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.
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
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
Biochem. Biophys. Res. Commun.
Date: Apr. 26, 2002
PubMed ID: 12054647
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