Localization of Enolase in the Subfractions of a Breast Cancer Cell Line

Seweryn, Ewa; Bednarz−Misa, Iwona; Ceremuga, Ireneusz; Saczko, Jolanta; Kulbacka, Julita; Gamian, Andrzej

doi:10.1515/znc-2009-9-1023

Cited by 17 publications

(12 citation statements)

References 22 publications

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“…Most probably, these proteins possess auxiliary function. Enolase is a glycolytic enzyme present in eukaryotes and prokaryotes (Seweryn et al 2007, 2009). In humans, besides catalyzing glycolysis and gluconeogenesis, it composes membranes of epithelial and endothelial cells, monocytes, leucocytes, and neutrophiles where it acts as a receptor of human plasminogen (Pancholi and Fischetti 1998; Pancholi 2001; Lopez-Alemany et al 2003; Diaz-Ramos et al 2012).…”

Section: Introductionmentioning

confidence: 99%

Enolase-like protein present on the outer membrane of Pseudomonas aeruginosa binds plasminogen

et al. 2014

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Pseudomonas aeruginosa is one of the pathogenic bacteria which utilize binding of the host plasminogen (Plg) to promote their invasion throughout the host tissues. In the present study, we confirmed that P. aeruginosa exhibits binding affinity for human plasminogen. Furthermore, we showed that the protein detected on the cell wall of P. aeruginosa and binding human plasminogen is an enolase-like protein. The hypothesis that alpha-enolase, a cytoplasmatic glycolytic enzyme, resides also on the cell surface of the bacterium was supported by electron microscopy analysis. The plasminogen-binding activity of bacterial cell wall outer membrane enolase-like protein was examined by immunoblotting assay.

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Section: Introductionmentioning

confidence: 99%

Enolase-like protein present on the outer membrane of Pseudomonas aeruginosa binds plasminogen

et al. 2014

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“…ENOA is localized on the cell surface of PDAC, breast and lung cancers [67,154,172,189] (Table 3), while in melanoma and NSCLC it is also secreted by exosomes [190,191]. On cell surfaces, ENOA is part of a multi-protein complex, together with uPA receptor (uPAR), integrins and certain cytoskeletal proteins, collectively known as a metastasome , responsible for adhesion, migration and proliferation, as clearly demonstrated in ovarian cancer cells [192].…”

Section: Introductionmentioning

confidence: 99%

Three are better than one: plasminogen receptors as cancer theranostic targets

et al. 2013

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Activation of plasminogen on the cell surface initiates a cascade of protease activity with important implications for several physiological and pathological events. In particular, components of the plasminogen system participate in tumor growth, invasion and metastasis. Plasminogen receptors are in fact expressed on the cell surface of most tumors, and their expression frequently correlates with cancer diagnosis, survival and prognosis. Notably, they can trigger multiple specific immune responses in cancer patients, highlighting their role as tumor-associated antigens. In this review, three of the most characterized plasminogen receptors involved in tumorigenesis, namely Annexin 2 (ANX2), Cytokeratin 8 (CK8) and alpha-Enolase (ENOA), are analyzed to ascertain an overall view of their role in the most common cancers. This analysis emphasizes the possibility of delineating new personalized therapeutic strategies to counteract tumor growth and metastasis by targeting plasminogen receptors, as well as their potential application as cancer predictors.

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“…It is expressed on the surface of eukaryotic cells such as macrophages, neutrophils, endothelial, neuronal and tumor cells (32). Moreover, it is important in myogenesis, tumorgenesis and angiogenesis (32), as well as for pathogen invasiveness and the development of tumors (33). It has been shown that enolase mediates the activation of enzymes involved in the invasion of tissues by pathogens and tumor cells, as well as in the evasion of host immune responses (34), and that it is sensitive to fluoride (35).…”

Section: Discussionmentioning

confidence: 99%

Elevated enolase and caveolin-1 in the heart of rats following dexamethasone-induced toxicity

Huang

Liu

2012

Mol Med Report

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Abstract. Dexamethasone (DEX)-induced heart damage is associated with enzyme and protein alterations. The purpose of this study was to investigate DEX-induced alterations in cardiac enolase and caveolin-1 (cav-1) following DEX administration. Male Wistar rats were randomly divided into two groups: a control and a DEX. The DEX group intraperitoneally received DEX at the single dose of 10 mg/kg for 7 consecutive days, and the control was given the same amount of saline via the same route. On day 8, the rats were anesthetized, and a thoracotomy was performed in all animals. Immunohistochemical analysis was performed to evaluate protein expression of enolase and cav-1. Sections were analyzed by digital image analysis. Our results demonstrated that cardiac protein expression of enolase and cav-1 was altered following DEX-induced toxicity in the rat. The expression of enolase and cav-1 was significantly increased after DEX treatment, supported by integrated optical density compared with the control (P<0.05). In conclusion, following DEX-induced toxicity, protein expression of enolase and cav-1 was significantly elevated. The current findings indicate that such alterations would be reflected in abnormal cardiac function, and the proteins identified in this study may be useful in revealing the mechanisms underlying DEX-induced toxicity and also in providing various clues for further research.

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Localization of Enolase in the Subfractions of a Breast Cancer Cell Line

Cited by 17 publications

References 22 publications

Enolase-like protein present on the outer membrane of Pseudomonas aeruginosa binds plasminogen

Enolase-like protein present on the outer membrane of Pseudomonas aeruginosa binds plasminogen

Three are better than one: plasminogen receptors as cancer theranostic targets

Elevated enolase and caveolin-1 in the heart of rats following dexamethasone-induced toxicity

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