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[Cancer Research 35, 438-441, February 1, 1975]
© 1975 American Association for Cancer Research

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A Comparison of Glycosyltransferase Activities and Malignant Properties in Normal and Transformed Cells Derived from BALB/c Mice1

Leonard M. Patt, Gary A. Van Nest and William J. Grimes

Department of Biochemistry, College of Medicine, University of Arizona, Tucson, Arizona 85724

The ability of suspensions of BALB/c cells to catalyze the incorporation of nucleotide sugars into complex polysaccharides has been compared. These cells have previously been characterized for concanavalin A-induced agglutinability, tumorigenicity, and malignancy. All of the cell lines tested catalyze transfer of the sugar moieties of cytosine 5'-monophosphate N-acetylneuraminic acid, uridine 5'-diphosphate galactose, uridine 5'-diphosphate N-acetylgalactosamine, uridine 5'-diphosphate N-acetylglucosamine, uridine 5'-diphosphate glucose, and guanidine 5'-diphosphate mannose into glycoproteins and glycolipids. While some transformed lines exhibit alterations in transferase levels, others cannot be distinguished from normal cells. Normal cells, transformed cells that cause tumors that regress, and transformed cells that cause tumors that kill an immunologically competent host show growth-dependent changes in transferase activities. Determining the ability to catalyze carbohydrate transfer is insufficient for predicting the tumorigenic and malignant properties of a cell line.

1 Supported by grants from the American Cancer Society (BC131) and the National Cancer Institute (CA12753).

Received 7/10/74. Accepted 11/ 5/74.







HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Cancer Research Clinical Cancer Research
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Molecular Cancer Research Cancer Prevention Research
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Annual Meeting Education Book Cell Growth & Differentiation
Copyright © 1975 by the American Association for Cancer Research.