FASEB J.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Hull, S. R.
Right arrow Articles by Carraway, K. L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hull, S. R.
Right arrow Articles by Carraway, K. L.

The FASEB Journal, Vol 2, 2380-2384, Copyright © 1988 by The Federation of American Societies for Experimental Biology

RESEARCH COMMUNICATIONS

Mechanism of expression of Thomsen-Friedenreich (T) antigen at the cell surface of a mammary adenocarcinoma

SR Hull and KL Carraway
Department of Anatomy and Cell Biology, University of Miami School of Medicine, Florida 33101.

The Thomsen-Friedenreich (T) antigen and its disaccharide component Gal beta 1,3GalNAc, which is recognized by the plant lectin peanut agglutinin (PNA), have been proposed as useful tumor markers because of their apparently specific occurrence in certain types of carcinomas. We have investigated the mechanism for the appearance of the disaccharide at the cell surface of ascites 13762 rat mammary adenocarcinoma cells using pulse-chase glucosamine labeling, proteolysis, and PNA precipitation of the cell-surface sialomucin ASGP-1. Glucosamine- labeled disaccharide appears at the cell surface in less than 10 min. Although the appearance of larger oligosaccharides continues to increase, the appearance of labeled disaccharide levels off within an hour. Analysis of intracellular vs. cell surface-labeled oligosaccharides showed that all disaccharide synthesized more than an hour before reaching the cell surface is converted to larger oligosaccharides. Thus, the presence of the disaccharide at the cell surface results from its synthesis late in the transit pathway of the sialomucin to the cell surface. We propose that the presence of T antigen at the surface of carcinoma cells results from an aberration of the pathway for O-linked glycosylation in these cells, probably caused by inappropriate localization of the enzymes involved in synthesis of the disaccharide.


This article has been cited by other articles:


Home page
 J. Exp. Med.Home page
Y. Xu, S. J. Gendler, and A. Franco
Designer Glycopeptides for Cytotoxic T Cell-based Elimination of Carcinomas
J. Exp. Med., March 1, 2004; 199(5): 707 - 716.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1988 by The Federation of American Societies for Experimental Biology.