Biopolym. Cell. 2008; 24(4):310-317.
Molecular Biomedicine
Investigation of expression of different subunits of eukaryotic translation elongation factor eEF1 in human glial brain tumors
- Institute of Molecular Biology and Genetics, NAS of Ukraine
150, Akademika Zabolotnoho Str., Kyiv, Ukraine, 03680 - Institute of Neurosurgery named after A. P. Romodanov, NAMS of Ukraine
32, Manuilskogo Str., Kyiv, Ukraine, 04050
Abstract
Eukaryotic elongation factor 1 (eEF1) mediates the binding of aminoacyl-tRNA to the ribosome in GTP-dependent manner. eEF1 consists of four subunits: eEF1A, eEF1Bα, eEF1Bβ and eEF1Bγ. eEF1A has two different isoforms: eEF1A1 is present throughout development and is ubiquitously expressed with the exception of adult muscle, while eEF1A2 is developmentally regulated and expressed only in muscle cells and neurons. Expression of eEF1A1, eEF1A2, eEF1Bα, eEF1Bβ and eEF1Bγ genes was analyzed by Northern blot hybridization of a panel of brain tumor and normal brain tissue RNAs. Totally 23 glioblastoma and 10 normal brain samples were investigated. In gliomas, no meaningful difference in the mRNA content for the eEF1A1, eEF1Bα and eEF1Bγ subunits as compared to normal brain tissues was found. However, we have observed approximately 2-fold decrease in the eEF1Bβ mRNA expression in human gliomas as compared to normal human brain by Northern blot analysis. Besides, we have shown reduced level of the eEF1A2 mRNA expression in glioblastoma as compared to normal human glia.
Keywords: eEF1, eukaryotic translation elongation factor 1, overexpression of genes, human glial brain tumors
Full text: (PDF, in English) (PDF, in Ukrainian)
References
[1]
Negrutskii BS, El'skaya AV. Eukaryotic translation elongation factor 1 alpha: structure, expression, functions, and possible role in aminoacyl-tRNA channeling. Prog Nucleic Acid Res Mol Biol. 1998;60:47-78.
[2]
Amons R, Guerrucci MA, Karssies RH, Morales J, Cormier P, M?ller W, Belle R. The leucine-zipper in elongation factor EF-1 delta, a guanine-nucleotide exchange protein, is conserved in Artemia and Xenopus. Biochim Biophys Acta. 1994;1218(3):346-50.
[3]
Janssen GM, Moller W. Kinetic studies on the role of elongation factors 1 beta and 1 gamma in protein synthesis. J Biol Chem. 1988;263(4):1773-8.
[4]
Janssen GM, van Damme HT, Kriek J, Amons R, M?ller W. The subunit structure of elongation factor 1 from Artemia. Why two alpha-chains in this complex? J Biol Chem. 1994;269(50):31410-7.
[5]
Tatsuka M, Mitsui H, Wada M, Nagata A, Nojima H, Okayama H. Elongation factor-1 alpha gene determines susceptibility to transformation. Nature. 1992;359(6393):333-6.
[6]
Anand N, Murthy S, Amann G, Wernick M, Porter LA, Cukier IH, Collins C, Gray JW, Diebold J, Demetrick DJ, Lee JM. Protein elongation factor EEF1A2 is a putative oncogene in ovarian cancer. Nat Genet. 2002;31(3):301-5.
[7]
Tomlinson VA, Newbery HJ, Wray NR, Jackson J, Larionov A, Miller WR, Dixon JM, Abbott CM. Translation elongation factor eEF1A2 is a potential oncoprotein that is overexpressed in two-thirds of breast tumours. BMC Cancer. 2005;5:113.
[8]
Chi K, Jones DV, Frazier ML. Expression of an elongation factor 1 gamma-related sequence in adenocarcinomas of the colon. Gastroenterology. 1992;103(1):98-102.
[9]
Lew Y, Jones DV, Mars WM, Evans D, Byrd D, Frazier ML. Expression of elongation factor-1 gamma-related sequence in human pancreatic cancer. Pancreas. 1992;7(2):144-52.
[10]
Ender B, Lynch P, Kim YH, Inamdar NV, Cleary KR, Frazier ML. Overexpression of an elongation factor-1 gamma-hybridizing RNA in colorectal adenomas. Mol Carcinog. 1993;7(1):18-20.
[11]
Ogawa K, Utsunomiya T, Mimori K, Tanaka Y, Tanaka F, Inoue H, Murayama S, Mori M. Clinical significance of elongation factor-1 delta mRNA expression in oesophageal carcinoma. Br J Cancer. 2004;91(2):282-6.
[12]
De Bortoli M, Castellino RC, Lu XY, Deyo J, Sturla LM, Adesina AM, Perlaky L, Pomeroy SL, Lau CC, Man TK, Rao PH, Kim JY. Medulloblastoma outcome is adversely associated with overexpression of EEF1D, RPL30, and RPS20 on the long arm of chromosome 8. BMC Cancer. 2006;6:223.
[13]
Chomczynski P, Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal Biochem. 1987;162(1):156-9.
[14]
Sambrook J., Fritsch E. F., Maniatis T. Molecular cloning: A laboratory manual New York: Cold Spring Harbor Lab. press, 1989 424 p.
[15]
Joseph P, O'Kernick CM, Othumpangat S, Lei YX, Yuan BZ, Ong TM. Expression profile of eukaryotic translation factors in human cancer tissues and cell lines. Mol Carcinog. 2004;40(3):171-9.
[16]
McClatchy DB, Knudsen CR, Clark BF, Kahn RA, Hall RA, Levey AI. Novel interaction between the M4 muscarinic acetylcholine receptor and elongation factor 1A2. J Biol Chem. 2002;277(32):29268-74.