| Autor: |
Yellaturu CR; Department of Veterans Affairs Medical Center, Memphis, TN, USA., Deng X, Cagen LM, Wilcox HG, Park EA, Raghow R, Elam MB |
| Jazyk: |
angličtina |
| Zdroj: |
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2005 Jun 24; Vol. 332 (1), pp. 174-80. |
| DOI: |
10.1016/j.bbrc.2005.04.112 |
| Abstrakt: |
Insulin and cAMP have opposing effects on de novo fatty acid synthesis in liver and in cultured hepatocytes mediated by sterol-regulatory element binding protein (SREBP). To determine whether these agents regulate the cleavage of full-length SREBP to generate the transcriptionally active N-terminal fragment (nSREBP) in primary rat hepatocytes, an adenoviral vector (Ad-SREBP-1a) was constructed to constitutively express full-length SREBP-1a. Insulin increased, and dibutyryl (db)-cAMP inhibited, generation of nSREBP-1a from its full-length precursor. Insulin stimulated processing of SREBP-1a within 1h, and the effect was sustained for at least 24h. The initial stimulation of SREBP processing by insulin preceded measurable reduction in Insig-2 mRNA levels. Rat hepatocytes were also infected with an adenovirus expressing the nuclear form of SREBP-1c (Ad-nSREBP-1c). Insulin increased the half-life of constitutively expressed nSREBP-1c, and this effect of insulin was also inhibited by db-cAMP. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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