Abstract
The role of Hsp27 (heat shock protein 27) chaperone in regulation of THP-1 tumor cell apoptosis was studied. Realization of tumor cell apoptosis under conditions of in vitro culturing with Hsp27 specific inhibitor (KRIBB3) was evaluated by fluorescent microscopy with FITC-labeled annexin V and propidium iodide. Measurements of Bcl-2 family proteins (Bcl-2, Bax, Bad) in tumor cells incubated with Hsp27 inhibitor were carried out by Western blotting. Chaperone Hsp27 acted as apoptosis inhibitor in THP-1 tumor cells modulating the proportion of antiapoptotic (Bcl-2) and proapoptotic (Bax and Bad) proteins.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adolescent
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Adult
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Anisoles / pharmacology*
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Annexin A5 / metabolism
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Apoptosis / physiology*
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Apoptosis Regulatory Proteins
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Cell Line, Tumor
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Female
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HSP27 Heat-Shock Proteins / antagonists & inhibitors
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HSP27 Heat-Shock Proteins / metabolism*
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Humans
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Isoxazoles / pharmacology*
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Leukemia / pathology*
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Leukocytes, Mononuclear
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Male
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Middle Aged
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Molecular Chaperones / metabolism
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Monocyte-Macrophage Precursor Cells / pathology
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Proto-Oncogene Proteins c-bcl-2 / metabolism*
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Young Adult
Substances
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5-(5-ethyl-2-hydroxy-4-methoxyphenyl)-4-(4-methoxyphenyl)isoxazole
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Anisoles
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Annexin A5
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Apoptosis Regulatory Proteins
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HSP27 Heat-Shock Proteins
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Isoxazoles
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Molecular Chaperones
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Proto-Oncogene Proteins c-bcl-2