title: GGCn polymorphism of eRF3a/GSPT1 gene and breast cancer susceptibility.
abstract: The significance of translation regulatory factors in elevating the risk of cancer has been recently recognized. Eukaryotic release factor 3a (eRF3a) is a translation termination protein that is encoded by G1 to S phase transition 1 gene (GSPT1). The eRF3a/GSPT1 exon 1 contains a trinucleotide GGC repeat coding for a polyglycine expansion in the N-terminal of the protein. In the present study, we determined the allelic length of the GGC(n) repeat in the eRF3a gene in 250 women with breast cancer and 250 age-matched controls. Our results show that the presence of the longer allele, 12-GGC, is correlated with threefold increased risk of breast cancer development. Our findings also suggest that women who are homozygous for 7-GGC allele are possibly at higher risk of developing breast cancer, especially before the age of 50. No significant effect of the allelic length of eRF3a/GSPT1 polymorphism on inheritance or the grade of this disease was observed.
authors.affiliation: Department of Biology, Faculty of Sciences, University of Isfahan, Hezar-Jarib, Isfahan, Iran.
authors.forename: Mahboobe
authors.initials: M
authors.lastname: Miri
authors.forename: Simin
authors.initials: S
authors.lastname: Hemati
authors.forename: Foruzan
authors.initials: F
authors.lastname: Safari
authors.forename: Manoochehr
authors.initials: M
authors.lastname: Tavassoli
mesh_terms: D001943:Breast Neoplasms / Q000235:genetics* / Q000473:pathology; D016022:Case-Control Studies; D005260:Female; D020022:Genetic Predisposition to Disease / Q000235:genetics*; D006801:Humans; D008875:Middle Aged; D060787:Neoplasm Grading; D010454:Peptide Termination Factors / Q000235:genetics*; D020641:Polymorphism, Single Nucleotide / Q000235:genetics*; D020133:Reverse Transcriptase Polymerase Chain Reaction
chemical_list: D010454:Peptide Termination Factors; C087971:peptide-chain-release factor 3
references.citation: Carcinogenesis. 2005 Dec;26(12):2046-9
references.pmid: 15987717
references.citation: Oncogene. 2008 Feb 21;27(9):1297-305
references.pmid: 17700517
references.citation: EMBO J. 1995 Aug 15;14(16):4065-72
references.pmid: 7664746
references.citation: Cytogenet Cell Genet. 1999;86(3-4):250-1
references.pmid: 10575220
references.citation: Nucleic Acids Res. 1988 Feb 11;16(3):1215
references.pmid: 3344216
references.citation: Oncol Rep. 2009 Jun;21(6):1551-8
references.pmid: 19424636
references.citation: Breast J. 2007 Jul-Aug;13(4):383-91
references.pmid: 17593043
references.citation: Cell Motil Cytoskeleton. 2002 Jul;52(3):161-73
references.pmid: 12112144
references.citation: Osteoarthritis Cartilage. 2004 Jul;12(7):525-35
references.pmid: 15219567
references.citation: Cell Motil Cytoskeleton. 1998;39(4):286-302
references.pmid: 9556329
references.citation: Biochemistry (Mosc). 1999 Dec;64(12):1367-72
references.pmid: 10648960
references.citation: Mol Cell Biol. 2005 Jul;25(14):5801-11
references.pmid: 15987998
references.citation: J Biol Chem. 2003 Oct 3;278(40):38699-706
references.pmid: 12865429
references.citation: Cancer Genet Cytogenet. 2009 Dec;195(2):132-42
references.pmid: 19963113
references.citation: Mol Cell Biol. 2007 Aug;27(16):5619-29
references.pmid: 17562865
references.citation: J Biol Chem. 1998 Aug 28;273(35):22254-9
references.pmid: 9712840
references.citation: Breast Cancer Res. 2004;6(6):229-39
references.pmid: 15535852
references.citation: Somat Cell Mol Genet. 1992 Mar;18(2):189-94
references.pmid: 1574740
references.citation: Public Health. 2000 Mar;114(2):143-5
references.pmid: 10800155
references.citation: Environ Mol Mutagen. 1989;13(1):34-43
references.pmid: 2783409