Proteomic analysis of MOLT-4 cells treated by valproic acid
Jazyk angličtina Země Nizozemsko Médium print-electronic
Typ dokumentu srovnávací studie, časopisecké články, práce podpořená grantem
- MeSH
- 2D gelová elektroforéza MeSH
- annexin A5 metabolismus MeSH
- apoptóza účinky léků MeSH
- heterogenní jaderné ribonukleoproteiny metabolismus MeSH
- inhibitory enzymů farmakologie MeSH
- inhibitory histondeacetylas MeSH
- kyselina valproová farmakologie MeSH
- leukemie T-buněčná farmakoterapie metabolismus patologie MeSH
- lidé MeSH
- nádorové proteiny metabolismus MeSH
- proteom analýza MeSH
- průtoková cytometrie MeSH
- signální transdukce MeSH
- spektrometrie hmotnostní - ionizace laserem za účasti matrice MeSH
- viabilita buněk účinky léků MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- srovnávací studie MeSH
- Názvy látek
- annexin A5 MeSH
- heterogenní jaderné ribonukleoproteiny MeSH
- inhibitory enzymů MeSH
- inhibitory histondeacetylas MeSH
- kyselina valproová MeSH
- nádorové proteiny MeSH
- proteom MeSH
The effect of valproic acid (VA) on protein expression in human T-lymphocytic leukemia cells MOLT-4 was studied. VA is an inhibitor of histonedeacetylases and has a potential use as antitumor agent in leukemia treatment. The authors in this work prove that 4 h long incubation with 2 mmol/l VA causes phosphorylation of histone H2A.X and its colocalization with 53BP1 in nuclear foci. Their co-localization is typical for DSB signaling machinery. These foci were detected in cells after 4 h exposure without increase of Annexin V positive apoptotic cells. Slight increase in apoptosis (Annexin V positivity) after 24 h is accompanied by more intensive increase in phosphorylation of H2A.X and also by formation of nuclear foci containing gammaH2A.X and 53BP1. Treatment of cells with 2 mmol/l VA resulted in induction of apoptosis affecting about 30% of cells after incubation for 72 h. The changes in protein expression were examined after cell incubation with 2 mmol/l VA for 4 h. Proteins were separated by two-dimensional electrophoresis and quantified using image evaluation system. Those exhibiting significant VA-induced abundance alterations were identified by mass spectrometry. Changes in expression of 22 proteins were detected, of which 15 proteins were down-regulated. Proteomic analysis resulted in successful identification of three proteins involving alfa-tubulin 3, tubulin-specific chaperone and heterogeneous nuclear ribonucloprotein F. Expression of seven proteins was up-regulated, including heterogeneous nuclear ribonucloprotein A/B. Identified proteins are related to microtubular system and hnRNP family. Suppression of microtubular proteins and changes of balance among hnRNPs can contribute to proliferation arrest and apoptosis induction.
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