...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Journal of Leukocyte Biology: An Official Publication of the Reticuloendothelial Society >Regulation of class A scavenger receptor-mediated cell adhesion and surface localization by PI3K: identification of a regulatory cytoplasmic motif.
【24h】

Regulation of class A scavenger receptor-mediated cell adhesion and surface localization by PI3K: identification of a regulatory cytoplasmic motif.

机译：PI3K对A类清道夫受体介导的细胞粘附和表面定位的调节：调节性细胞质基序的鉴定。

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

The importance of cytoplasmic motifs in differentially regulating SR-A function was demonstrated by deleting the first 49 cytoplasmic aa (SR-A(Delta1-49)), which abolished SR-A-mediated ligand internalization without reducing cell adhesion. To identify additional cytoplasmic motifs within the first 49 aa that regulate SR-A function, the acidic residues in a conserved motif (EDAD) were changed to their amide derivatives (SR-A(QNAN)). The function and regulation of SR-A(QNAN) were compared with that of SR-A(Delta1-49) and SR-A in transfected HEK-293 cells. Blocking PI3K activation inhibited SR-A, but not SR-A(Delta1-49)- or SR-A(QNAN)-mediated cell adhesion. Although deleting (SR-A(Delta1-49)) or mutating (SR-A(QNAN)) the EDAD motif abolished the PI3K sensitivity of SR-A-mediated cell adhesion, these mutations did not affect ligand internalization or PI3K activation during cell adhesion. To define the mechanism by which PI3K regulates SR-A-mediated cell adhesion, the cellular localization of wild-type and mutant SR-A was examined. PI3K inhibition reduced surface localization of SR-A but not of SR-A(Delta1-49) or SR-A(QNAN). The regulation of SR-A surface localization by PI3K was confirmed in peritoneal macrophages, which endogenously express SR-A. Together, these results suggest a pathway in which SR-A binding to an immobilized ligand activates PI3K to recruit more receptor to the plasma membrane and enhances cell adhesion.
机译：通过删除前49个胞质氨基酸（SR-A（Delta1-49）），证明了胞质基序在差异调节SR-A功能中的重要性，该氨基酸取消了SR-A介导的配体内化作用，而没有降低细胞粘附。为了确定前49个氨基酸中调节SR-A功能的其他胞质基序，将保守基序（EDAD）中的酸性残基更改为其酰胺衍生物（SR-A（QNAN））。比较了转染的HEK-293细胞中SR-A（QNAN）与SR-A（Delta1-49）和SR-A的功能和调控。阻止PI3K激活抑制SR-A，但不抑制SR-A（Delta1-49）-或SR-A（QNAN）介导的细胞粘附。尽管删除（SR-A（Delta1-49））或突变（SR-A（QNAN））EDAD基序消除了SR-A介导的细胞粘附的PI3K敏感性，但这些突变并不影响配体内在化或PI3K活化附着力。为了定义PI3K调节SR-A介导的细胞粘附的机制，研究了野生型和突变SR-A的细胞定位。 PI3K抑制降低了SR-A的表面定位，但没有降低SR-A（Delta1-49）或SR-A（QNAN）的表面定位。在内源性表达SR-A的腹膜巨噬细胞中证实了PI3K对SR-A表面定位的调节。在一起，这些结果表明了一条途径，其中SR-A与固定的配体结合会激活PI3K，以招募更多的质膜受体并增强细胞粘附。

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