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2. rasoncogene‐induced transformation of a rat seminal vesicle epithelial cell line produces a marked increase of adenylate cyclase and protein kinase C activities

Author

Spina, A.M., Chiosi, E., Naviglio, S., Valente, F., Marchese, M., Furgi, A., Metafora, S., and Illiano, G.

Abstract

Cells transformed by Kirsten murine sarcoma virus (Ki‐MSV) have basal adenylate cyclase activity (AC) higher than control cells and comparable level of forskolin‐stimulated AC activity. Moreover, a higher protein kinase C (PKC) activity was found to be present in the transformed cells. The molecular mechanism underlying the increase of AC activity was investigated. Our findings strongly suggest that this biochemical event is due to a marked decrease of the αinegative control of the enzyme, even though the αiof transformed cells appears to possess fully functional domains interacting with both the effector enzyme and the agonist‐activated receptor.

Published
1993
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3. rasoncogene-induced transformation of a rat seminal vesicle epithelial cell line produces a marked increase of adenylate cyclase and protein kinase C activities

Author

A. Furgi, Emilio Chiosi, Magda Marchese, F. Valente, Annamaria Spina, Silvio Naviglio, G. Illiano, Salvatore Metafora, Spina, Annamaria, Chiosi, Emilio, Naviglio, Silvio, Valente, F, Marchese, M, Furgi, A, Metafora, S, and Illiano, G.

Subjects
Male, G-protein, G protein, Biophysics, ras oncogene, Adenylate kinase, Biology, Biochemistry, Cyclase, Epithelium, GTP-Binding Proteins, Protein kinase C, Structural Biology, Genetics, Animals, Adenylate cyclase, Virulence Factors, Bordetella, Receptor, Molecular Biology, Adenosine Diphosphate Ribose, Oncogene, Effector, Colforsin, Seminal Vesicles, Epithelial Cells, Cell Biology, Cell Transformation, Viral, Rats, Cell biology, Enzyme Activation, Genes, ras, Cell transformation, Adenylate Cyclase Toxin, Cyclase activity, Adenylyl Cyclases, Signal Transduction
Abstract

Cells transformed by Kirsten murine sarcoma virus (Ki-MSV) have basal adenylate cyclase activity (AC) higher than control cells and comparable level of forskolin-stimulated AC activity. Moreover, a higher protein kinase C (PKC) activity was found to be present in the transformed cells. The molecular mechanism underlying the increase of AC activity was investigated. Our findings strongly suggest that this biochemical event is due to a marked decrease of the α i negative control of the enzyme, even though the α i of transformed cells appears to possess fully functional domains interacting with both the effector enzyme and the agonist-activated receptor.

Published
1993

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