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Involvement of Ras in the expression of glycolipid sulfotransferase in human renal cancer cells
Author(s) -
Yabunaka Norijuki,
Honke Koichi,
Ishii Atsushi,
Ogiso Yoshifumi,
Kuzumaki Noboru,
Agishi Yuko,
Makita Akira
Publication year - 1997
Publication title -
international journal of cancer
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.475
H-Index - 234
eISSN - 1097-0215
pISSN - 0020-7136
DOI - 10.1002/(sici)1097-0215(19970516)71:4<620::aid-ijc18>3.0.co;2-f
Subject(s) - sulfotransferase , signal transduction , glycolipid , tyrosine kinase , epidermal growth factor , biology , cell culture , cancer cell , tyrosine , receptor tyrosine kinase , receptor , endocrinology , microbiology and biotechnology , biochemistry , cancer , sulfation , genetics
Abstract Glycolipid sulfotransferase activity in a human renal cell carcinoma cell line, SMKT‐R3, is enhanced by epidermal growth factor (EGF); tyrosine kinase inhibitors suppress this enhancement. To investigate the involvement of Ras in the signal transduction pathway from the EGF receptor to the expression of glycolipid sulfotransferase, we introduced v‐H‐ras into SMKT‐R3 cells. In a quiescent state, the percent GTP bound to Ras in v‐H‐ras‐expressing cells increased about 2.5‐fold compared with control cells, suggesting that v‐Ras introduced into the renal cancer cells is in an active form without EGF stimulation. Glycolipid sulfotransferase activity in v‐H‐ras‐expressing cells was higher than in control cells. The sulfotransferase activity was affected neither by EGF nor by genistein, a tyrosine kinase inhibitor, in v‐H‐ras‐expressing cells, whereas it was enhanced by EGF and reduced by genistein in control cells. Our observations suggest that Ras mediates the regulation pathway of glycolipid sulfotransferase activity in SMKT‐R3 cells. Int. J. Cancer 71:620‐623, 1997. © 1997 Wiley‐Liss, Inc.