Effects of HSP27 Chaperone on THP-1 Tumor Cell Apoptosis

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 specifi c inhibitor (KRIBB3) was evaluated by fluorescent microscopy with FITC-labeled annexin V and prop...

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Bibliographic Details
Published in:Bulletin of experimental biology and medicine 2012-11, Vol.154 (1), p.77-79
Main Authors: Kaigorodova, E. V., Ryazantseva, N. V., Novitskii, V. V., Maroshkina, A. N., Belkina, M. V.
Format: Article
Language:English
Subjects:
Adolescent
Adult
Anisoles - pharmacology
Annexin A5 - metabolism
Apoptosis
Apoptosis - physiology
Apoptosis Regulatory Proteins
Biomedical and Life Sciences
Biomedicine
Cell Biology
Cell Line, Tumor
Female
Heat shock proteins
HSP27 Heat-Shock Proteins - antagonists & inhibitors
HSP27 Heat-Shock Proteins - metabolism
Humans
Internal Medicine
Isoxazoles - pharmacology
Laboratory Medicine
Leukemia - pathology
Leukocytes, Mononuclear
Male
Middle Aged
Molecular Chaperones - metabolism
Monocyte-Macrophage Precursor Cells - pathology
Oncology
Pathology
Proteins
Proto-Oncogene Proteins c-bcl-2 - metabolism
Tumors
Young Adult
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Summary: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 specifi c 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.
ISSN:0007-4888
1573-8221
DOI:10.1007/s10517-012-1879-1