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Epidermal growth factor inhibits phosphoenolpyruvate carboxykinase gene expression in rat hepatocytes in primary culture
Author(s) -
Fillat Cristina,
Valera Alfons,
Bosch Fatima
Publication year - 1993
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(93)80530-8
Subject(s) - phosphoenolpyruvate carboxykinase , epidermal growth factor , tyrosine aminotransferase , endocrinology , gtp' , medicine , gene expression , tyrosine kinase , hepatocyte , biology , cell culture , microbiology and biotechnology , protein kinase c , chemistry , kinase , signal transduction , gene , biochemistry , enzyme , in vitro , enzyme inducer , genetics
Epidermal growth factor (EGF) decreased the basal, and blocked the dibutyryl cyclic AMP (Bt 2 cAMP)‐induced, expression of P‐enolpyruvate carboxykinase (GTP) (PEPCK) and tyrosine aminotransferase (TAT) genes in both rat hepatocytes in primary culture and the FTO‐2B hepatoma cell line. Treatment of hepatocytes with EGF in combination with phorbol ester (TPA) resulted in an additive decrease of PEPCK mRNA levels. Overnight pretreatment of hepatocytes with TPA, which is known to downregulate protein kinase C, abolished the TPA and reduced the EGF‐mediated inhibition of PEPCK gene expression. These results suggested that EGF caused its effect, at least in part, through protein kinase C.