1992
DOI: 10.1016/0003-9861(92)90093-c
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Short- and long-term effects of insulin on tyrosine aminotransferase gene expression

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Cited by 11 publications
(7 citation statements)
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“…In neonates, both PEPCK and TAT mRNA levels decrease markedly during the first 2 h of refeeding, and then remain almost constant (32). In hepatocytes exposed to insulin for a short period of time, glucocorticoid-and cAMP-induced transcription of the TAT gene is inhibited (33). The results we obtained following glucose treatment after 16 h of fasting were the same as those seen with refeeding after fasting.…”
Section: Discussionsupporting
confidence: 75%
“…In neonates, both PEPCK and TAT mRNA levels decrease markedly during the first 2 h of refeeding, and then remain almost constant (32). In hepatocytes exposed to insulin for a short period of time, glucocorticoid-and cAMP-induced transcription of the TAT gene is inhibited (33). The results we obtained following glucose treatment after 16 h of fasting were the same as those seen with refeeding after fasting.…”
Section: Discussionsupporting
confidence: 75%
“…While the control of tyrosine aminotransferase expression and activity has been extensively studied as a target of insulin signaling in vertebrates [30]–[34], [36], [38], a connection between tyrosine aminotransferase or tyrosine metabolism and insulin action has not been demonstrated. Prior work in C. elegans has suggested that the hpd-1 gene, which encodes 4-hydroxyphenylpyruvate dioxygenase, is repressed in daf-2 mutants and that knock-down of hpd-1 by RNAi delayed dauer exit and extended lifespan [39].…”
Section: Discussionmentioning
confidence: 99%
“…The IRS-like element is found in various genes, including phosphoenolpyruvate carboxykinase (PEPCK, [37]) and glucose 6-phosphatase [38] where insulin effects their transcriptional modulation. It is noteworthy that insulin may exert negative regulatory effects on the expression of various genes at both transcriptional and post-transcriptional levels [23,39,40]. In separate investigations, we have been attempting to characterize signal transduction pathways associated with insulin in primary hepatocytes.…”
Section: Discussionmentioning
confidence: 99%
“…The use of artificially high insulin levels will likely confound estimations of drug-metabolizing activity in vitro. Insulin can act as an inducer of the glucokinase [21] and pyruvate kinase genes [22] while also functioning to repress the cAMPmediated induction of tyrosine aminotransferase [23]. Saad et al [18] reported that lowered insulin concentrations or increased insulin:glucagon ratios led to a 2-3-fold elevation in functional activities associated with PB-inducible CYP proteins.…”
Section: Introductionmentioning
confidence: 99%