gms | German Medical Science

27th German Cancer Congress Berlin 2006

German Cancer Society (Frankfurt/M.)

22. - 26.03.2006, Berlin

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Expression of glycodelin in human ovarian cancer: immunohistochemistry and possible function

Meeting Abstract

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  • corresponding author presenting/speaker Udo Jeschke - I. Frauenklinik der LMU München, Deutschland
  • Christiane Kunert-Keil - Institut für Pathophysiologie der EMAU Greifswald
  • Renate Stahn - Glycotope GmbH Berlin
  • Christoph Scholz - I. Frauenklinik der LMU München
  • Lan Schumacher - I. Frauenklinik der LMU München
  • Wolfgang Janni - I. Frauenklinik der LMU München
  • Ioannis Mylonas - I. Frauenklinik der LMU München
  • Eike Schröder - Institut für Pathologie der EMAU Greifswald
  • Christina Kuhn - I. Frauenklinik der LMU München
  • Doris Mayr - Institut für Pathologie der LMU München
  • Volker Briese - Frauenklinik der Uni. Rostock
  • Klaus Friese - I. Frauenklinik der LMU München

27. Deutscher Krebskongress. Berlin, 22.-26.03.2006. Düsseldorf, Köln: German Medical Science; 2006. DocPO353

The electronic version of this article is the complete one and can be found online at: http://www.egms.de/en/meetings/dkk2006/06dkk463.shtml

Published: March 20, 2006

© 2006 Jeschke et al.
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Outline

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Glycodelin A (GdA) is primarily produced in endometrial and decidual tissue, although it was also demonstrated in several cancer types, including ovarian serous cancer. GdA acts as a T-cell inhibitor and is involved in inactivation of human monocytes. With a new polyclonal anti-glycodelin antibody, derived from the sequence of human glycodelin and in situ hybridization experiments, the expression of glycodelin in serous, mucinous, endometrioid and clear cell ovarian tumors was demonstrated. A positive immunohistochemical reaction in all forms of epithelium ovarian cancer was observed, which was confirmed by in situ hybridization. Glycodelin is also expressed by granulose cell tumors, a non epithelial form of ovarian cancer. Furthermore, glycodelin was purified from ascites fluid of ovarian cancer patients and from supernatants of the ovarian cancer cell line ovcar-3. Ascites Gd and also ovcar Gd showed differences in its structure of sialyl Lewis type oligosaccharides compared to GdA. Additionally, ascites Gd was demonstrated to be a sufficient inhibitor of the E-selectin mediated HepG2-cell adhesion on immobilized E-selectin with a 102 fold higher potency compared to the monovalent tetrasaccharide sialyl Lewis X but with lower inhibitor potency compared to GdA and serum glycodelin. Another functional assay showed that ascites Gd inhibits IL-2 stimulated proliferation of peripheral blood leucocytes. Therefore, glycodelin could act as an inhibitor of lymphocyte activation and adhesion in ovarian cancer.