Proteins implicated in the increase of adhesivity induced by suberoylanilide hydroxamic acid in leukemic cells
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F12%3A10130575" target="_blank" >RIV/00216208:11310/12:10130575 - isvavai.cz</a>
Nalezeny alternativní kódy
RIV/61388971:_____/12:00390148 RIV/00023736:_____/12:00010315
Výsledek na webu
<a href="http://dx.doi.org/10.1016/j.jprot.2012.09.014" target="_blank" >http://dx.doi.org/10.1016/j.jprot.2012.09.014</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.jprot.2012.09.014" target="_blank" >10.1016/j.jprot.2012.09.014</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Proteins implicated in the increase of adhesivity induced by suberoylanilide hydroxamic acid in leukemic cells
Popis výsledku v původním jazyce
We have previously shown that suberoylanilide hydroxamic acid (SAHA) treatment increases the adhesivity of leukemic cells to fibronectin at clinically relevant concentrations. Now, we present the results of the proteomic analysis of SAHA effects on leukemic cell lines using 2-DE and ProteomLab PF2D system. Histone acetylation at all studied acetylation sites reached the maximal level after 5 to 10 h of SAHA treatment No difference in histone acetylation between subtoxic and toxic SAHA doses was observed. SAHA treatment induced cofilin phosphorylation at Ser3, an increase in vimentin and paxillin expression and a decrease in stathmin expression as confirmed by western-blotting and immunofluorescence microscopy. The interaction of cofilin with 14-3-3 epsilon was documented using both Duolink system and coimmunoprecipitation. However, this interaction was independent of cofilin Ser3 phosphorylation and the amount of 14-3-3-epsilon-bound cofilin did not rise following SAHA treatment SARA-i
Název v anglickém jazyce
Proteins implicated in the increase of adhesivity induced by suberoylanilide hydroxamic acid in leukemic cells
Popis výsledku anglicky
We have previously shown that suberoylanilide hydroxamic acid (SAHA) treatment increases the adhesivity of leukemic cells to fibronectin at clinically relevant concentrations. Now, we present the results of the proteomic analysis of SAHA effects on leukemic cell lines using 2-DE and ProteomLab PF2D system. Histone acetylation at all studied acetylation sites reached the maximal level after 5 to 10 h of SAHA treatment No difference in histone acetylation between subtoxic and toxic SAHA doses was observed. SAHA treatment induced cofilin phosphorylation at Ser3, an increase in vimentin and paxillin expression and a decrease in stathmin expression as confirmed by western-blotting and immunofluorescence microscopy. The interaction of cofilin with 14-3-3 epsilon was documented using both Duolink system and coimmunoprecipitation. However, this interaction was independent of cofilin Ser3 phosphorylation and the amount of 14-3-3-epsilon-bound cofilin did not rise following SAHA treatment SARA-i
Klasifikace
Druh
J<sub>x</sub> - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)
CEP obor
EA - Morfologické obory a cytologie
OECD FORD obor
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Návaznosti výsledku
Projekt
<a href="/cs/project/GA301%2F09%2F1026" target="_blank" >GA301/09/1026: Proteomová analýza účinků suberoylanilidu hydroxamové kyseliny (SAHA) na lidské leukemické buňky</a><br>
Návaznosti
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Ostatní
Rok uplatnění
2012
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Journal of Proteomics
ISSN
1874-3919
e-ISSN
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Svazek periodika
77
Číslo periodika v rámci svazku
25. září
Stát vydavatele periodika
NL - Nizozemsko
Počet stran výsledku
17
Strana od-do
406-422
Kód UT WoS článku
000313535900032
EID výsledku v databázi Scopus
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