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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Antineoplastic Agents, Phytogenic / pharmacology*
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Base Sequence
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Breast Neoplasms / metabolism*
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Breast Neoplasms / pathology
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Cell Line, Tumor
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DNA Primers
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HSP27 Heat-Shock Proteins
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Heat-Shock Proteins / chemistry
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Heat-Shock Proteins / genetics
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Heat-Shock Proteins / metabolism*
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Humans
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Molecular Chaperones
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Molecular Sequence Data
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Neoplasm Proteins / chemistry
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Neoplasm Proteins / genetics
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Neoplasm Proteins / metabolism*
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Phosphorylation
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Protein Processing, Post-Translational
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Proteome
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Serine / metabolism
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Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
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Vincristine / pharmacology*
Substances
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Antineoplastic Agents, Phytogenic
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DNA Primers
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HSP27 Heat-Shock Proteins
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HSPB1 protein, human
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Heat-Shock Proteins
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Molecular Chaperones
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Neoplasm Proteins
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Proteome
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Serine
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Vincristine