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Up-regulation of PDCD4 in senescent human diploid fibroblasts.

http://www.ncbi.nlm.nih.gov/pubmed/12054647

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 RIS Download

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

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