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18 results on '"Fedorova, Tatiana V."'

2. Comparative analysis of the white rot fungus Trametes hirsuta 072 laccases ability to modify 17β-oestradiol in the aqueous medium.

Author

Savinova, Olga S., Solyev, Pavel N., Fedorova, Tatiana V., Kochetkov, Sergey N., and Savinova, Tatiana S.

Subjects
LACCASE, OXIDATIVE coupling, ISOENZYMES, COMPARATIVE studies, LIQUID chromatography, CATALYTIC activity
Abstract

A comparative study of the ability of Trametes hirsuta laccase isoenzymes to biotransform 17β-oestradiol (3,17β-dihydroxyestra-1,3,5(10)-triene, E2) was carried out. Native major LacA and recombinant minor isoenzymes (rLacC, rLacD, and rLacF) obtained in Penicillium canescens were used. It was found that all the studied isozymes are capable of catalysing the oxidative coupling of E2 in an aqueous medium (22 ± 2 °C, pH 4.5) with the formation of predominantly dimers and trimers. Other concurrently formed products were detected by high-pressure liquid chromatography – high-resolution mass spectrometry (HPLC–HRMS) and characterized, summarizing the overall condensation pathway of E2 in laccases. The highest catalytic activity was observed for major LacA. For other laccases, the activity decreased in the following sequence rLacF > rLacD > rLacC. Utilization of T. hirsuta enzymatic variety of laccases can be of benefit for detoxification of phenol-like steroid compounds in the environment. [ABSTRACT FROM AUTHOR]

Published
2023
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13. Draft Genome Sequence of the Fungus Trametes hirsuta 072

Author

Pavlov, Andrey R., primary, Tyazhelova, Tatiana V., additional, Moiseenko, Konstantin V., additional, Vasina, Daria V., additional, Mosunova, Olga V., additional, Fedorova, Tatiana V., additional, Maloshenok, Lilya G., additional, Landesman, Elena O., additional, Bruskin, Sergei A., additional, Psurtseva, Nadezhda V., additional, Slesarev, Alexei I., additional, Kozyavkin, Sergei A., additional, and Koroleva, Olga V., additional

Published
2015
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14. The Trametes hirsuta 072 laccase multigene family: Genes identification and transcriptional analysis under copper ions induction

Author

Vasina, Daria V., primary, Mustafaev, Orkhan N., additional, Moiseenko, Konstantin V., additional, Sadovskaya, Natalia S., additional, Glazunova, Olga A., additional, Tyurin, Аlexander А., additional, Fedorova, Tatiana V., additional, Pavlov, Andrey R., additional, Tyazhelova, Tatiana V., additional, Goldenkova-Pavlova, Irina V., additional, and Koroleva, Olga V., additional

Published
2015
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17. Sensitivity of acute myeloid leukemia Kasumi-1 cells to binase toxic action depends on the expression of KITand АML1-ETOoncogenes

Author

Mitkevich, Vladimir A., Petrushanko, Irina Y., Spirin, Pavel V., Fedorova, Tatiana V., Kretova, Olga V., Tchurikov, Nickolai A., Prassolov, Vladimir S., Ilinskaya, Olga N., and Makarov, Alexander A.

Abstract

Some RNases selectively attack malignant cells, triggering an apoptotic response, and therefore are considered as alternative chemotherapeutic drugs. Here we studied the effects of Bacillus intermedius RNase (binase) on murine myeloid progenitor cells FDC-P1; transduced FDC-P1 cells ectopically expressing mutated human KIT N822K oncogene and/or human AML1-ETO oncogene; and human leukemia Kasumi-1 cells expressing both of these oncogenes. Expression of both KIT and AML1-ETO oncogenes makes FDC-P1 cells sensitive to the toxic effects of binase. Kasumi-1 cells were the most responsive to the toxic actions of binase among the cell lines used in this work with an IC50 value of 0.56 µM. Either blocking the functional activity of the KIT protein with imatinib or knocking-down oncogene expression using lentiviral vectors producing shRNA against AML1-ETO or KIT eliminated the sensitivity of Kasumi-1 cells to binase toxic action and promoted their survival, even in the absence of KIT-dependent proliferation and antiapoptotic pathways. Here we provide evidence that the cooperative effect of the expression of mutated KIT and AML1-ETO oncogenes is crucial for selective toxic action of binase on malignant cells. These findings can facilitate clinical applications of binase providing a useful screen based on the presence of the corresponding target oncogenes in malignant cells.

Published
2011
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18. Sensitivity of acute myeloid leukemia Kasumi-1 cells to binase toxic action depends on the expression of KIT and АML1-ETO oncogenes.

Author

Mitkevich VA, Petrushanko IY, Spirin PV, Fedorova TV, Kretova OV, Tchurikov NA, Prassolov VS, Ilinskaya ON, and Makarov AA

Subjects
Animals, Apoptosis, Bacillus enzymology, Benzamides, Cell Line, Tumor, Cell Proliferation, Cell Survival, Core Binding Factor Alpha 2 Subunit genetics, Drug Screening Assays, Antitumor, Gene Knockdown Techniques, Humans, Imatinib Mesylate, Inhibitory Concentration 50, Lentivirus genetics, Lentivirus metabolism, Leukemia, Myeloid, Acute drug therapy, Leukemia, Myeloid, Acute genetics, Leukemia, Myeloid, Acute metabolism, Mice, Oncogene Proteins, Fusion genetics, Piperazines pharmacology, Proto-Oncogene Proteins c-kit antagonists & inhibitors, Proto-Oncogene Proteins c-kit genetics, Pyrimidines pharmacology, RNA, Small Interfering genetics, RNA, Small Interfering metabolism, RUNX1 Translocation Partner 1 Protein, Time Factors, Core Binding Factor Alpha 2 Subunit metabolism, Endoribonucleases toxicity, Gene Expression Regulation, Leukemic, Leukemia, Myeloid, Acute pathology, Oncogene Proteins, Fusion metabolism, Proto-Oncogene Proteins c-kit metabolism
Abstract

Some RNases selectively attack malignant cells, triggering an apoptotic response, and therefore are considered as alternative chemotherapeutic drugs. Here we studied the effects of Bacillus intermedius RNase (binase) on murine myeloid progenitor cells FDC-P1; transduced FDC-P1 cells ectopically expressing mutated human KIT N822K oncogene and/or human AML1-ETO oncogene; and human leukemia Kasumi-1 cells expressing both of these oncogenes. Expression of both KIT and AML1-ETO oncogenes makes FDC-P1 cells sensitive to the toxic effects of binase. Kasumi-1 cells were the most responsive to the toxic actions of binase among the cell lines used in this work with an IC50 value of 0.56 µM. Either blocking the functional activity of the KIT protein with imatinib or knocking-down oncogene expression using lentiviral vectors producing shRNA against AML1-ETO or KIT eliminated the sensitivity of Kasumi-1 cells to binase toxic action and promoted their survival, even in the absence of KIT-dependent proliferation and antiapoptotic pathways. Here we provide evidence that the cooperative effect of the expression of mutated KIT and AML1-ETO oncogenes is crucial for selective toxic action of binase on malignant cells. These findings can facilitate clinical applications of binase providing a useful screen based on the presence of the corresponding target oncogenes in malignant cells.

Published
2011
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