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Up-regulation of PDCD4 in senescent human diploid fibroblasts.

Programmed cell death 4 (PDCD4) has a common MI domain sharing with death associated protein 5 (DAP5) and a component of eukaryotic translation initiation factor (eIF4G) complex and it might also work as a tumor suppressor. We could find that the message and product of Pdcd4 gene were up-regulated in senescent human diploid fibroblasts. In yeast two hybrid analysis, the C-terminal region of PDCD4 interacted with ribosomal protein S13 (RPS13), ribosomal protein L5 (RPL5), and TI-227H. In in vitro binding assay, RPS13, a component of 40S ribosome was stably bound to PDCD4. We also found that PDCD4 was localized to polysome fractions. We could pull out eIF4G with GST-PDCD4, but eIF4E did not interact with PDCD4. From these results, we could assume that PDCD4 might regulate the eIF4G-dependent translation through direct interactions with eIF4G and RPS13 in senescent fibroblasts.

Pubmed ID: 12054647

Authors

  • Kang MJ
  • Ahn HS
  • Lee JY
  • Matsuhashi S
  • Park WY

Journal

Biochemical and biophysical research communications

Publication Data

April 26, 2002

Associated Grants

None

Mesh Terms

  • Animals
  • Apoptosis
  • Apoptosis Regulatory Proteins
  • Cell Aging
  • Cells, Cultured
  • Cycloheximide
  • Eukaryotic Initiation Factor-4G
  • Fibroblasts
  • Gene Expression Regulation
  • HeLa Cells
  • Humans
  • Infant, Newborn
  • Male
  • Peptide Initiation Factors
  • Polyribosomes
  • Proteins
  • RNA-Binding Proteins
  • Rabbits
  • Recombinant Proteins
  • Ribosomal Proteins
  • Skin Physiological Phenomena