...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Molecular and Cellular Biology >Isolation and Functional Characterization of cDNA of Serum Amyloid A-Activating Factor That Binds to the Serum Amyloid A Promoter
【24h】

Isolation and Functional Characterization of cDNA of Serum Amyloid A-Activating Factor That Binds to the Serum Amyloid A Promoter

机译：与血清淀粉样蛋白A启动子结合的血清淀粉样蛋白A激活因子cDNA的分离和功能鉴定

获取原文
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Serum amyloid A (SAA), a plasma protein inducible in response to many inflammatory conditions, is associated with the pathogenesis of several diseases including reactive amyloidosis, rheumatoid arthritis, and atherosclerosis. We have previously reported an element of the SAA promoter, designated SAA-activating sequence (SAS), that is involved in the inflammation-induced SAA expression, and a nuclear factor, SAS-binding factor (SAF), that interacts with the SAS element has been identified previously (A. Ray and B. K. Ray, Mol. Cell. Biol. 16:1584–1594, 1996). To evaluate how SAF is involved in SAA promoter activation, we have investigated structural features and functional characteristics of this transcription factor. Our studies indicate that SAF belongs to a family of transcription factors characterized by the presence of multiple zinc finger motifs of the Cys2-His2 type at the carboxyl end. Of the three cloned SAF cDNAs (SAF-1, SAF-5, and SAF-8), SAF-1 isoform showed a high degree of homology to MAZ/ZF87/Pur-1 protein while SAF-5 and SAF-8 isoforms are unique and are related to SAF-1/MAZ/ZF87/Pur-1 at the zinc finger domains but different elsewhere. Although structurally distinct, all members are capable of activating SAS element-mediated expression and display virtually identical sequence specificities. However, varying levels of expression of members of this gene family were observed in different tissues. Functional activity of SAF is regulated by a posttranslational event as SAF DNA-binding and transactivation abilities are increased by a protein phosphatase inhibitor, okadaic acid, and inhibited by a protein kinase inhibitor, H7. Consistent with this observation, increased DNA binding of the cloned SAF and its hyperphosphorylation, in response to okadaic acid treatment of the transfected cells, were observed. Taken together, our results suggest that, in addition to tissue-specific expression, SAFs, a family of zinc finger transcription factors, undergo a modification by a posttranslational event that confers their SAA promoter-binding activity and transactivation potential.
机译：血清淀粉样蛋白A（SAA）是一种可响应多种炎症状况而诱导的血浆蛋白，与多种疾病的发病机理有关，包括反应性淀粉样变性，类风湿性关节炎和动脉粥样硬化。我们先前已经报道了SAA启动子的一个元素，称为SAA激活序列（SAS），它参与炎症诱导的SAA表达，而一个核因子SAS结合因子（SAF），与SAS元素相互作用以前已经被鉴定过（A. Ray and BK Ray，Mol。Cell。Biol。16：1584-1594，1996）。为了评估SAF如何参与SAA启动子激活，我们研究了该转录因子的结构特征和功能特征。我们的研究表明，SAF属于转录因子家族，其特征是在羧基末端存在Cys 2 -His 2 类型的多个锌指基序。在三个克隆的SAF cDNA（SAF-1，SAF-5和SAF-8）中，SAF-1同工型与MAZ / ZF87 / Pur-1蛋白具有高度同源性，而SAF-5和SAF-8同工型是独特，与锌指结构域的SAF-1 / MAZ / ZF87 / Pur-1有关，但在其他地方有所不同。尽管结构上不同，但是所有成员都能够激活SAS元素介导的表达并显示出几乎相同的序列特异性。但是，在不同组织中观察到该基因家族成员表达水平的变化。 SAF的功能活性受翻译后事件的调节，因为SAF的DNA结合和反式激活能力被蛋白磷酸酶抑制剂冈田酸提高，而被蛋白激酶抑制剂H7抑制。与该观察结果一致，观察到响应冈田酸处理转染细胞，克隆的SAF的DNA结合增加及其超磷酸化。综上所述，我们的结果表明，除组织特异性表达外，SAF（锌指转录因子家族）还受到翻译后事件的修饰，赋予其SAA启动子结合活性和反式激活潜能。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号