Protein elongation factor EEF1A2 is a putative oncogene in ovarian cancer

10.1038/ng904 ◽  
2002 ◽  
Vol 31 (3) ◽  
pp. 301-305 ◽  
Author(s):  
Nisha Anand ◽  
Sabita Murthy ◽  
Gudrun Amann ◽  
Meredith Wernick ◽  
Lisa A. Porter ◽  
...  
Keyword(s):  
Ovarian Cancer ◽  
Elongation Factor ◽  
Protein Elongation

The possible interaction of CDA14 and protein elongation factor 1α

2008 ◽  
Vol 1784 (2) ◽  
pp. 312-318 ◽  
Author(s):  
Ying-Fang Yang ◽  
Min-Yuan Chou ◽  
Chia-Yu Fan ◽  
Sung-Fang Chen ◽  
Ping-Chiang Lyu ◽  
...  
Keyword(s):  
Elongation Factor ◽  
Elongation Factor 1Α ◽  
Protein Elongation

Expression of protein elongation factor eEF1A2 predicts favorable outcome in breast cancer

2006 ◽  
Vol 102 (1) ◽  
pp. 31-41 ◽  
Author(s):  
Geeta Kulkarni ◽  
Dmitry A. Turbin ◽  
Anahita Amiri ◽  
Sujeeve Jeganathan ◽  
Miguel A. Andrade-Navarro ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Elongation Factor ◽  
Favorable Outcome ◽  
Protein Elongation

scholarly journals Plitidepsin, an inhibitor of the cell elongation factor eEF1a, and molnupiravir an analogue of the ribonucleoside cytidine, two new chemical compounds with intense activity against SARS-CoV-2

2021 ◽  
Author(s):  
Jordi Reina ◽  
Keyword(s):  
Elongation Factor ◽  
Chemical Compounds ◽  
Cellular Protein ◽  
Lethal Mutagenesis ◽  
Good Target ◽  
Therapeutic Possibility ◽  
Intense Activity ◽  
Protein Elongation ◽  
Natural Inhibitors ◽  
Replicative Cycle

The knowledge of the replicative cycle of SARS-CoV-2 and its interactions with cellular proteins has opened a new therapeutic possibility based on blocking those essential for the virus. The cellular protein elongation factor eEF1A could be a good target. Among its natural inhibitors are didemnins and their related chemical compounds such as plitidepsin. In human cell culture, this compound is capable of inhibiting the virus with a potency 27,5 times that of remdesivir. It must be administered intravenously. Of the ribonucleoside analogues, molnupiravir (MK-4483/EIDD-2801) (hydroxy-cytidine) determines a lethal mutagenesis on SARS-CoV-2. In animals, after oral administration, the pulmonary viral load decreases 25,000 times and when administered as prophylaxis, approximately 100,000 times. It prevents the transmission of the virus and eliminates its presence in the oropharynx. Both chemicals have started Phase I / II human clinical trials

The prognostic significance of elongation factor eEF1A2 in ovarian cancer

2008 ◽  
Vol 108 (3) ◽  
pp. 561-568 ◽  
Author(s):  
Dixie E. Pinke ◽  
Steve E. Kalloger ◽  
Tanja Francetic ◽  
David G. Huntsman ◽  
Jonathan M. Lee
Keyword(s):  
Ovarian Cancer ◽  
Prognostic Significance ◽  
Elongation Factor

scholarly journals F-actin sequesters elongation factor 1alpha from interaction with aminoacyl-tRNA in a pH-dependent reaction.

1996 ◽  
Vol 135 (4) ◽  
pp. 953-963 ◽  
Author(s):  
G Liu ◽  
J Tang ◽  
B T Edmonds ◽  
J Murray ◽  
S Levin ◽  
...  
Keyword(s):  
Ph Dependence ◽  
Elongation Factor ◽  
Ph Sensitive ◽  
Actin Binding ◽  
Local Concentration ◽  
Competition Binding ◽  
Translational Apparatus ◽  
Protein Elongation ◽  
Trna Binding

The machinery of eukaryotic protein synthesis is found in association with the actin cytoskeleton. A major component of this translational apparatus, which is involved in the shuttling of aa-tRNA, is the actin-binding protein elongation factor 1alpha (EF-1alpha). To investigate the consequences for translation of the interaction of EF-1alpha with F-actin, we have studied the effect of F-actin on the ability of EF-1alpha to bind to aa-tRNA. We demonstrate that binding of EF-1alpha:GTP to aa-tRNA is not pH sensitive with a constant binding affinity of approximately 0.2 microM over the physiological range of pH. However, the sharp pH dependence of binding of EF-1alpha to F-actin is sufficient to shift the binding of EF-1alpha from F-actin to aa-tRNA as pH increases. The ability of EF-1alpha to bind either F-actin or aa-tRNA in competition binding experiments is also consistent with the observation that EF-1alpha's binding to F-actin and aa-tRNA is mutually exclusive. Two pH-sensitive actin-binding sequences in EF-1alpha are identified and are predicted to overlap with the aa-tRNA-binding sites. Our results suggest that pH-regulated recruitment and release of EF-1alpha from actin filaments in vivo will supply a high local concentration of EF-1alpha to facilitate polypeptide elongation by the F-actin-associated translational apparatus.

scholarly journals Comparative mRNA Expression of eEF1A Isoforms and a PI3K/Akt/mTOR Pathway in a Cellular Model of Parkinson’s Disease

2016 ◽  
Vol 2016 ◽  
pp. 1-11 ◽  
Author(s):  
Kawinthra Khwanraj ◽  
Suriyat Madlah ◽  
Khwanthana Grataitong ◽  
Permphan Dharmasaroja
Keyword(s):  
Parkinson’S Disease ◽  
Parkinson's Disease ◽  
Mrna Level ◽  
Elongation Factor ◽  
Relative Increase ◽  
Mtor Pathway ◽  
Gene Profiling ◽  
Cellular Model ◽  
Protein Elongation

The PI3K/Akt/mTOR pathway is one of dysregulated pathways in Parkinson’s disease (PD). Previous studies in nonneuronal cells showed that Akt regulation can be increased by eukaryotic protein elongation factor 1 alpha 2 (eEF1A2). eEF1A2 is proposed to contribute protection against apoptotic death, likely through activation of the PI3K/Akt pathway. Whether eEF1A2 plays a role in the prevention of cell death in PD has not been investigated. Recently, gene profiling on dopaminergic neurons from postmortem PD patients showed both upregulation and downregulation of some PI3K and mTOR genes. In this paper, the expression of all gene members of the PI3K/Akt/mTOR pathway in relation to those of the eEF1A isoforms in a cellular model of PD was investigated at the mRNA level. The results showed a similar trend of upregulation of genes of the eEF1A isoforms (eEF1A1andeEF1A2) and of the PI3K (classes I–III)/Akt (Akt1,Akt2, andAkt3)/mTOR (mTORC1andmTORC2) pathway in both nondifferentiated and differentiated SH-SY5Y dopaminergic cells treated with 1-methyl-4-phenylpyridinium (MPP+). Upregulation ofeEF1A2,Akt1, andmTORC1was consistent with the relative increase of eEF1A2, Akt, phospho-Akt, and mTORC1 proteins. The possible role of eEF1A isoforms in the regulation of the PI3K/Akt/mTOR pathway in PD is discussed.

scholarly journals Chemical interplay and complementary adaptative strategies toggle bacterial antagonism and co-existence

2021 ◽  
Author(s):  
Carlos Molina-Santiago ◽  
David Vela-Corcía ◽  
Daniel Petras ◽  
Luis Díaz-Martínez ◽  
Alicia Isabel Pérez-Lorente ◽  
...  
Keyword(s):  
Bacterial Communities ◽  
Bacterial Species ◽  
Elongation Factor ◽  
Protein Translation ◽  
Cellular Responses ◽  
Cell Membrane Permeability ◽  
Pseudomonas Chlororaphis ◽  
Bacterial Cells ◽  
Bacterial Antagonism ◽  
Protein Elongation

AbstractBacterial communities are in a continuous adaptive and evolutionary race for survival. A myriad of molecules that kill, defend, or mediate communication between bacterial cells of different lineages shape the final structure of the microbial community. In this work we expand our knowledge on the chemical interplay and specific mutations that modulate the transition from antagonism to co-existence between two plant-beneficial bacteria, Pseudomonas chlororaphis PCL1606 and Bacillus amyloliquefaciens FZB42. We reveal that the bacteriostatic activity of bacillaene produced by Bacillus relies on an interaction with the protein elongation factor FusA and how mutations in this protein lead to tolerance to bacillaene and other protein translation inhibitors. Additionally, we describe how the unspecific tolerance to antimicrobials associated with mutations in the glycerol kinase GlpK is provoked mainly by a decrease of Bacillus cell membrane permeability among other pleiotropic cellular responses. We conclude that nutrient specialization and mutations in basic biological functions are bacterial evolutive and adaptive strategies that lead to the coexistence of two primary competitive bacterial species rather than their mutual eradication.

The Role of Protein Elongation Factor EEF1A2 in Breast Cancer

2004 ◽  
Author(s):  
Jonathan M. Lee
Keyword(s):  
Breast Cancer ◽  
Elongation Factor ◽  
Protein Elongation

The oncogene elongation factor 1 alpha-2 mRNA expression in epithelial ovarian cancer

2005 ◽  
Vol 23 (16_suppl) ◽  
pp. 5034-5034 ◽  
Author(s):  
S. Sharma ◽  
D. Driscoll ◽  
K. Odusni
Keyword(s):  
Ovarian Cancer ◽  
Epithelial Ovarian Cancer ◽  
Mrna Expression ◽  
Elongation Factor ◽  
Elongation Factor 1 Alpha ◽  
Elongation Factor 1
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