Dissecting the expression of EEF1A1/2 genes in human prostate cancer cells: the potential of EEF1A2 as a hallmark for prostate transformation and progression

Abstract

Background:In prostate adenocarcinoma, the dissection of the expression behaviour of the eukaryotic elongation factors (eEF1A1/2) has not yet fully elucidated.Methods:The EEF1A1/A2 expressions were investigated by real-time PCR, western blotting (cytoplasmic and cytoskeletal/nuclear-enriched fractions) and immunofluorescence in the androgen-responsive LNCaP and the non-responsive DU-145 and PC-3 cells, displaying a low, moderate and high aggressive phenotype, respectively. Targeted experiments were also conducted in the androgen-responsive 22Rv1, a cell line marking the progression towards androgen-refractory tumour. The non-tumourigenic prostate PZHPV-7 cell line was the control.Results:Compared with PZHPV-7, cancer cells showed no major variations in EEF1A1 mRNA; eEF1A1 protein increased only in cytoskeletal/nuclear fraction. On the contrary, a significant rise of EEF1A2 mRNA and protein were found, with the highest levels detected in LNCaP. Eukaryotic elongation factor 1A2 immunostaining confirmed the western blotting results. Pilot evaluation in archive prostate tissues showed the presence of EEF1A2 mRNA in near all neoplastic and perineoplastic but not in normal samples or in benign adenoma; in contrast, EEF1A1 mRNA was everywhere detectable.Conclusion:Eukaryotic elongation factor 1A2 switch-on, observed in cultured tumour prostate cells and in human prostate tumour samples, may represent a feature of prostate cancer; in contrast, a minor involvement is assigned to EEF1A1. These observations suggest to consider EEF1A2 as a marker for prostate cell transformation and/or possibly as a hallmark of cancer progression.

The Ubiquitin-like Protein FAT10 Stabilizes eEF1A1 Expression to Promote Tumor Proliferation in a Complex Manner

“…eEF1A1 is a protein that triggers the initiation of protein translation elongation, and involved in the control of various cellular processes (16,18). Studies have shown that eEF1A1 is high expression in many tumors, and overexpression of eEF1A1 promotes cancer cell proliferation and cancer development (16,18). In this study, our data also found that eEF1A1 is upregulated in a variety of cancer cells, including HCC, breast cancer, colorectal cancer, pancreatic cancer, and cervical cancer.…”

“…To understand the molecular mechanism of tumor proliferation will contribute to the prevention and treatment of tumor (36,37). eEF1A1 is a protein that triggers the initiation of protein translation elongation, and involved in the control of various cellular processes (16,18). Studies have shown that eEF1A1 is high expression in many tumors, and overexpression of eEF1A1 promotes cancer cell proliferation and cancer development (16,18).…”

“…eEF1A1 is a highly conserved GTP-binding protein in eukaryotic cells that plays a significant role in peptide chain extension during protein synthesis (14). Research indicates that eEF1A1 plays an important role in the regulation of various biological characteristics of cells, such as the cell cycle, cell growth, and cell death (16,17). Studies have shown that eEF1A1 is aberrantly upregulated in many tumor tissues (18,19).…”

Novel hepatocellular carcinoma molecules with prognostic and therapeutic potentials

“…Whereas the molecular mechanisms contributing to carcinogenesis and progression of HCC still need to be fully clarified, many biological molecules have been proposed as relevant players. Some of them are mutually exclusive of neoplastic transformation as in the case of eukaryotic elongation factor 1 A2, a protein normally expressed only by skeletal muscle, heart and nervous system [2][3][4][5][6][7] . Thus, a better understanding of the mechanisms underlying these signaling cascades may be of great diagnostic and therapeutic potentials.…”

Tumor suppressor p16INK4a inhibits cancer cell growth by down-regulating eEF1A2 through a direct interaction

“…The eEF1A1 mRNA and protein are expressed ubiquitously in many cancer cell types (Joseph et al, 2004;Scaggiante et al, 2012) (supplementary material Fig. S4).…”