α‐enolase: a promising therapeutic and diagnostic tumor target

Capello, Michela; Ferri-Borgogno, Sammy; Cappello, Paola; Novelli, Francesco

doi:10.1111/j.1742-4658.2011.08025.x

Cited by 227 publications

(235 citation statements)

References 125 publications

(161 reference statements)

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“…In line with these considerations, high levels of ENO-1 were found in many types of cancer, including head, neck, breast, and lung cancer (44). High levels of ENO-1 in cancer cells correlate with cancer progression and a poor clinical outcome of the affected patients (12). Ectopic overexpression of ENO-1 promotes cell proliferation, migration, invasion, and colony formation, thereby contributing to metastasis formation (19,21,45).…”

Section: Discussionmentioning

confidence: 77%

“…Enolase-1 is a glycolytic enzyme primarily localized in the cytoplasm of prokaryotic and eukaryotic cells (12). However, under stimulatory conditions, ENO-1 can be translocated to the cell surface, where it acts as a PLG receptor (13).…”

Section: Discussionmentioning

confidence: 99%

“…Cell surface bound enolase-1 (ENO-1) is one of them. It primarily acts as a glycolytic enzyme localized in the cytoplasm (12). However, under stimulatory conditions, it can be translocated to the cell surface where it interacts with PLG and thus participates in the regulation of pericellular proteolysis, allowing cells to invade tissue (13)(14)(15).…”

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confidence: 99%

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STIM1/ORAI1-mediated Ca2+ Influx Regulates Enolase-1 Exteriorization

Didiášová

Zakrzewicz

Magdolen

et al. 2015

Journal of Biological Chemistry

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Background: Cell surface-associated enolase-1 regulates plasmin formation and thus pericellular proteolysis. Results: STIM1/ORAI1-mediated Ca 2ϩ influx controls enolase-1 exteriorization in cancer cells. Conclusion: Extracellular enolase-1 regulates migratory and invasive properties of cancer cells. Significance: Enhanced exteriorization of enolase-1 may aggravate the malignant behavior of cancer cells and thus contribute to metastasis formation.

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Section: Discussionmentioning

confidence: 77%

Section: Discussionmentioning

confidence: 99%

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STIM1/ORAI1-mediated Ca2+ Influx Regulates Enolase-1 Exteriorization

Didiášová

Zakrzewicz

Magdolen

et al. 2015

Journal of Biological Chemistry

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“…5 In the cytoplasm, ENO1 acts as a glycolytic enzyme, whereas on the membrane it acts as a plasminogen receptor and plays an important role in cell migration. 6,7 We have shown that patients with PDA with autoantibodies to ENO1 also present an ENO1-specific T-cell response that is not observed in patients with no ENO1 autoantibodies. On transfer into immunocompromised mice, ENO1-specific T cells inhibit the growth of xenotransplanted human pancreatic tumors.…”

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confidence: 99%

Vaccination With ENO1 DNA Prolongs Survival of Genetically Engineered Mice With Pancreatic Cancer

et al. 2013

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See Covering the Cover synopsis on page 862. BACKGROUND & AIMS:Pancreatic ductal adenocarcinoma (PDA) is an aggressive tumor, and patients typically present with late-stage disease; rates of 5-year survival after pancreaticoduodenectomy are low. Antibodies against ␣-enolase (ENO1), a glycolytic enzyme, are detected in more than 60% of patients with PDA, and ENO1-specific T cells inhibit the growth of human pancreatic xenograft tumors in mice. We investigated whether an ENO1 DNA vaccine elicits antitumor immune responses and prolongs survival of mice that spontaneously develop autochthonous, lethal pancreatic carcinomas. METHODS:We injected and electroporated a plasmid encoding ENO1 (or a control plasmid) into Kras G12D /Cre (KC) mice and Kras G12D /Trp53 R172H /Cre (KPC) mice at 4 weeks of age (when pancreatic intraepithelial lesions are histologically evident). Antitumor humoral and cellular responses were analyzed by histology, immunohistochemistry, enzyme-linked immunosorbent assays, flow cytometry, and enzyme-linked immunosorbent spot and cytotoxicity assays. Survival was analyzed by Kaplan-Meier analysis. RESULTS: The ENO1 vaccine induced antibody and a cellular response and increased survival times by a median of 138 days in KC mice and 42 days in KPC mice compared with mice given the control vector. On histologic analysis, the vaccine appeared to slow tumor progression. The vaccinated mice had increased serum levels of anti-ENO1 immunoglobulin G, which bound the surface of carcinoma cells and induced complement-dependent cytotoxicity. ENO1 vaccination reduced numbers of myeloid-derived suppressor cells and T-regulatory cells and increased T-helper 1 and 17 responses. CONCLU-SIONS: In a genetic model of pancreatic carcinoma, vaccination with ENO1 DNA elicits humoral and cellular immune responses against tumors, delays tumor progression, and significantly extends survival. This vaccination strategy might be developed as a neoadjuvant therapy for patients with PDA.

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“…Recent studies have revealed that ENO1 can be detected in many prokaryotic and eukaryotic cells, and localized in cytoplasm, cell surface and nucleus of various mammalian cells to possibly mediate distinct functions (Liu et al, 2007). ENO1 gene up-regulation in mRNA and/or protein levels have been observed in several tumors, including brain, breast, cervix, colon, eye, and so on (Liu et al, 2007;Capello et al, 2011).…”

Section: Resultsmentioning

confidence: 99%

Expression of Eleven Egg Performance-associated Genes in the Ovary of Zi Geese <i>Anser anser domestica</i>

Wang

Guo

et al. 2013

J. Poult. Sci.

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a These authors contributed equallyThe relative expression of eleven egg performance-associated genes including the tau-crystallin/α enolase (ENO1), ribosomal protein S27a (RPS27A), calmodulin 1 (CALM1), solute carrier family 25 A6 (SLC25A6), arylsulfatase A (ARSA), syndecan 2 (SDC2), ribosomal protein L10a (RPL10A), ornithine decarboxylase antizyme 1 (OAZ1), cytochrome c somatic variant 2 (CYCS), adenosine triphosphate synthase, H + transporting, α subunit, isoform 1 (ATP5A1) and the ring finger protein 130 (RNF130) in the ovaries of pre-laying and laying Zi geese were analyzed using quantitative real-time PCR (qRT-PCR). Comparison between pre-laying and egg-laying stages, the relative expression of ENO1, RPS27A, SLC25A6, ARSA, SDC2, RPL10A, OAZ1, CYCS and RNF130 were significantly upregulated (P＜0.05), whereas the CALM1 and ATP5A1 were highly significantly up-regulated (P＜0.01). This study established the primary foundation to understand the possible roles of these genes in the ovaries.Key words: egg performance-associated genes, geese, ovaries, qRT-PCR J. Poult. Sci., 50: 91-98, 2013 Introduction Zi geese (Anser anser domestica) are excellent layers (around 100 per year) with a superior feed-to-egg conversion ratio (Kang et al., 2009). This species breeds in Northeast China (HeiLongjiang and JiLin provinces). In our previous study, in order to study the molecular genetic mechanisms of egg laying and improve laying performance, suppression subtractive hybridization (SSH) and reverse dot-blot were employed to identify egg laying performance-associated genes in the ovaries. We have discovered that the expression of 18 known and 8 unknown gene fragments were higher in the ovaries of egg-laying geese than pre-laying geese (Kang et al., 2009 identified to be differentially expressed in the ovaries by SSH. Their expression were confirmed by using quantitative real-time PCR (qRT-PCR) in both egg-laying and pre-laying stages in the ovaries of the Zi geese. This results provided the primary foundation to understand the possible roles of these genes in egg formation in geese. Materials and Methods Geese and Tissue CollectionTwenty female Zi geese were selected on a local farm and were raised according to the program used in farm. All the geese were fed according to conventional farming (Kang et al., 2009). Ten geese were killed by exsanguination at 5-month-old (average BW＝3.0±0.2 kg) and the ovaries were treated at pre-laying stage. Another 10 geese were killed at 8-month-old (average BW＝3.5±0.2 kg) and the ovaries were treated at egg-laying stage. Ovaries samples, which comprised the whole ovary including the small and large yellow follicles, were rapidly removed, wrapped in foil, frozen in liquid nitrogen, and stored at −70℃ until analysis. Extraction of Total RNA and Quality ControlTotal RNA was prepared by the Trizol reagent (Invitrogen Corporation, CA, U.S.A.) according to the instructions of the manufacturer. The total RNA samples from pre-laying and laying ovaries (n＝10, for each) were pooled separately. Genom...

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α‐enolase: a promising therapeutic and diagnostic tumor target

Cited by 227 publications

References 125 publications

STIM1/ORAI1-mediated Ca2+ Influx Regulates Enolase-1 Exteriorization

STIM1/ORAI1-mediated Ca2+ Influx Regulates Enolase-1 Exteriorization

Vaccination With ENO1 DNA Prolongs Survival of Genetically Engineered Mice With Pancreatic Cancer

Expression of Eleven Egg Performance-associated Genes in the Ovary of Zi Geese <i>Anser anser domestica</i>

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