrinogen by PII were analysed by SDS-PAGE under reducing conditions with further immunoprobing using the mouse monoclonal 1-5A (anti-Aα509-610) and ІІ-5С (anti-Aα20-78) antibodies. It was shown that PII cleaved preferentially the Aα-chain of fibrinogen splitting off the peptide with apparent molecular weight of 10 kDa that corresponded the C-terminal part of Aα-chain of fibrinogen molecule. MALDI-TOF analysis of hydrolysis of fibrinogen was performed using a Voyager-DE. Results analyzed by Data Explorer 4.0.0.0 allowed to detect the main peak occurring at mass/charge (M/Z) ratio of 11 441 Da. According to “Peptide Mass Calculator” this peptide corresponded to fragment Аα505-610 of fibrinogen molecule. The result showed that PII cleaves the peptide bond AαAsp-Thr-Ala504-Ser505. Thus, PII can be used for the obtaining of unique fragments of fibrinogen molecule. As far as αC-domain contains numerous sites of fibrin intermolecular interactions we can consider PII as a prospective agent for their study and for the defibrination.

Published
2016
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9. Novel monoclonal antibody to fibrin(ogen) αC-region for detection of the earliest forms of soluble fibrin

Author

Platonova Tm, I. M. Kolesnikova, G .K. Gogolinska, Serhiy Komisarenko, N. E. Lugovska, A. V. Rebriev, L. D. Varbanets, Ye. M. Stohnii, N. A. Dziubliuk, V. O. Chernyshenko, and O. P. Kostiuchenko

Subjects
biology, medicine.drug_class, Chemistry, immunodiagnostics, Monoclonal antibody, C region, Biochemistry, Molecular biology, Fibrin, lcsh:Biochemistry, αc-region of the molecule fibrin(ogen), monoclonal antibody, medicine, biology.protein, hemostasis, lcsh:QD415-436, fibrin, fibrinogen, Soluble fibrin
Abstract

Obtaining new monoclonal antibodies (mAbs) towards fibrin(ogen) and its fragments is an important task for studying mechanisms of blood clot formation, searching for novel antithrombotic agents and developing immunodiagnostics. The aim of the present work was to create and characterize a new mAb towards the fibrin(ogen) αС-region. We surmise that having a specific mAb towards this flexible part of the molecule will allow us to study the role of the αС-region in fibrin polymerization and also to develop an approach for detecting the earliest forms of soluble fibrin by sandwich ELISA. Using hybridoma technology we оbtained mAb 1-5A to the αC-region of fibrinogen.. It was characterized using several variations of ELISA and Western blot. Application of specific proteases together with MALDI-TOF analysis allowed us to localize its epitope that is located in fragment 537-595 of the Aα-chain of fibrin(ogen). МAb 1-5A can be used as a detecting tag-antibody in sandwich ELISA for the quantification of the earliest forms of soluble fibrin which are uncleaved by plasmin and preserved C-terminal portions of αC-regions. These earliest forms of soluble fibrin are direct evidence of blood coagulation system activation, thrombin generation and the danger of intravascular thrombus formation. Their determination will provide additional, more accurate information about the state of the blood coagulation system and the risk of blood clotting, which is very important for the timely and correct selection of adequate antithrombotic therapy. MAb 1-5A effectively binds the αC-containing molecules of fibrinogen and fibrin in blood plasma. It also can be used for studying protein-protein and protein-cellular interactions of the αC-regions of fibrin(ogen).

Published
2020

10. THE MECHANISM OF CLOTS FORMATION IN BLOOD PLASMA UNDER THE ACTION OF CHITIN DERIVATIVES

Author

Ushkalov V.O, V H Spiridonov, I M Kolesnikova, O V Gornitska, E M Stognij, A V Petik, and T M Chernyshenko

Subjects
haemostasis system, lcsh:Biotechnology, macromolecular substances, chitin and its derivates, carbohydrates (lipids), chemistry.chemical_compound, Action (philosophy), Chitin, chemistry, lcsh:TP248.13-248.65, Blood plasma, Biophysics, fibrinogen, Mechanism (sociology)
Abstract

The aim of the research was to find out the clot formation by the action of chitin derivates. The biochemical and immunologic investigation methods such as obtaining of fibrinogen, chitosan derivates, electrophoresis in PAAG, Western blot analysis, ELISE, the activated partial thromboplastin time and prothrombin time coagulological tests were used in these studies. The next results were obtained: chitin derivatives in equal measure cause the clot formation in whole blood, blood plasma and fibrinogen solution; the fibrinogen precipitate formed as a result of their action, practically does not contain fibrin; chitosan does not cause the activation of coagulation factors and the absence of newly-formed fibrin confirms it; the addition of calcium chloride to fibrinogen solution in concentration-dependent manner inhibits effect of chitosan. Thus, under the action of chitosan, a fibrinogen precipitate forms due to the destabilization of its molecule by the lack of calcium. Absence of fibrin degradation products excludes the possibility of the fibrinolytic system activation and physiological degradation of the clot. It makes no sense to use haemostatic drugs based on chitosan in clinical practice.

Published
2019
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12. 37th International Symposium on Intensive Care and Emergency Medicine (part 2 of 3)

Author

D. Rob, R. Špunda, J. Lindner, J. Šmalcová, O. Šmíd, T. Kovárník, A. Linhart, J. Bìlohlávek, M. M. Marinoni, G. Cianchi, S. Trapani, M. L. Migliaccio, L. Gucci, M. Bonizzoli, A. Cramaro, M. Cozzolino, S. Valente, A. Peris, E. Grins, E. Kort, M. Weiland, N. Manandhar Shresta, P. Davidson, L. Algotsson, S. Fitch, G. Marco, J. Sturgill, S. Lee, M. Dickinson, T. Boeve, A. Khaghani, P. Wilton, S. Jovinge, A. N. Ahmad, R. Loveridge, S. Vlachos, S. Patel, E. Gelandt, L. Morgan, S. Butt, M. Whitehorne, V. Kakar, C. Park, M. Hayes, C. Willars, T. Hurst, T. Best, A. Vercueil, G. Auzinger, B. Adibelli, N. Akovali, A. Torgay, P. Zeyneloglu, A. Pirat, Z. Kayhan, S. S. Schmidbauer, J. Herlitz, T. Karlsson, H. Friberg, R. Knafelj, P. Radsel, F. Duprez, T. Bonus, G. Cuvelier, S. Mashayekhi, M. Maka, S. Ollieuz, G. Reychler, R. Mosaddegh, S. Abbasi, S. Talaee, V. Z. Zotzmann, D. S. Staudacher, T. W. Wengenmayer, D. D. Dürschmied, C. B. Bode, A. Nelskylä, J. Nurmi, M. Jousi, A. Schramko, E. Mervaala, G. Ristagno, M. Skrifvars, G. Ozsoy, T. Kendirli, E. Azapagasi, O. Perk, U. Gadirova, E. Ozcinar, M. Cakici, C. Baran, S. Durdu, A. Uysalel, M. Dogan, M. Ramoglu, T. Ucar, E. Tutar, S. Atalay, R. Akar, M. Kamps, G. Leeuwerink, J. Hofmeijer, O. Hoiting, J. Van der Hoeven, C. Hoedemaekers, A. Konkayev, V. Kuklin, T. Kondratyev, M. Konkayeva, N. Akhatov, M. Sovershaev, T. Tveita, V. Dahl, L. Wihersaari, M. B. Skrifvars, S. Bendel, K. M. Kaukonen, J. Vaahersalo, J. Romppanen, V. Pettilä, M. Reinikainen, A. Lybeck, T. Cronberg, N. Nielsen, M. Rauber, K. Steblovnik, A. Jazbec, M. Noc, P. Kalasbail, F. Garrett, E. Kulstad, D. J. Bergström, H. R. Olsson, S. Schmidbauer, I. Mandel, S. Mikheev, Y. Podoxenov, I. Suhodolo, A. Podoxenov, J. Svirko, A. Sementsov, L. Maslov, V. Shipulin, L. V. Vammen, S. R. Rahbek, N. S. Secher, J. P. Povlsen, N. J. Jessen, B. L. Løfgren, A. G. Granfeldt, A. Grossestreuer, S. Perman, P. Patel, S. Ganley, J. Portmann, M. Cocchi, M. Donnino, Y. Nassar, S. Fathy, A. Gaber, S. Mokhtar, Y. C. Chia, R. Lewis-Cuthbertson, K. Mustafa, A. Sabra, A. Evans, P. Bennett, W. Eertmans, C. Genbrugge, W. Boer, J. Dens, C. De Deyne, F. Jans, A. Skorko, M. Thomas, M. Casadio, A. Coppo, A. Vargiolu, J. Villa, M. Rota, L. Avalli, G. Citerio, J. B. Moon, J. H. Cho, C. W. Park, T. G. Ohk, M. C. Shin, M. H. Won, P. Papamichalis, V. Zisopoulou, E. Dardiotis, S. Karagiannis, D. Papadopoulos, T. Zafeiridis, D. Babalis, A. Skoura, I. Staikos, A. Komnos, S. Silva Passos, F. Maeda, L. Silva Souza, A. Amato Filho, T. Araújo Guerra Granjeia, M. Schweller, D. Franci, M. De Carvalho Filho, T. Martins Santos, P. De Azevedo, R. Wall, I. Welters, P. Tansuwannarat, P. Sanguanwit, T. Langer, M. Carbonara, A. Caccioppola, C. Ferraris Fusarini, E. Carlesso, E. Paradiso, M. Battistini, E. Cattaneo, F. Zadek, R. Maiavacca, N. Stocchetti, A. Pesenti, A. Ramos, F. Acharta, J. Toledo, M. Perezlindo, L. Lovesio, A. Dogliotti, C. Lovesio, N. Schroten, B. Van der Veen, M. C. De Vries, J. Veenstra, Y. B. Abulhasan, S. Rachel, M. Châtillon-Angle, N. Alabdulraheem, I. Schiller, N. Dendukuri, M. Angle, C. Frenette, S. Lahiri, K. Schlick, S. A. Mayer, P. Lyden, M. Akatsuka, J. Arakawa, M. Yamakage, J. Rubio, J. A. Rubio Mateo-Sidron, R. Sierra, M. Celaya, L. Benitez, S. Alvarez-Ossorio, A. Fernandez, O. Gonzalez, H. Engquist, E. Rostami, P. Enblad, L. Canullo, J. Nallino, M. Perreault, J. Talic, A. J. Frenette, L. Burry, F. Bernard, D. R. Williamson, D. Adukauskiene, J. Cyziute, A. Adukauskaite, L. Malciene, L. Luca, A. Rogobete, O. Bedreag, M. Papurica, M. Sarandan, C. Cradigati, S. Popovici, C. Vernic, D. Sandesc, V. Avakov, I. Shakhova, H. Trimmel, M. Majdan, G. H. Herzer, C. S. Sokoloff, M. Albert, D. Williamson, C. Odier, J. Giguère, E. Charbonney, Z. Husti, T. Kaptás, Z. Fülep, Z. Gaál, M. Tusa, J. Donnelly, M. Aries, M. Czosnyka, C. Robba, M. Liu, A. Ercole, D. Menon, P. Hutchinson, P. Smielewski, R. López, J. Graf, J. M. Montes, M. Kenawi, A. Kandil, K. Husein, A. Samir, J. Heijneman, J. Huijben, F. Abid-Ali, M. Stolk, J. Van Bommel, H. Lingsma, M. Van der Jagt, R. C. Cihlar, G. Mancino, P. Bertini, F. Forfori, F. Guarracino, D. Pavelescu, I. Grintescu, L. Mirea, S. Alamri, M. Tharwat, N. Kono, H. Okamoto, H. Uchino, T. Ikegami, T. Fukuoka, M. Simoes, E. Trigo, P. Coutinho, J. Pimentel, A. Franci, D. Basagni, M. Boddi, V. Anichini, A. Cecchi, D. Markopoulou, K. Venetsanou, I. Papanikolaou, T. Barkouri, D. Chroni, I. Alamanos, E. Cingolani, M. G. Bocci, L. Pisapia, A. Tersali, S. L. Cutuli, V. Fiore, A. Palma, G. Nardi, M. Antonelli, R. Coke, A. Kwong, D. J. Dwivedi, M. Xu, E. McDonald, J. C. Marshall, A. E. Fox-Robichaud, P. C. Liaw, I. Kuchynska, I. R. Malysh, L. V. Zgrzheblovska, L. Mestdagh, E. F. Verhoeven, I. Hubloue, J. Ruel-laliberte, R. Zarychanski, F. Lauzier, P. Lessard Bonaventure, R. Green, D. Griesdale, R. Fowler, A. Kramer, D. Zygun, T. Walsh, S. Stanworth, C. Léger, A. F. Turgeon, D. M. Baron, J. Baron-Stefaniak, G. C. Leitner, R. Ullrich, O. Tarabrin, A. Mazurenko, Y. Potapchuk, D. Sazhyn, P. Tarabrin, A. González Pérez, J. Silva, V. Artemenko, A. Bugaev, I. Tokar, S. Konashevskaya, I. M. Kolesnikova, E. V. Roitman, T. Rengeiné Kiss, Z. Máthé, L. Piros, E. Dinya, E. Tihanyi, A. Smudla, J. Fazakas, R. Ubbink, P. Boekhorst te, E. Mik, L. Caneva, G. Ticozzelli, S. Pirrelli, D. Passador, F. Riccardi, F. Ferrari, E. M. Roldi, M. Di Matteo, I. Bianchi, G. A. Iotti, G. Zurauskaite, A. Voegeli, M. Meier, D. Koch, S. Haubitz, A. Kutz, M. Bargetzi, B. Mueller, P. Schuetz, G. Von Meijenfeldt, M. Van der Laan, C. Zeebregts, K. B. Christopher, P. Vernikos, T. Melissopoulou, G. Kanellopoulou, M. Panoutsopoulou, D. Xanthis, K. Kolovou, T. Kypraiou, J. Floros, H. Broady, C. Pritchett, M. Marshman, N. Jannaway, C. Ralph, C. L. Lehane, C. K. Keyl, E. Z. Zimmer, D. T. Trenk, A. S. Ducloy-Bouthors, M. J. Jonard, F. Fourrier, F. Piza, T. Correa, A. Marra, J. Guerra, R. Rodrigues, A. Vilarinho, V. Aranda, S. Shiramizo, M. R. Lima, E. Kallas, A. B. Cavalcanti, M. Donoso, P. Vargas, J. McCartney, S. Ramsay, K. McDowall, I. Novitzky-Basso, C. Wright, M Grgic Medic, L Bielen, V Radonic, O Zlopasa, N Gubarev Vrdoljak, V Gasparovic, R Radonic, G. Narváez, D. Cabestrero, L. Rey, M. Aroca, S. Gallego, J. Higuera, R. De Pablo, L. Rey González, G. Narváez Chávez, J. Higuera Lucas, D. Cabestrero Alonso, M. Aroca Ruiz, L. Jaramillo Valarezo, R. De Pablo Sánchez, A. Quinza Real, T. W. Wigmore, I. Bendavid, J. Cohen, I. Avisar, I. Serov, I. Kagan, P. Singer, J Hanison, U Mirza, D Conway, A. Takasu, H. Tanaka, N. Otani, S. Ohde, S. Ishimatsu, F Coffey, P Dissmann, K Mirza, M Lomax, P. Dissmann, F. Coffey, K. Mirza, M. Lomax, JR Miner, R Leto, AM Markota, PG Gradišek, VA Aleksejev, AS Sinkovič, S. Romagnoli, C. Chelazzi, G. Zagli, F. Benvenuti, P. Mancinelli, P. Boninsegni, L. Paparella, A. T. Bos, O. Thomas, T. Goslar, A. Martone, P. R. Sandu, V. A. Rosu, A. Capilnean, P. Murgoi, A. Lecavalier, D. Jayaraman, P. Rico, P. Bellemare, C. Gelinas, T. Nishida, T. Kinoshita, N. Iwata, K. Yamakawa, S. Fujimi, L. Maggi, F. Sposato, G. Citterio, C. Bonarrigo, M. Rocco, V. Zani, R. A. De Blasi, D Alcorn, L Barry, M. A. Riedijk, D. M. Milstein, J. Caldas, R. Panerai, L. Camara, G. Ferreira, E. Bor-Seng-Shu, M. Lima, F. Galas, N. Mian, R. Nogueira, G. Queiroz de Oliveira, J. Almeida, J. Jardim, T. G. Robinson, F. Gaioto, L. A. Hajjar, I. Zabolotskikh, T. Musaeva, W. Saasouh, J. Freeman, A. Turan, S. Saseedharan, E. Pathrose, S. Poojary, J. Messika, Y. Martin, N. Maquigneau, M. Henry-Lagarrigue, C. Puechberty, A. Stoclin, L. Martin-Lefevre, F. Blot, D. Dreyfuss, A. Dechanet, D. Hajage, J. Ricard, E. Almeida, G. Landoni, J. Fukushima, E. Fominskiy, C. De Brito, L. Cavichio, L. Almeida, U. Ribeiro, E. Osawa, R. Boltes, L. Battistella, L. Hajjar, P. Fontela, T. Lisboa, L. Forgiarini Junior, G. F. Friedman, F. Abruzzi, J. Azevedo Peixoto Primo, P. Marques Filho, J. Stormorvski de Andrade, K. Matos Brenner, M. Scorsato boeira, C. Leães, C. Rodrigues, A. Vessozi, A. SantAnna Machado, M. Weiler, H. Bryce, A. Hudson, T. Law, R. Reece-Anthony, A. Molokhia, F. Abtahinezhadmoghaddam, E. Cumber, L. Channon, A. Wong, R. Groome, D. Gearon, J. Varley, A. Wilson, J. Reading, F. G. Zampieri, F. A. Bozza, M. Ferez, H. Fernandes, A. Japiassú, J. Verdeal, A. C. Carvalho, M. Knibel, J. I. Salluh, M. Soares, J. Gao, E. Ahmadnia, B. Patel, A. MacKay, S. Binning, R. J. Pugh, C. Battle, C. Hancock, W. Harrison, T. Szakmany, F. Mulders, J. Vandenbrande, J. Dubois, B. Stessel, K. Siborgs, D. Ramaekers, U. V. Silva, W. S. Homena, G. C. Fernandes, A. P. Moraes, L. Brauer, M. F. Lima, F. De Marco, N. Maric, M. Mackovic, N. Udiljak, CE Bosso, RD Caetano, AP Cardoso, OA Souza, R Pena, MM Mescolotte, IA Souza, GM Mescolotte, H. Bangalore, E. Borrows, D. Barnes, V. Ferreira, L. Azevedo, G. Alencar, A. Andrade, A. Bierrenbach, L. Tadini Buoninsegni, L. Cecci, J. Lindskog, K. Rowland, P. Sturgess, A. Ankuli, R Rosa, T Tonietto, A Ascoli, L Madeira, W Rutzen, M Falavigna, C Robinson, J Salluh, A Cavalcanti, L Azevedo, R Cremonese, D Da Silva, A Dornelles, Y Skrobik, J Teles, T Ribeiro, C Eugênio, C Teixeira, M. Zarei, H. Hashemizadeh, M. Eriksson, G. Strandberg, M. Lipcsey, A. Larsson, M. Lignos, E. Crissanthopoulou, K. Flevari, P. Dimopoulos, A. Armaganidis, JG Golub, AS Stožer, H. Rüddel, C. Ehrlich, C. M. Burghold, C. Hohenstein, J. Winning, W. Sellami, Z. Hajjej, M. Bousselmi, H. Gharsallah, I. Labbene, M. Ferjani, J. Sattler, D. Steinbrunner, H. Poppert, G. Schneider, M. Blobner, K. G. Kanz, S. J. Schaller, K. Apap, G. Xuereb, L. Massa, N. Delvau, A Penaloza, G Liistro, F Thys, I. K. Delattre, P. Hantson, P. M. Roy, P. Gianello, L Hadîrcă, A Ghidirimschi, N Catanoi, N Scurtov, M Bagrinovschi, Y. S. Sohn, Y. C. Cho, B. Golovin, O. Creciun, A. Ghidirimschi, M. Bagrinovschi, R. Tabbara, J. Z. Whitgift, A. Ishimaru, A. Yaguchi, N. Akiduki, M. Namiki, M. Takeda, J. N. Tamminen, A. Uusaro, C. G. Taylor, E. D. Mills, A. D. Mackay, C. Ponzoni, R. Rabello, A. Serpa, M. Assunção, A. Pardini, G. Shettino, T. Corrêa, P. V. Vidal-Cortés, L. Álvarez-Rocha, P. Fernández-Ugidos, A. Virgós-Pedreira, M. A. Pérez-Veloso, I. M. Suárez-Paul, L. Del Río-Carbajo, S. Pita Fernández, A. Castro-Iglesias, A. Butt, A. A. Alghabban, S. K. Khurshid, Z. A. Ali, I. N. Nizami, N. S. Salahuddin, M. Alshahrani, A. W. Alsubaie, A. S. Alshamsy, B. A. Alkhiliwi, H. K. Alshammari, M. B. Alshammari, N. K. Telmesani, R. B. Alshammari, L. P. Asonto, L. P. Damiani, F Bozza, A. El Khattate, M. Bizrane, N. Madani, J. Belayachi, R. Abouqal, D. Ramnarain, B. Gouw-Donders, C. Benstoem, A. Moza, P. Meybohm, C. Stoppe, R. Autschbach, D. Devane, A. Goetzenich, L. U. Taniguchi, L. Araujo, G. Salgado, J. M. Vieira, J. Viana, N. Ziviani, I. Pessach, A. Lipsky, A. Nimrod, M. O´Connor, I. Matot, E. Segal, A. Kluzik, A. Gradys, P. Smuszkiewicz, I. Trojanowska, M. Cybulski, A. De Jong, M. Sebbane, G. Chanques, S. Jaber, R. Rosa, C. Robinson, M. Bessel, L. Cavalheiro, L. Madeira, W. Rutzen, R. Oliveira, J. Maccari, M. Falavigna, E. Sanchez, F. Dutra, C. Dietrich, P. Balzano, J. Rezende, C. Teixeira, S. Sinha, K. Majhi, J. G. Gorlicki, F. P. Pousset, J. Kelly, J. Aron, A. Crerar Gilbert, N. Prevec Urankar, M. Irazabal, M. Bosque, J. Manciño, A. Kotsopoulos, N. Jansen, W. Abdo, Ú. M. Casey, B. O’Brien, R. Plant, and B. Doyle

Subjects
Fatal outcome, business.industry, Traumatic brain injury, 030208 emergency & critical care medicine, 030204 cardiovascular system & hematology, Critical Care and Intensive Care Medicine, medicine.disease, Outcome (game theory), 03 medical and health sciences, 0302 clinical medicine, Anesthesia, Medicine, business, Acute subdural hematoma
Published
2017
Full Text
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13. [Evaluation of the blood coagulation system after surgeries on abdominal aortic aneurysms]

Author

P I, Nikul'nikov, O V, Liksunov, A V, Ratushniuk, E V, Lugovs'koĭ, I M, Kolesnikova, L M, Lytvynova, O P, Kostiuchenko, T M, Chernyshenko, O V, Hornyts'ka, and T M, Platonova

Subjects
Male, Fibrin, Anticoagulants, Fibrinogen, Thrombosis, Middle Aged, Prognosis, Fibrin Fibrinogen Degradation Products, Solubility, Humans, Aorta, Abdominal, Blood Coagulation Tests, Blood Coagulation, Aortic Aneurysm, Abdominal
Abstract

Basing on data of analysis of the hemostasis system state in the patients, suffering abdominal aorta aneurysm, a tendency for raising of postoperative soluble fibrin and D-dimer content in the blood plasm and reduction of these indices on the third day was noted. The abovementioned markers content depends on the aneurysm size, the fibrin deposits presence, the terms from clinical signs beginning to the certain therapy administration and anticoagulants application. Information about correlation between content of D-dimer and soluble fibrin in the treatment dynamics is important for determination of activation degree in the patients blood coagulation system and the thrombotic complications prognosis.

Published
2013

14. [Features of plasminogen activation in a complex with antiplasminogen monoclonal antibody IV-1C]

Author

O Iu, Slominsk'kyĭ, Ie M, Makohonenko, I M, Kolesnikova, and S A, Cederholm-Williams

Subjects
Epitopes, Antibodies, Monoclonal, Plasminogen, Amides, Catalysis
Abstract

Antiplasminogen monoclonal antibody IV-1c (IV-1c) with antigenic determinant in V709-G718 site of plasminogen (Pg) protease domain (Druzhina N.N. et al. 1996.) can induce catalytic activity in Pg moiety of the complex. Catalytic activity appeared in Pg-IV-1c complex after approximately 2 h lag-period. Rate of Lys-Pg activation was higher then that of Glu-Pg. Amidolytic activity of Pg-SK equimolar complex was completely inhibited by IV-1c at 2:1 = Pg:IV-1c molar ratio. At constant Glu-Pg concentration increasing of the IV-1c concentration to equimolar of Pg accelerated Pg activation. Subsequent increase of IV-1c concentration inhibited the Pg activation sharply. Increasing of Glu-Pg concentration at constant IV-1c one did not inhibit Glu-Pg activation in Pg-IV-1c complex. The rate dependence of Pg activation from Glu-Pg-IV-1c complex concentration curve had bell-shaped form with maximum at 500 nM. Electrophoretic analysis of components of Glu-Pg-IV-1c complex showed that Lys-Pg and Lys-Pm were not observed at 100 nM complex concentration for 6 h period of reaction. At 680 nM concentration Glu-Pg-IV-1c complex these forms appeared in initial moments of reaction activation after lag-period. Kinetic scheme and peculiarities of Pg activation reaction in Pg-IV-1c complex are discussed.

Published
2000

16. [Immunochemical properties of a soluble immune complex from the blood serum of cancer patients]

Author

I M, Kolesnikova, E G, Kostrzhevskaia, and E I, Polianskaia

Subjects
Chromatography, Erythrocytes, Sheep, Immunochemistry, Antigen-Antibody Complex, Hemagglutination Tests, Molecular Weight, Coombs Test, Epitopes, Mice, Immunoglobulin G, Neoplasms, Chromatography, Gel, Animals, Humans, Immunization, Antigens, Carcinoma, Ehrlich Tumor, Antilymphocyte Serum
Published
1974

17. [Studies on the heterogeneity of blood serum high-molecular fraction proteins in healthy people and patients with cancer]

Author

O G, Kostrzhevs'ka, I M, Kolesnikova, V P, Korotkoruchko, and T L, Grigor'eva

Subjects
Molecular Weight, Reference Values, Humans, Blood Proteins, Electrophoresis, Disc, Neoplasm Proteins
Abstract

Heterogeneity of proteins of blood serum high-molecular fraction in healthy people, patients with cancer and those with pathologies of nonmalignant nature was studied by the method of disc electrophoresis in 4% polyacrylamide gel. It is established that under conditions of the experiment sharp differences are observed in heterogeneity of studied proteins manifesting in a growth of the discrete electrophoretic bands in disc electrophoregrams of high-molecular fractions of sera from the cancer patients. Disc electrophoregrams of proteins of the studied fractions from the sera of patients with nonmalignant pathologies also differ from those of control groups, though not so sharply as when comparing the preparations obtained from the sera of healthy people and cancer patients. Possible reasons of the observed differences are discussed.

Published
1977

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