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The Ca-MOv18 molecule, a cell-surface marker of human ovarian carcinomas, is anchored to the cell membrane by phosphatidylinositol

Authors
Journal
Biochemical and Biophysical Research Communications
0006-291X
Publisher
Elsevier
Publication Date
Volume
171
Issue
3
Identifiers
DOI: 10.1016/0006-291x(90)90790-t
Disciplines
  • Biology

Abstract

Abstract The struture of the 38 kD cell surface glycoprotein identified by the monoclonal antibody MOv18 and specifically expressed by human ovarian carcinomas has been investigated at a molecular level. The ovarian carcinoma cell line IGROV-1, which expresses high levels of Ca-MOv18, was treated with the phosphatidylinositol-specific phospholipase C from B. thuringiensis. The phospholipase C specifically released most of the Ca-MOv18 molecules as shown by flow cytometric analysis of the treated cells and by radioimmunometric assays of the corresponding supernatants. Consistent with the known structure of other phosphatidylinositol-linked molecules, Ca-MOv18 was biosynthetically labeled by [ 3H]ethanolamine and the labeled molecules were immunoprecipitated from the supernatant of the phospholipase C treated cells. Evidence that Ca-MOv18 is anchored to the cell membrane via phosphatidylinositol may prove to be relevant in current investigations regarding the biological and clinical significance of this tumor marker.

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