Tae H J, Zhang S, Kim K H
Department of Biochemistry, Purdue University, West Lafayette, Indiana 47907, USA.
J Biol Chem. 1995 Sep 15;270(37):21487-94. doi: 10.1074/jbc.270.37.21487.
The acetyl-CoA carboxylase (ACC) gene contains two distinct promoters, denoted PI and PII. PI is responsible for the generation of class I ACC mRNAs which are induced in a tissue-specific manner under lipogenic conditions. PII generates class II ACC mRNAs which are expressed constitutively. During 30A5 preadipocyte differentiation, both promoters are activated; the preadipocytes must be pretreated with cAMP for this activation to occur. In this report, we present evidence that CAAT enhancer-binding protein-beta (C/EBP-beta) is induced and involved in the PI activation by cAMP. Expression of the reporter gene under the control of the PI promoter is activated within 3 h after treatment of 30A5 cells with a cyclic AMP analogue, 8-(4-chlorophenylthio)-adenosine 3',5'-cyclic monophosphate, and 3-isobutyl-1-methylxanthine, in association with the accumulation of C/EBP-beta mRNA and protein. These accumulations were inhibited in the presence of H8, a protein kinase inhibitor; H8 also inhibited activation of PI by cAMP. However, the induction of reporter gene expression and the increase of C/EBP-beta mRNA by cAMP were not affected by treatment with tumor necrosis factor alpha, which completely inhibited the accumulation of C/EBP-alpha mRNA. Overexpression of C/EBP-beta by transfection with the C/EBP-beta gene led to increased binding of C/EBP-beta to DNA and partial PI activation. cAMP did not affect the amount of C/EBP-beta binding to the DNA but did promote phosphorylation of C/EBP-beta and PI activation. As in the case of C/EBP-alpha, C/EBP-beta bound to the CCAAT box of the PI promoter. These results indicate that cAMP not only induces, but also activates, bound C/EBP-beta through phosphorylation for PI activation. Our studies also indicate that cAMP induces C/EBP-alpha. C/EBP-beta induction, however, precedes that of C/EBP-alpha.
乙酰辅酶A羧化酶(ACC)基因包含两个不同的启动子,分别为PI和PII。PI负责生成I类ACC mRNA,其在脂肪生成条件下以组织特异性方式被诱导。PII生成II类ACC mRNA,其组成性表达。在30A5前脂肪细胞分化过程中,两个启动子均被激活;前脂肪细胞必须用cAMP预处理才能发生这种激活。在本报告中,我们提供证据表明CCAAT增强子结合蛋白β(C/EBP-β)被诱导并参与cAMP介导的PI激活。在用环磷酸腺苷类似物8-(4-氯苯硫基)-腺苷3',5'-环一磷酸和3-异丁基-1-甲基黄嘌呤处理30A5细胞后3小时内,PI启动子控制下的报告基因表达被激活,同时伴有C/EBP-β mRNA和蛋白质的积累。在蛋白激酶抑制剂H8存在的情况下,这些积累受到抑制;H8也抑制cAMP对PI的激活。然而,cAMP诱导的报告基因表达和C/EBP-β mRNA的增加不受肿瘤坏死因子α处理的影响,肿瘤坏死因子α完全抑制C/EBP-α mRNA的积累。通过转染C/EBP-β基因过表达C/EBP-β导致C/EBP-β与DNA的结合增加以及PI的部分激活。cAMP不影响C/EBP-β与DNA的结合量,但确实促进C/EBP-β的磷酸化和PI的激活。与C/EBP-α的情况一样,C/EBP-β与PI启动子的CCAAT框结合。这些结果表明,cAMP不仅诱导,而且通过磷酸化激活结合的C/EBP-β以实现PI的激活。我们的研究还表明,cAMP诱导C/EBP-α。然而,C/EBP-β的诱导先于C/EBP-α。