RETRACTED: Proteomics-based identification of α-enolase as a potential prognostic marker in cholangiocarcinoma

Yonglitthipagon, Ponlapat; Pairojkul, Chawalit; Bhudhisawasdi, Vajarabhongsa; Mulvenna, Jason; Loukas, Alex; Sripa, Banchob

doi:10.1016/j.clinbiochem.2012.04.004

Cited by 20 publications

(15 citation statements)

References 30 publications

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“…For example, ENO1 is involved with various types of human cancer. ENO1 is upregulated in retinoblastoma (4) and is considered a diagnostic marker of hepatocellular carcinoma (5), pancreatic cancer (6), renal cell carcinoma (7,8) and cholangiocarcinoma (9). In addition, abnormally upregulated ENO1 is associated with poor survival and prognosis in patients with mammary carcinoma (10).…”

Section: Introductionmentioning

confidence: 99%

Enolase 1 differentially contributes to cell transformation in lung cancer but not in esophageal cancer

et al. 2020

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Enolase transforms 2-phospho-D-glycerate into phosphoenolpyruvate during glycolysis. The human enolase (ENO) family comprises three members named ENO3, which is restricted to muscle tissues, ENO2, which is neuron-and neuroendocrine tissue-specific, and ENO1, which is expressed in almost all tissues. ENO1 is involved in various types of human cancer, including retinoblastoma, hepatocellular carcinoma, pancreatic cancer, renal cell carcinoma, cholangiocarcinoma and gastric cancer. Furthermore, ENO1 enhances cell transformation in numerous cancer cell lines. It has been reported that ENO1 is involved in various activities that are detrimental to cell transformation, including apoptosis and differentiation. However, a few studies demonstrated that ENO1 can be downor upregulated in various types of lung cancer, which suggests that ENO1 has an ambiguous role in the development of lung cancer. The present study aimed to investigate the differential influences of ENO1 on various types of cancer, and to clarify the role of ENO1 in lung cancer in particular. Western blotting was performed to assess ENO1 protein expression levels in lung cancer and esophageal cancer tissues. Furthermore, exogenous ENO1 was overexpressed in cell lines derived from various tissues and single cell proliferation, flowcytometric analysis, and western blotting were performed to determine the cell proliferation rate, cell transformation status, cell cycle progression and the expression of cell cycle regulators, such as cyclins and cyclin-dependent kinases, and survival factors, such as MAPK and AKT. The results demonstrated that ENO1 was upregulated in collected panels of lung cancer tissues, but not in esophageal cancer tissues. In addition, overexpression of ectopic ENO1 promoted cell proliferation and survival in lung cancer cell lines, which was not the case in other cells, including an esophageal cell line. Furthermore, mechanistic analyses revealed that ENO1 enhanced cell proliferation by accelerating G 1 progression and upregulating G 1 phase cyclin-dependent kinase 6 (CDK6), and improved cell survival by upregulating p38 in the MAPK cascade and increasing p-AKT in the AKT cascade, in particular in lung cancer cell lines. Overall, the results from the present study demonstrated that ENO1 may contribute to the development of lung cancers, but not esophageal cancers.

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Section: Introductionmentioning

confidence: 99%

Enolase 1 differentially contributes to cell transformation in lung cancer but not in esophageal cancer

et al. 2020

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“…ENO1 expression is frequently increased in diverse tumors, including head and neck, 6 thyroid, 7 breast, 8 lung, 9,10 prostate, 11 colon and gastric cancer, 12,13 glioma 14 and cholangiocarcinoma. 15 Moreover, overexpression of ENO1 is positively associated with progression and poor prognosis in several tumors.…”

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confidence: 99%

FBXW7 negatively regulates ENO1 expression and function in colorectal cancer

Zhan

Wang

Zhao

et al. 2015

Laboratory Investigation

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FBXW7 (F-box and WD40 domain protein 7) is a tumor suppressor frequently inactivated in human cancers. The precise molecular mechanisms by which FBXW7 exerts antitumor activity remain under intensive investigation and are thought to relate in part to FBXW7-mediated destruction of key cancer-relevant proteins. Enolase 1 (ENO1) possesses oncogenic activity and is often overexpressed in various human cancers, besides its critical role in glycolysis. However, the detailed regulatory mechanisms of ENO1 expression remain unclear. Here we show that the elevated expression of ENO1 was identified in FBXW7-depletion HCT116 cells through two-dimensional protein electrophoresis and mass spectrometry assays (2DE-MS). Subsequent western blotting and immunohistochemical assays confirmed that ENO1 expression reversely correlates with FBXW7 expression in several cells and colon cancer tissues. Furthermore, we show that FBXW7 physically binds to ENO1 and targets ENO1 for ubiquitin-mediated degradation. Functionally, we found that FBXW7 suppresses the ENO1-induced gene expression, lactate production, cell proliferation and migration. These findings suggest that ENO1 is a novel substrate of FBXW7, and its activity can be negatively regulated by FBXW7 at the posttranslational level. Our work provides a novel molecular insight into FBXW7-directed tumor suppression through regulation of ENO1.

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“…The expression level of this protein was downregulated in H69 cells at all time-points except at 48 h after incubation with O. viverrini ES products, at which point it was significantly upregulated. Interestingly, Yonglitthipagon et al [32] suggested a role for alpha-enolase as a prognostic indicator for CCA patients because the expression level of this protein was upregulated in carcinogenic cells when compared to non-carcinogenic H69 cells. The fact that the expression level of this protein was only upregulated after 48 h could be linked to a change in the cell growth pattern observed for this cell line, but more time-points should be studied to confirm this hypothesis.…”

Section: Discussionmentioning

confidence: 99%

Proteomic characterization of the internalization of Opisthorchis viverrini excretory/secretory products in human cells

Chaiyadet

Smout

Laha

et al. 2017

Parasitology International

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The association between liver fluke infection caused by Opisthorchis viverrini and cholangiocarcinoma (CCA — hepatic cancer of the bile duct epithelium) has been well established. Multiple mechanisms play a role in the development of CCA, but the excretory/secretory products released by O. viverrini (OvES) represent the major interface between the parasite and its host, and their uptake by biliary epithelial cells has been suggested to be responsible for proliferation of cholangiocytes, the cells that line the biliary epithelium. Despite recent progress in the study of the molecular basis of O. viverrini–host interactions, little is known about the effects that OvES induces upon internalization by host cells. In the present study we incubated non-cancerous human cholangiocytes (H69) and human colon cancer (CaCo-2) cells with OvES and performed a time-course quantitative proteomic analysis on the cells to determine the early changes induced by the parasite. Different KEGG pathways were altered in H69 cells compared to Caco-2 cells: glycolysis/gluconeogenesis and protein processing in the endoplasmic reticulum. In addition, the Reactome pathway analysis showed a predominance of proteins involved in cellular pathways related to apoptosis and apoptotic execution phase in H69 cells after incubation with OvES. The present study provides the first proteomic analysis to address the molecular mechanisms by which OvES products interact with host cells, and Sheds light on the cellular processes involved in O. viverrini-induced CCA.

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RETRACTED: Proteomics-based identification of α-enolase as a potential prognostic marker in cholangiocarcinoma

Cited by 20 publications

References 30 publications

Enolase 1 differentially contributes to cell transformation in lung cancer but not in esophageal cancer

Enolase 1 differentially contributes to cell transformation in lung cancer but not in esophageal cancer

FBXW7 negatively regulates ENO1 expression and function in colorectal cancer

Proteomic characterization of the internalization of Opisthorchis viverrini excretory/secretory products in human cells

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