Proteomic analysis of MCF-7 cell lines expressing the zinc-finger or the proline-rich domain of retinoblastoma-interacting-zinc-finger protein

J Proteome Res. 2006 May;5(5):1176-85. doi: 10.1021/pr0504743.

Abstract

To identify a growth-promoting activity related to retinoblastoma-interacting-zinc-finger (RIZ) protein, differential protein expression of MCF-7 cell lines expressing the zinc-finger or the proline-rich domain of RIZ protein was analyzed by a robust bottom-up mass-spectrometry proteomic approach. Spots corresponding to qualitative and quantitative differences in protein expression have been selected and identified. Some of these proteins have been previously reported as being associated with different types of carcinomas or involved in cell proliferation and differentiation. Knowledge of specific differentially expressed proteins by MCF-7-derived cell lines expressing RIZ different domains will provide the basis for identifying a growth-promoting activity related to RIZ gene products.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biomarkers, Tumor / metabolism
  • Breast Neoplasms / metabolism*
  • Breast Neoplasms / pathology
  • Cathepsin D / metabolism
  • Cell Line, Tumor
  • Cytoskeleton / metabolism
  • DNA-Binding Proteins / analysis*
  • DNA-Binding Proteins / genetics
  • DNA-Binding Proteins / metabolism
  • Electrophoresis, Gel, Two-Dimensional
  • Energy Metabolism
  • Female
  • Histone-Lysine N-Methyltransferase
  • Humans
  • Nuclear Proteins / analysis*
  • Nuclear Proteins / genetics
  • Nuclear Proteins / metabolism
  • Phosphopyruvate Hydratase / metabolism
  • Protein Isoforms
  • Protein Structure, Tertiary
  • Proteomics / methods*
  • RNA / metabolism
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / methods
  • Transcription Factors / analysis*
  • Transcription Factors / genetics
  • Transcription Factors / metabolism
  • Tumor Suppressor Proteins / metabolism

Substances

  • Biomarkers, Tumor
  • DNA-Binding Proteins
  • Nuclear Proteins
  • Protein Isoforms
  • Transcription Factors
  • Tumor Suppressor Proteins
  • RNA
  • Histone-Lysine N-Methyltransferase
  • PRDM2 protein, human
  • Cathepsin D
  • ENO1 protein, human
  • Phosphopyruvate Hydratase