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  • Title: Tumor-promoting phorbol ester induces alterations of sialidase and sialyltransferase activities of JB6 cells.
    Author: Miyagi T, Sagawa J, Kuroki T, Matsuya Y, Tsuiki S.
    Journal: Jpn J Cancer Res; 1990 Dec; 81(12):1286-92. PubMed ID: 2125997.
    Abstract:
    Sialidase and sialyltransferase activities were studied in JB6 mouse epidermal cells before and after exposure to phorbol ester, 12-O-tetradecanoyl phorbol-13-acetate (TPA), which irreversibly induces anchorage-independent growth and tumorigenicity. JB6 cells exhibited sialidase activities toward 4-methylumbelliferyl-alpha-D-N-acetylneuraminic acid (4MU-NeuAc) and gangliosides at pH 4.5 in the particulate fraction but apparently not in the cytosol at pH 4.5 or 6.0. In JB6 cells exposed to TPA and in the anchorage-independent transformants, the sialidase activity toward 4MU-NeuAc was decreased and the activity toward gangliosides was increased compared with those in untreated JB6 cells. Immunological analysis with antisera against membrane-associated sialidases I and II revealed that plasma membrane-associated sialidase I was increased and lysosomal membrane-associated sialidase II was decreased under these conditions. TPA treatment also affected the sialyltransferase activities of JB6 cells: and elevation of the transfer activities toward asialo-orosomucoid and asialo-porcine submaxillary mucin but a reduction of GM3 and GD3 synthase activities were observed on exposure to TPA and in cells transformed by TPA to retain anchorage-independency. These results suggest that an increase in sialic acid bound to glycoproteins and a decrease in that bound to glycolipids may occur in JB6 cells exposed to TPA and in the anchorage-independent transformants.
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