Vincristine regulates the phosphorylation of the antiapoptotic protein HSP27 in breast cancer cells |
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Authors: | Casado Pedro Zuazua-Villar Pedro del Valle Eva Martínez-Campa Carlos Lazo Pedro S Ramos Sofía |
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Affiliation: | Departamento de Bioquimica y Biología Molecular, Instituto Universitario de Oncología del Principado de Asturias (I.U.O.P.A), Universidad de Oviedo, 33071 Oviedo, Spain. |
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Abstract: | Vincristine is an antitumor drug that inhibits microtubule polymerization, causes G2/M arrest and induces apoptosis. 2D-PAGE and MALDI-TOF-MS analysis of vincristine effects on MCF7 cells, revealed a vincristine upregulated form and a vincristine downregulated form of the antiapoptotic protein HSP27. These findings linked to the lack of vincristine effect over HSP27 mRNA, suggest a protein post-translational modification. Further assays indicated the presence of a phosphorylated peptide, containing serine 82, only in the vincristine upregulated form. Serine 82 phosphorylation was confirmed using specific antibodies. Thus, phosphorylation of HSP27 may play a role in the cellular response to vincristine. |
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