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157 results on '"Fabczak, Hanna"'

9. Systematic Studies on Anti-Cancer Evaluation of Stilbene and Dibenzo[ b,f ]oxepine Derivatives.

Author

Borys, Filip, Tobiasz, Piotr, Poterała, Marcin, Fabczak, Hanna, Krawczyk, Hanna, and Joachimiak, Ewa

Subjects
STILBENE derivatives, STILBENE, SPINDLE apparatus, TUBULINS, HETERODIMERS, MULTIDRUG resistance, CYTOSKELETON
Abstract

Cancer is one of the most common causes of human death worldwide; thus, numerous therapies, including chemotherapy, have been and are being continuously developed. In cancer cells, an aberrant mitotic spindle—a microtubule-based structure necessary for the equal splitting of genetic material between daughter cells—leads to genetic instability, one of the hallmarks of cancer. Thus, the building block of microtubules, tubulin, which is a heterodimer formed from α- and β-tubulin proteins, is a useful target in anti-cancer research. The surface of tubulin forms several pockets, i.e., sites that can bind factors that affect microtubules' stability. Colchicine pockets accommodate agents that induce microtubule depolymerization and, in contrast to factors that bind to other tubulin pockets, overcome multi-drug resistance. Therefore, colchicine-pocket-binding agents are of interest as anti-cancer drugs. Among the various colchicine-site-binding compounds, stilbenoids and their derivatives have been extensively studied. Herein, we report systematic studies on the antiproliferative activity of selected stilbenes and oxepine derivatives against two cancer cell lines—HCT116 and MCF-7—and two normal cell lines—HEK293 and HDF-A. The results of molecular modeling, antiproliferative activity, and immunofluorescence analyses revealed that compounds 1a, 1c, 1d, 1i, 2i, 2j, and 3h were the most cytotoxic and acted by interacting with tubulin heterodimers, leading to the disruption of the microtubular cytoskeleton. [ABSTRACT FROM AUTHOR]

Published
2023
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10. PCD Genes—From Patients to Model Organisms and Back to Humans

Author

Niziolek, Michal, primary, Bicka, Marta, additional, Osinka, Anna, additional, Samsel, Zuzanna, additional, Sekretarska, Justyna, additional, Poprzeczko, Martyna, additional, Bazan, Rafal, additional, Fabczak, Hanna, additional, Joachimiak, Ewa, additional, and Wloga, Dorota, additional

Published
2022
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32. Multiple phosphorylation sites on γ‐tubulin are essential and contribute to the biogenesis of basal bodies in Tetrahymena

Author

Joachimiak, Ewa, primary, Jerka‐Dziadosz, Maria, additional, Krzemień‐Ojak, Łucja, additional, Wacławek, Ewa, additional, Jedynak, Katarzyna, additional, Urbanska, Paulina, additional, Brutkowski, Wojciech, additional, Sas‐Nowosielska, Hanna, additional, Fabczak, Hanna, additional, Gaertig, Jacek, additional, and Wloga, Dorota, additional

Published
2018
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37. Ciliopatie - choroby spowodowane nieprawidłowym funkcjonowaniem rzęsek.

Author

Joachimiak, Ewa, Włoga, Dorota, Filipek, Anna, and Fabczak, Hanna

Abstract

Copyright of Advances in Biochemistry / Postepy Biochemii is the property of Polish Biochemical Society / Acta Biochimica Polonica and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Published
2018

41. Regulation of katanin activity in the ciliate Tetrahymena thermophila.

Author

Waclawek, Ewa, Joachimiak, Ewa, Hall, Malgorzata Hanna, Fabczak, Hanna, and Wloga, Dorota

Subjects
TETRAHYMENA thermophila, MICROTUBULES, CELL division, CELL migration, CAENORHABDITIS elegans, XENOPUS
Abstract

Katanin is a microtubule severing protein that functions as a heterodimer composed of an AAA domain catalytic subunit, p60, and a regulatory subunit, a WD40 repeat protein, p80. Katanin-dependent severing of microtubules is important for proper execution of key cellular activities including cell division, migration, and differentiation. Published data obtained in Caenorhabditis elegans, Xenopus and mammals indicate that katanin is regulated at multiple levels including transcription, posttranslational modifications (of both katanin and microtubules) and degradation. Little is known about how katanin is regulated in unicellular organisms. Here we show that in the ciliated protist Tetrahymena thermophila, as in Metazoa, the localization and activity of katanin requires specific domains of both p60 and p80, and that the localization of p60, but not p80, is sensitive to the levels of microtubule glutamylation. A prolonged overexpression of either a full length, or a fragment of p80 containing WD40 repeats, partly phenocopies a knockout of p60, indicating that in addition to its activating role, p80 could also contribute to the inhibition of p60. We also show that the level of p80 depends on the 26S proteasome activity. [ABSTRACT FROM AUTHOR]

Published
2017
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