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A viral K-RAS protein increases the stimulability of adenylate cyclase by cholera toxin in NRK cells |
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| Authors: | D J Franks J F Whitfield J P Durkin |
| Affiliation: | 1. Department of Pathology, Faculty of Health Sciences, University of Ottawa, Ottawa, Ontario, Canada K1H 8M5;2. Cellular Oncology Group, Division of Biological Sciences, National Research Council of Canada, Ottawa, Ontario, Canada K1A OR6;1. Division of Hematology, Anschutz Medical Campus, University of Colorado, Aurora, CO 80045, USA;2. Department of Biochemistry and Molecular Genetics, Anschutz Medical Campus, University of Colorado, Aurora, CO 80045, USA;3. Department of Pediatrics, Anschutz Medical Campus, University of Colorado, Aurora, CO 80045, USA;4. Genomics Research Center, University of Rochester, NY 14642, USA;5. School of Medicine, Dentistry and Biomedical Sciences, Queens University, Belfast, UK;6. Feinberg Cardiovascular and Renal Research Institute, Northwestern University School of Medicine, Chicago, IL 60611, USA |
| Abstract: | Incubation at 41 degrees C stops the proliferation of tsK-NRK rat kidney cells in serum-deficient medium by inactivating the mitogenic/oncogenic thermolabile viral K-RAS protein that is produced in these cells. Dropping the temperature to 36 degrees C reactivates the viral K-RAS protein which stimulates the serum-starved quiescent cells to resume proliferating without added serum factors. Here it is shown that while the reactivated viral protein does not by itself significantly stimulate adenylate cyclase, it greatly increases the stimulability of adenylate cyclase by cholera toxin. The data suggest that the viral K-RAS protein directly or indirectly affects adenylate cyclase by inactivating the Gi inhibitory component of the membrane associated enzyme. |
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