| Marked elevation of hypusine formation activity on eukaryotic initiation factor 5A in v-HA-RAS transformed mouse NIH3T3 cells. | |
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MedLine Citation:
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PMID: 9149130 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Hypusine formation on the eukaryotic initiation factor 5A (eIF-5A) precursor is ubiquitously present in eukaryotic cells and archebacteria. In this reaction, deoxyhypusine synthase catalyzes the conversion of one unique lysine residue on eIF-5A to deoxyhypusine using spermidine as the substrate. Hydroxylation of the deoxyhypusine residue completes hypusine formation on eIF-5A. Hypusine formation activity can be measured by an in vitro labeling technique in polyamine-depleted cells. In addition, an in vitro cross-labeling assay can be employed to measure simultaneously the relative deoxyhypusine synthase activity and protein substrate amount. Using these approaches, together with Western blot analysis, we showed that hypusine formation activity is serum-responsive and significantly elevated in Ras oncogene transfected NIH3T3 cells as compared to NIH3T3 cells. The large difference, >30-fold, in hypusine formation activity between these two cells is mainly due to difference in the amount of newly synthesized eIF-5A precursor rather than deoxyhypusine synthase. The deoxyhypusine synthase activity is about three-fold higher in Ras-3T3 cells than in 3T3 cells, and remains constant throughout serum stimulation in both cells. Despite the significant difference in eIF-5A protein amounts, the eIF-5A mRNA levels in 3T3 cells and in Ras-3T3 cells are almost identical. Furthermore, unlike serum-dependent increase in eIF-5A precursor protein, the eIF-5A mRNA in both cells is constitutively expressed after serum stimulation, suggesting that eIF-5A gene is regulated at posttranscriptional/translational level during serum stimulation and cell transformation. |
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Authors:
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Z P Chen; K Y Chen |
Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: Cancer letters Volume: 115 ISSN: 0304-3835 ISO Abbreviation: Cancer Lett. Publication Date: 1997 May |
Date Detail:
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Created Date: 1997-06-04 Completed Date: 1997-06-04 Revised Date: 2009-07-24 |
Medline Journal Info:
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Nlm Unique ID: 7600053 Medline TA: Cancer Lett Country: IRELAND |
Other Details:
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Languages: eng Pagination: 235-41 Citation Subset: IM |
Affiliation:
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Department of Chemistry, Rutgers, The State University of New Jersey, Piscataway 08855-0939, USA. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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3T3 Cells
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drug effects,
metabolism* Animals Cell Transformation, Neoplastic* Eflornithine / pharmacology Gene Expression Lysine / analogs & derivatives*, biosynthesis Mice Oncogene Protein p21(ras) / pharmacology* Oxidoreductases Acting on CH-NH Group Donors / metabolism Peptide Initiation Factors / biosynthesis* RNA-Binding Proteins* Spermidine / metabolism |
| Grant Support | |
ID/Acronym/Agency:
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CA49695/CA/NCI NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Peptide Initiation Factors; 0/RNA-Binding Proteins; 0/eukaryotic translation initiation factor 5A; 124-20-9/Spermidine; 34994-11-1/hypusine; 56-87-1/Lysine; 70052-12-9/Eflornithine; EC 1.5.-/Oxidoreductases Acting on CH-NH Group Donors; EC 1.5.1.-/deoxyhypusine synthase; EC 3.6.5.2/Oncogene Protein p21(ras) |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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