Donnelly S R, Moss S E
Department of Physiology, University College London, Gower Street, London WC1E 6BT, UK.
Biochem J. 1998 Jun 15;332 ( Pt 3)(Pt 3):681-7. doi: 10.1042/bj3320681.
To gain insight into the molecular basis of annexin gene expression we have analysed the annexin I and VI gene promoters. A previously described 881 bp sequence immediately upstream of the annexin I transcription start site and a similar size fragment proximal to the annexin VI transcription start site both drove expression of the luciferase reporter gene in fibroblasts and epithelial cells. Neither promoter displayed any sensitivity to dexamethasone, suggesting that the putative glucocorticoid response element in the annexin I promoter is non-functional. Consistent with this, endogenous annexin I gene expression was unaffected by dexamethasone at the mRNA and protein levels in A431 cells. A series of 5' deletions of the two promoters were examined to define the minimal active sequences. For annexin I this corresponded to a sequence approx. 150 bp upstream of the transcription start site that included CAAT and TATA boxes. Unexpectedly, the annexin VI promoter, which also contains CAAT and TATA boxes, was fully active in the absence of these elements, a 53 bp sequence between these boxes and the transcription start site having maximal activity. Electrophoretic mobility-shift assays with nuclear extracts from A431 and HeLa cells with probes corresponding to this region revealed an SP1-binding site. These results show that the annexin I and VI genes have individual modes of transcriptional regulation and that if either annexin I or annexin VI has an anti-inflammatory role, then this is in the absence of steroid-induced gene expression.
为深入了解膜联蛋白基因表达的分子基础,我们分析了膜联蛋白I和VI基因的启动子。在膜联蛋白I转录起始位点上游先前描述的881 bp序列以及靠近膜联蛋白VI转录起始位点的类似大小片段,均能驱动荧光素酶报告基因在成纤维细胞和上皮细胞中表达。两个启动子均未表现出对地塞米松的任何敏感性,这表明膜联蛋白I启动子中假定的糖皮质激素反应元件无功能。与此一致的是,在A431细胞中,地塞米松在mRNA和蛋白质水平上均未影响内源性膜联蛋白I基因的表达。对两个启动子进行了一系列5'端缺失分析,以确定最小活性序列。对于膜联蛋白I而言,这对应于转录起始位点上游约150 bp的一段序列,该序列包含CAAT盒和TATA盒。出乎意料的是,同样含有CAAT盒和TATA盒的膜联蛋白VI启动子,在没有这些元件的情况下仍具有完全活性,这些盒与转录起始位点之间的一段53 bp序列具有最大活性。用A431和HeLa细胞核提取物与对应于该区域的探针进行电泳迁移率变动分析,揭示了一个SP1结合位点。这些结果表明,膜联蛋白I和VI基因具有各自的转录调控模式,并且如果膜联蛋白I或膜联蛋白VI具有抗炎作用,那么这种作用并非由类固醇诱导的基因表达介导。