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

Enolase - a glycolytic enzyme is also expressed on the surface of eukaryotic cells such as macrophages, neutrophils, endothelial, neuronal, tumor cells. Surface enolase as plasminogen receptor plays an important role in myogenesis, tumorgenesis and angiogenesis. Determination of enolase localization...

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Main Authors: Tomasz Dawiskiba, Julita Kulbacka, Jolanta Saczko, Regina Danielewicz, Iwona S Bednarz-Misa, Ewa Seweryn, Jadwiga Pietkiewicz
Format: Article
Language:English
Published: Via Medica 2009-01-01
Series:Folia Histochemica et Cytobiologica
Online Access:http://czasopisma.viamedica.pl/fhc/article/view/4393
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spelling doaj-2811415a4b344136af3b4a906257492b2020-11-24T20:56:12ZengVia MedicaFolia Histochemica et Cytobiologica0239-85081897-56312009-01-0146451952410.5603/4393Distribution of beta-enolase in normal and tumor rat cells.Tomasz DawiskibaJulita KulbackaJolanta SaczkoRegina DanielewiczIwona S Bednarz-MisaEwa SewerynJadwiga PietkiewiczEnolase - a glycolytic enzyme is also expressed on the surface of eukaryotic cells such as macrophages, neutrophils, endothelial, neuronal, tumor cells. Surface enolase as plasminogen receptor plays an important role in myogenesis, tumorgenesis and angiogenesis. Determination of enolase localization in the cell lines may give rise to the elucidation of its receptor function in tumor cells. The cellular localization of the muscle-specific isoform of the enolase in normal rat cardiomyocytes (H9c2, an embryonic rat heart-derived cell line) and a rat sarcoma (R1) cell line is reported here. Immunocytochemical assays showed that this enolase isoform is freely diffused in the sarcoplasm of rat cells. The evident location of enolase molecules on the perinuclear surface is observed in immunofluorescence assays. Enolase localization on the surface of some intact normal rat cardiomyocytes was also observed. This surface protein maintains enolase catalytic activity.http://czasopisma.viamedica.pl/fhc/article/view/4393
collection DOAJ
language English
format Article
sources DOAJ
author Tomasz Dawiskiba
Julita Kulbacka
Jolanta Saczko
Regina Danielewicz
Iwona S Bednarz-Misa
Ewa Seweryn
Jadwiga Pietkiewicz
spellingShingle Tomasz Dawiskiba
Julita Kulbacka
Jolanta Saczko
Regina Danielewicz
Iwona S Bednarz-Misa
Ewa Seweryn
Jadwiga Pietkiewicz
Distribution of beta-enolase in normal and tumor rat cells.
Folia Histochemica et Cytobiologica
author_facet Tomasz Dawiskiba
Julita Kulbacka
Jolanta Saczko
Regina Danielewicz
Iwona S Bednarz-Misa
Ewa Seweryn
Jadwiga Pietkiewicz
author_sort Tomasz Dawiskiba
title Distribution of beta-enolase in normal and tumor rat cells.
title_short Distribution of beta-enolase in normal and tumor rat cells.
title_full Distribution of beta-enolase in normal and tumor rat cells.
title_fullStr Distribution of beta-enolase in normal and tumor rat cells.
title_full_unstemmed Distribution of beta-enolase in normal and tumor rat cells.
title_sort distribution of beta-enolase in normal and tumor rat cells.
publisher Via Medica
series Folia Histochemica et Cytobiologica
issn 0239-8508
1897-5631
publishDate 2009-01-01
description Enolase - a glycolytic enzyme is also expressed on the surface of eukaryotic cells such as macrophages, neutrophils, endothelial, neuronal, tumor cells. Surface enolase as plasminogen receptor plays an important role in myogenesis, tumorgenesis and angiogenesis. Determination of enolase localization in the cell lines may give rise to the elucidation of its receptor function in tumor cells. The cellular localization of the muscle-specific isoform of the enolase in normal rat cardiomyocytes (H9c2, an embryonic rat heart-derived cell line) and a rat sarcoma (R1) cell line is reported here. Immunocytochemical assays showed that this enolase isoform is freely diffused in the sarcoplasm of rat cells. The evident location of enolase molecules on the perinuclear surface is observed in immunofluorescence assays. Enolase localization on the surface of some intact normal rat cardiomyocytes was also observed. This surface protein maintains enolase catalytic activity.
url http://czasopisma.viamedica.pl/fhc/article/view/4393
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