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Adenylate cyclase activity of ν‐ ras ‐ k transformed rat epithelial thyroid cells
Author(s) -
Colletta Giulia,
Corda Daniela,
Schettini Gennaro,
Cirafici Anna Maria,
Kohn Leonard D.,
Consiglio Eduardo
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80579-9
Subject(s) - cyclase , adenylate kinase , cholera toxin , forskolin , pertussis toxin , medicine , endocrinology , growth hormone releasing hormone receptor , cell culture , gtp' , adcy9 , biology , chemistry , microbiology and biotechnology , g protein , biochemistry , receptor , enzyme , hormone receptor , stimulation , genetics , cancer , breast cancer
The regulation of adenylate cyclase has been analyzed in normal rat thyroid cells as well as in the same cells transformed by the ν‐ ras ‐ k oncogene. In both cell types the adenylate cyclase complex consists of the two GTP‐binding proteins, G i and G s , as demonstrated by the specific ADP‐ribosylation induced by pertussis and cholera toxin, respectively. The response of adenylate cyclase of the transformed cells to forskolin, pertussis toxin and cholera toxin is attenuated with respect to the control cell line. The thyrotropic hormone (TSH), that acts on normal thyroid cells in culture as a growth factor by stimulating the adenylate cyclase activity, is not able to induce DNA synthesis nor does it stimulate adenylate cyclase in ν‐ ras ‐ k transformed cells.