Distribution of beta-enolase in normal and tumor rat cells.

Seweryn, Ewa; Bednarz−Misa, Iwona; Danielewicz, Regina; Saczko, Jolanta; Kulbacka, Julita; Dawiskiba, Tomasz

doi:10.2478/v10042-008-0075-7

Cited by 5 publications

(6 citation statements)

References 28 publications

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“…Similar observations were reported by Witkowska et al (2005) for a enolase-like protein of the surface bacterial cells of Klebsiella pneumonia. This phenomenon was observed in experiments with intact cell lines of rat sarcoma and normal cardiomyocytes (Seweryn et al, 2008).…”

Section: Resultsmentioning

confidence: 57%

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

Seweryn

Bednarz−Misa

Ceremuga

et al. 2009

Zeitschrift Für Naturforschung C

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Cell fractionationCells were washed twice in cold PBS and then resuspended in hypotonic buffer containing 10 mM Localization of Enolase in the Subfractions of a Breast Cancer Cell LineEwa Seweryn*, Jadwiga Pietkiewicz, Iwona S. Bednarz-Misa, Ireneusz Ceremuga, Jolanta Saczko, Julita Kulbacka, and Andrzej Gamian Enolase detected on the cell surface may be a receptor for certain ligands, especially for plasminogen. It is important for the pathogen invasiveness and in the development of a tumour. Therefore, we sought to preliminarily determine the enolase location and catalytic activity in the subfractions of MCF-7 cells. The latter was done on intact cells and in subfractions of MCF-7 cells. We identifi ed enolase by immunoblotting. The binding of human plasminogen to enolase was performed by immunoblotting using monoclonal antibodies against plasminogen. The intact MCF-7 cells demonstrated activity of enolase. Enolase in postnuclear and perinuclear fractions is catalyticly active too. We identifi ed the enolase protein in immunoblots of these fractions, except for the nuclear subfraction. These results provide evidence that enolase is present on the intact surface of MCF-7 cells and in post-and perinuclear fractions. The surface protein maintained catalytic activity, which suggests that its location in the plasma membrane didn't change the active centre of the enzyme.

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Section: Resultsmentioning

confidence: 57%

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

Seweryn

Bednarz−Misa

Ceremuga

et al. 2009

Zeitschrift Für Naturforschung C

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“…ENOB is a glycolytic enzyme, which can reversibly catalyze the conversion of 2-phosphoglycerate to phosphoenolpyruvate. This enzyme is found in muscle cells, where it may be involved in muscle development and regeneration ( 28 ). α-enolase (ENOA), another enolase, can switch to ENOB in rodents during muscle tissue development.…”

Section: Discussionmentioning

confidence: 99%

Comparative proteomic analysis of rats subjected to water immersion and restraint stress as an insight into gastric ulcers

Zhou

Huang

Song

et al. 2017

Molecular Medicine Reports

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In the present study, comparative proteomic analysis was performed in rats subjected to water immersion-restraint stress (WRS). A total of 26 proteins were differentially expressed and identified using matrix-assisted laser desorption/ionization time of flight mass spectrometry. Among the 26 differentially expressed protein spots identified, 13 proteins were significantly upregulated under WRS, including pyruvate kinase and calreticulin, which may be closely associated with energy metabolism. In addition, 12 proteins were downregulated under WRS, including hemoglobin subunit β-2 and keratin type II cytoskeletal 8, which may be important in protein metabolism and cell death. Gene Ontology analysis revealed the cellular distribution, molecular function and biological processes of the identified proteins. The mRNA levels of certain differentially expressed proteins were analyzed using fluorescence quantitative polymerase chain reaction analysis. The results of the present study aimed to offer insights into proteins, which are differentially expressed in gastric ulcers in stress, and provide theoretical evidence of a radical cure for gastric ulcers in humans.

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“…Recently, enolase was revealed to be an important protein in many pathophysiological and disease processes (31). 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).…”

Section: Discussionmentioning

confidence: 99%

“…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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Distribution of beta-enolase in normal and tumor rat cells.

Cited by 5 publications

References 28 publications

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

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

Comparative proteomic analysis of rats subjected to water immersion and restraint stress as an insight into gastric ulcers

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

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