دورية أكاديمية
The Carcinoma-associated Antigen EpCAM Induces Glyoxalase 1 Resulting in Enhanced Methylglyoxal Turnover.
| العنوان: | The Carcinoma-associated Antigen EpCAM Induces Glyoxalase 1 Resulting in Enhanced Methylglyoxal Turnover. |
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| المؤلفون: | Münz M; Clinical Cooperation Group Molecular Oncology, GSF-Research Center for Environment and Health, and Head and Neck Research Department Munich., Hofmann T; Head and Neck Research Department, University Clinics Großhadern, Marchioninistr. 15, 81377 Munich., Scheibe B; Amersham Biosciences Europe GmbH, Münzingerstr. 9, 79111 Freiburg., Gänge M; Amersham Biosciences Europe GmbH, Münzingerstr. 9, 79111 Freiburg., Junghanns KT; Amersham Biosciences Europe GmbH, Münzingerstr. 9, 79111 Freiburg., Zeidler R; Vaecgene Biotech. Inc., Marchioninistr. 25, D-81377 Munich, Germany., Gires O; Clinical Cooperation Group Molecular Oncology, GSF-Research Center for Environment and Health, and Head and Neck Research Department Munich.; Head and Neck Research Department, University Clinics Großhadern, Marchioninistr. 15, 81377 Munich. |
| المصدر: | Cancer genomics & proteomics [Cancer Genomics Proteomics] 2004 May-Jun; Vol. 1 (3), pp. 241-248. Date of Electronic Publication: 2004 May 01. |
| نوع المنشور: | Journal Article |
| اللغة: | English |
| بيانات الدورية: | Publisher: International Institute of Anticancer Research Country of Publication: Greece NLM ID: 101188791 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1790-6245 (Electronic) Linking ISSN: 11096535 NLM ISO Abbreviation: Cancer Genomics Proteomics Subsets: PubMed not MEDLINE; MEDLINE |
| أسماء مطبوعة: | Original Publication: Kapandriti, Attiki, Greece : International Institute of Anticancer Research, [2004]- |
| مستخلص: | Background: The epithelial cell adhesion molecule (EpCAM) is a homophilic adhesion molecule expressed de novo on a variety of epithelial tumors. Overexpression of EpCAM results in enhanced proliferation and rapid induction of the proto-oncogene c-myc. Materials and Methods: The novel proteomics-based fluorescence difference gel electrophoresis (DIGE technology) was used to study EpCAM effects on the proteome of human epithelial cells. Results: DIGE analysis resulted in the identification of five proteins with a significantly changed regulation ranging from -1.3 to +5.8-fold. One of the identified proteins, namely glyoxalase 1, experienced a shift in the isoelectric point from pH 5.2 to 5.0 upon EpCAM expression. This shift correlated with a gain of enzymatic activity of glyoxalase 1 resulting in an enhanced methylglyoxal turnover. Conclusion: We show the potential of the DIGE technology to rapidly and quantitatively analyze proteomes for changed expression levels and, importantly, posttranslational modifications. Furthermore, we describe new targets of the carcinoma antigen EpCAM including glyoxalase1. (Copyright© 2004 International Institute of Anticaner Research (Dr. John G. Delinassios), All rights reserved.) |
| تواريخ الأحداث: | Date Created: 20190810 Latest Revision: 20190809 |
| رمز التحديث: | 20240628 |
| PMID: | 31394659 |
| قاعدة البيانات: | MEDLINE |
| تدمد: | 1790-6245 |
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