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XXII. BIOCHEMICKÝ ZJAZD - Jesseniova lekárska fakulta

XXII. BIOCHEMICKÝ ZJAZD - Jesseniova lekárska fakulta

XXII. BIOCHEMICKÝ ZJAZD - Jesseniova lekárska fakulta

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Posters<br />

68.<br />

STUDY OF THE EffECT OF HISTONE DEACETYLASE INHIBITOR ON THE<br />

SENSITIVITY OF LEUKAEMIC CELLS TO THE CYTOSTATICS<br />

Andrea Štefániková 1 , Jozef Hatok 1 , Jana Jurečeková 1 , Ivana Plameňová 2 ,<br />

Dušan Dobrota 1 and Peter Račay 1<br />

1<br />

Department of Medical Biochemistry, 2 Clinic of Haematology and Transfusiology,<br />

JLF UK Martin<br />

One of the possibilities how to overcome a chemoresistance of tumor cells is a combination<br />

of classic cytostatics with substances possessing a potential to block proliferation<br />

or induce apoptosis of these cells. Histone deacetylases are a group of enzymes that<br />

catalyze removing acetic acid residue from histones. This epigenetic process leads to<br />

condensation of chromatin and suppresion of transcription. The influence of histone<br />

deacetylases inhibitors is intensively studied nowadays, especially because of their connection<br />

with antiproliferative and antineoplastic effect. There has long been known an<br />

inhibitor of histone deacetylases class I - sodium butyrate. It is a short chain fatty acid<br />

that has effects at the molecular, cellular, and tissue level. By performing of in vitro MTT<br />

test, we have revealed polyresistance of leukaemic blasts isolated from blood of AML<br />

patient to almost all cytostatics tested. Addition of sodium butyrate in concentration of<br />

2mM led to significantly increased chemosensitivity of blasts. In search for molecular<br />

mechanism of butyrate action we have performed analysis of leukaemic cell line HL60<br />

treated with sodium butyrate. Our results open possibility that addition of butyrate<br />

increases chemosensitivity of blasts by alteration of expression of proteins involved in<br />

apoptosis initiation.<br />

Acknowledgement: This work was supported by grant UK/223/2010 to Andrea Štefaniková.<br />

190 <strong>XXII</strong>. Biochemistry Congress, Martin

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