Posttranscriptional control of tyrosine aminotransferase synthesis by insulin.
نویسندگان
چکیده
Adrenal steroid hormones induce the synthesis of tyrosine amino-transferase (TAT) in HTC cells, an established line of rat hepatoma cells in tissue culture. The addition of insulin to cells previously induced in a serum-free medium results in a rapid two- to threefold further increase in the rate of synthesis of TAT and a small increase in total amino acid incorporation. These changes do not require concomitant RNA synthesis, suggesting that insulin acts at a step in protein synthesis beyond that of gene transcription. Although the effects of insulin on HTC cells are similar to those caused by dialyzed bovine serum, evidence is presented that insulin and serum affect different aspects of TAT synthesis. Unlike the glucocorticoids, insulin does not cause the accumulation of TAT mRNA, nor the sustained induction of TAT. The continued presence of the inducing steroid is required to permit maximal expression of the insulin effect.
منابع مشابه
Induction of tyrosine aminotransferase by dexamethasone, insulin, and serum. Characterization of the induced enzyme.
Dexamethasone induces the synthesis of tyrosine aminotransferase in hepatoma tissue culture (HTC) cells, an established line of rat hepatoma cells in tissue culture. The addition of insulin or dialyzed serum to cells previously induced with dexamethasone in a serum-free medium causes a further doubling in tyrosine aminotransferase activity, which is not dependent on concomitant RNA synthesis. T...
متن کاملInsulin selectively slows the degradation rate of tyrosine aminotransferase.
Glucocorticoids induce a selective 5to lo-fold increase in the rate of synthesis of tyrosine aminotransferase in rat hepatoma cells in tissue culture. Addition of insulin to steroid-induced cells stimulates a further 2to 3-fold increase in the cellular concentration of this enzyme. The induction by insulin occurs after a lag of only 6 min and does not require concomitant RNA synthesis. Insulin ...
متن کاملEffects of cyclic AMP, glucocorticoids and insulin on the activities of phosphatidate phosphohydrolase, tyrosine aminotransferase and glycerol kinase in isolated rat hepatocytes in relation to the control of triacylglycerol synthesis and gluconeogenesis.
Rat hepatocytes were incubated in monolayer culture in modified Leibovitz L-15 medium containing either 10% (v/v) newborn-calf serum or 0.2% (w/v) fatty-acid-poor bovine serum albumin. The addition of 100 nM-dexamethasone increased the activities of both phosphatidate phosphohydrolase and tyrosine aminotransferase by about 3.5-fold after 8h, and these activities continued to rise until at least...
متن کاملRegulation of Tyrosine Aminotransferase Activity in Two Liver-derived Permanent Cell Lines
The regulation of tyrosine aminotransferase (TAT) activity has been examined in two liver-derived heteroploid cell lines. One (hepatoma tissue culture cells [HTC]) was derived from a hepatoma, the other (rat liver culture cells [RLC]) was derived from normal liver. The two cell lines show the following striking similarities in the control of this specific protein: (a) The kinetics of TAT induct...
متن کاملRat hepatoma cell variants resistant to insulin-diphtheria toxin A fragment conjugates. Genetic evidence for the separate pathways for insulin receptor-mediated mitogenic and hormonal stimulation.
The rat hepatoma H35 cells in serum-free medium produce tyrosine aminotransferase (TAT) and initiate DNA synthesis and cell division upon exposure to 10(-9)-10(-10) M insulin. This insulin-dependent hormonal and mitogenic stimulation is through the insulin receptors and not through the receptors for insulin-like growth factor type I. We have isolated genetic variants of H35 cells which are resi...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Proceedings of the National Academy of Sciences of the United States of America
دوره 66 2 شماره
صفحات -
تاریخ انتشار 1970