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Regulation of Activity Levels of Glycolipid Sulfotransferases by Transforming Growth Factor in Renal Cell Carcinoma Cells

Biochemistry and Virology Laboratory, Cancer Institute, and the Third Department of Internal Medicine, Hokkaido University School of Medicine, Sapporo, Japan

¹ To whom requests for reprints should be addressed, at Biochemistry Laboratory, Cancer Institute, Hokkaido University School of Medicine, Kita-ku N15 W7, Sapporo 060, Japan.

Accumulation of sulfolipids associated with markedly elevated levels of glycolipid sulfotransferase activities was previously demonstrated in human renal cell carcinoma cells. To explore the regulation mechanisms of sulfoglycolipid synthesis in renal cancer, effects of various growth factors on the metabolic enzymes of sulfoglycolipids were investigated by using a human renal cell carcinoma cell line, SMKT-R3. Among the growth factors tested, transforming growth factor a (TGF-) and epidermal growth factor (EGF) were found to increase the sulfotransferase activity markedly (about 300%), but did not change that of arylsulfatase A, which hydrolyzes sulfoglycolipids. The augmented effects of TGF- was abolished by cycloheximide.

Since TGF- is known to bind to the same receptor as EGF, SMKT-R3 cells were investigated for the EGF receptor by affinity cross-linking with ¹²⁵I-EGF. A radiolabeled protein with a molecular mass of 175 kDa corresponding to the ligand-receptor complex was immunoprecipitated with a monoclonal anti-EGF receptor antibody. When production of the growth factors was examined immunochemically, the cells were found to secrete TGF- at a low level and retain it in a membrane-bound form, whereas EGF was not detected. These observations suggest that the sulfotransferase activities are regulated through the autocrine, paracrine, and/or juxtacrine modes of intercellular stimulation by TGF- in human renal cancer cells.

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Received 7/12/93. Accepted 9/30/93.

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