Characterization of proteins associated with heat shock protein hsp27 in the squamous cell carcinoma cell line A431. |
| |
Authors: | Ingela Kindas‐Mügge Constanze Riedler Ilse Frhlich Michael Micksche Franz Trautinger |
| |
Institution: | Department of Applied and Experimental Oncology, Institute of Tumorbiology/Cancer Research, Vienna, Austria. margaret.kindas-muegge@univie.ac.at |
| |
Abstract: | Heat shock protein hsp27 is a molecular chaperone and identification of hsp27-binding proteins might help to elucidate its functional role in keratinocyte biology. In the present investigation we used a human epidermal cell carcinoma cell line (A431) transfected with hsp27 (A431/16) to study interference between hsp27 protein and other proteins. Immunoprecipitation experiments with anti-hsp27 antibody revealed a multicomponent complex when analysed by silver staining. By immunoblotting analysis we could demonstrate that hsp27 associates with actin, the mutant form of p53, hsp70 and hsp90. Immunofluorescence analysis showed a co-localization between hsp27 and p53, hsp70 and hsp90. To control for the specificity of the observed interactions, immuno-precipitations with antibodies to actin, p53, hsp70 and hsp90 respectively, were performed. All of the tested proteins demonstrated a coimmunoprecipitation with hsp27. We conclude that hsp27, like the other heat shock proteins, is part of a complex system of molecular chaperones in epidermal keratinocytes. |
| |
Keywords: | heat shock protein hsp27 associated proteins epidermal cell carcinoma cell line |
本文献已被 ScienceDirect 等数据库收录! |
|