Anti-α-enolase is a prognostic marker in postoperative lung cancer patients

Hsiao, Kuan Chung; Shih, Neng Yao; Chu, Pei Yi; Hung, Yi Mei; Liao, Jia; Chou, Shao Wen; Yang, Yi Yuan; Chang, Gee Chen; Liu, Ko Jiunn

doi:10.18632/oncotarget.5316

Cited by 20 publications

(22 citation statements)

References 37 publications

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“…There are a few biomarkers for the diagnosis and prognosis prediction in lung cancer and their usefulness is hampered because of low diagnostic and prognostic value 11-13. Although it was unclear whether the soluble and secretory form of AIMP2-DX2 would exist in the blood, its autoantibody was detectable in the blood and showed the correlation with serum CYFRA 21-1 (γ = 0.133, P = 0.056; data not shown), a soluble fragment of cytokeratin 19 filaments 14, 15…”

Section: Discussionmentioning

confidence: 99%

Ratio of Autoantibodies of Tumor Suppressor AIMP2 and Its Oncogenic Variant Is Associated with Clinical Outcome in Lung Cancer

Jung¹,

Kim²,

Kim³

et al. 2017

J. Cancer

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Aminoacyl-tRNA synthetase-interacting multi-functional protein 2 (AIMP2) works as potent tumor suppressor, while its splicing variant lacking exon 2 (AIMP2-DX2) competes with AIMP2 for binding to target proteins and compromises its anti-tumor activity. Assuming that AIMP2 and its variant AIMP2-DX2 could be released out to human sera in pathological condition, we investigated the diagnostic and prognostic usefulness of autoantibodies against AIMP2 and AIMP2-DX2 by measuring their serum levels in 80 normal and lung cancer samples that were matched in age, gender and smoking status. The area under the curve of AIMP2-DX2, AIMP2, and AIMP2-DX2/AIMP2 autoantibody ratio was low (0.416, 0.579, and 0.357, respectively), suggesting limited diagnostic value. A total of 165 lung cancer patients were classified into low and high AIMP2-DX2, AIMP2, and AIMP2-DX2/AIMP2 based on the median expression of each parameter. The high AIMP2-DX2 group was older and had larger tumors (>3 cm) than the low AIMP2-DX2 group. The high AIMP2-DX2/AIMP2 group had higher CYFRA-21 levels and significantly shorter overall survival than the low AIMP2-DX2/AIMP2 group (18.6 vs. 48.9 months, P = 0.021, Log Rank Test). Taken together, autoantibodies against AIMP2-DX2 and AIMP2 are detectable in the human blood and the increased ratio of AIMP2-DX2/AIMP2 is related to poor clinical outcome of lung cancer.

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Section: Discussionmentioning

confidence: 99%

Ratio of Autoantibodies of Tumor Suppressor AIMP2 and Its Oncogenic Variant Is Associated with Clinical Outcome in Lung Cancer

Jung¹,

Kim²,

Kim³

et al. 2017

J. Cancer

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“…It is responsible for catalysing the conversion of 2‐phosphate‐D‐glycerate to phosphoric acid pyruvate during glycolysis and the reverse conversion during glycogen synthesis . ENO1 is predominantly expressed in the cytoplasm; however, it is also expressed on the cell surface and in the nucleus of various eukaryotes . In addition, ENO1 also plays an important role in several biological and pathophysiological processes .…”

Section: Discussionmentioning

confidence: 99%

“…Alpha‐enolase (ENO1) is a key glycolytic enzyme responsible for the glycolytic pathway. It is a multifunctional protein and is involved in many different physiological and pathophysiological processes . Cytoskeletal components are closely connected with viral transport mechanisms within cells, subcellular localization of associated transport systems and maintenance of the viral replication status.…”

Section: Introductionmentioning

confidence: 99%

Alpha‐enolase regulates hepatitis B virus replication through suppression of the interferon signalling pathway

Ding

Xiaoqing

Yan

et al. 2017

Journal of Viral Hepatitis

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Persistent chronic infection with hepatitis B virus (HBV) is a major risk factor for the development of HBV-related diseases. The molecular mechanisms that underlie HBV infection and associated carcinogenesis are not fully understood. The aim of this study was to explore the role of ENO1 in HBV replication processes. Here, we examined ENO1 expression levels in HBV-infected and non-HBV-infected liver tissues and cells by Western blot analysis, real-time PCR and immunohistochemistry. In addition, HBsAg and HBeAg in the media of transfected HepG2.2.15 cells were detected using an electrochemical luminescence analyser within 48 hours after ENO1-specific siRNA transfection. The expression levels of HBV DNA, type I interferon and 5 downstream IFN-stimulated genes in HepG2.2.15 cells were examined using real-time PCR. We found ENO1 expression was upregulated in the HBV-infected liver tissues and cells. Silencing of ENO1 resulted in a significant reduction in HBV replication, and this siRNA-mediated reaction also caused the upregulation of expression of type I interferon and downstream IFN-stimulated genes. Therefore, we come to the conclusion ENO1 is involved in HBV replication. It is therefore likely that HBV replication is enhanced following suppression of the IFN signalling pathway. However, the mechanisms that underpin ENO1-mediated modulation of the IFN signalling pathway remain to be elucidated.

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“…Patients with a higher increase in anti-a-enolase had a lower hazard ratio and better PFS [85] Sera from patients with lung cancer (n = 72), benign lung diseases (n = 69), and healthy individuals (n = 70) Autoantibodies were higher in lung cancer sera compared with sera from normal and benign lung disease patients; Autoantibodies were higher in stage I/II than in stage III/IV [89] Lymphoma…”

Section: Enolase Inhibitors Are Potential Anticancer Agentsmentioning

confidence: 99%

“…Autoantibodies generated against a-enolase in its capacity as a tumour-associated antigen represent an additional type of prognostic biomarker that may be assayed in serum. The presence of autoantibodies against a-enolase correlated with longer disease-free survival and overall survival in pancreatic and lung cancer patients [45,[85][86][87] [ Table 4]. Furthermore, compared with healthy individuals, a-enolase antibodies…”

Section: Alpha-enolase Is a Prognostic Factor For Multiple Cancer Typesmentioning

confidence: 99%

Unlikely role of glycolytic enzyme ��-enolase in cancer metastasis and its potential as a prognostic biomarker

Schofield¹,

Lincz²,

Skelding³

2020

JCMT

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Reliance on glycolysis for energy production is considered a hallmark of cancer and the glycolytic enzyme a-enolase is overexpressed in a range of cancer types. However, recent studies have revealed that a-enolase is involved in a variety of unrelated physiological processes and can be found in multiple unexpected cellular locations. This review focuses on the unlikely role of a-enolase as an extracellular plasminogen-binding receptor localised to the plasma membrane. Conversion of plasminogen to plasmin on the surface of cancer cells enhances their ability to invade through stroma by activating collagenases and degrading fibrin as well as extracellular matrix proteins. Increased expression of a-enolase is associated with increased migration and invasion of cancer cells, and decreased metastasis-free survival in patients with several cancer types, including non-small cell lung, pancreatic, breast and colorectal cancers. Due to its overexpression in a range of cancer types and multi-functional roles in key areas of tumour metabolism and metastasis, a-enolase may be useful as a universal cancer prognostic biomarker or therapeutic target.

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Anti-α-enolase is a prognostic marker in postoperative lung cancer patients

Cited by 20 publications

References 37 publications

Ratio of Autoantibodies of Tumor Suppressor AIMP2 and Its Oncogenic Variant Is Associated with Clinical Outcome in Lung Cancer

Ratio of Autoantibodies of Tumor Suppressor AIMP2 and Its Oncogenic Variant Is Associated with Clinical Outcome in Lung Cancer

Alpha‐enolase regulates hepatitis B virus replication through suppression of the interferon signalling pathway

Unlikely role of glycolytic enzyme ��-enolase in cancer metastasis and its potential as a prognostic biomarker

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