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Effect of Retinoic Acid and Phorbol-12-myristate-13-acetate on Glycosyltransferase Activities in Normal and Transformed Cells¹

Laboratory of Cell Biology, National Institute of Mental Health, Bethesda, Maryland 20892 [J. R. M.]; Union Carbide Corporation, Sisterville, West Virginia 26175 [M. W. L.]; Cancer Research Laboratory, Southern California Cancer Center, Los Angeles, California 90015 [C. C. M.]; Department of Pediatrics and Human Development, College of Human Medicine, Michigan State University, East Lansing, Michigan 48824 [J. E. T.]; and Department of Biochemistry, Michigan State University, East Lansing, Michigan 48824 [C. C. S.]

Retinoic acid was found to increase the activity of cytidine monophosphosialic acid:lactosylceramide sialyltransferase activity in a nontransformed clonal hamster cell line, NIL 8, and a virally transformed clone, NIL 8-HSV. The potent tumor promoter phorbol-12-myristate-13-acetate (PMA) had no significant effect on sialyltransferase activity in NIL 8 cells but stimulated this activity almost 6-fold when added to NIL 8-HSV cells. There was a synergistically additive effect on sialyltransferase activity when PMA was added to NIL 8 cells in concert with retinoic acid. On the other hand neither PMA nor retinoic acid had an appreciable effect on two other glycosyltransferases measured, uridine diphospho-N-acetylgalactosamine:globotriaosylceramide N-acetylgalactosaminyl-transferase and uridine diphosphogalactose:asialoagalactofetuin galactosyltransferase. Examination of sialyltransferase activity in a human epidermoid carcinoma cell line showed a large increase in enzyme activity in response to retinoic acid administration. Two nontransformed hamster cell lines had less basal sialyltransferase activity but also showed marked elevations after retinoic acid treatment. It is proposed that one of the molecular mechanisms underlying the biological effects of retinoic acid and PMA may be an increase in sialyltransferase activity. Possible regulatory mechanisms are discussed.

¹ This work was supported by a grant from the NIH (AM 12434) to C. C. S.

² To whom requests for reprints should be addressed, at Department of Neurosurgery and Neuroscience, Albert Einstein College of Medicine, Montefiore Medical Center, Broxn, NY 10467.

Received 7/29/86. Revised 10/20/86. Accepted 10/23/86.

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