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热休克蛋白70激动剂SW02对脂多糖诱导的巨噬细胞iNOS表达的调控及机制

花慧莲 黄超

中国药理学通报Issue(2):279-284,6.
中国药理学通报Issue(2):279-284,6.DOI:10.3969/j.issn.1001-1978.2016.02.025

热休克蛋白70激动剂SW02对脂多糖诱导的巨噬细胞iNOS表达的调控及机制

Effects of heat shock protein 70 activator SW02 on lipopolysaccharide-induced expression of inducible nitric oxide synthase in macrophages

花慧莲 1黄超2

作者信息

  • 1. 泰州市人民医院药学部,江苏 泰州 225300
  • 2. 南通大学药学院药理学系,江苏 南通 226001
  • 折叠

摘要

Abstract

Aim To observe the effects of heat shock protein 70 ( Hsp70 ) activator SW02 on lipopolysaccha-ride( LPS)-induced expression of inducible nitric oxide synthase ( iNOS ) and LPS-induced production of nitric oxide ( NO ) in macrophages. Methods RAW264. 7 cells were stimulated by LPS, and were divided into DMSO,DMSO+LPS(1 mg·L-1),SW02,and SW02+LPS ( 1 mg · L-1 ) groups. The protein expression was detected by Western blot. NO concentration was measured by Griess kit. The iNOS mRNA was detected by real-time PCR. The NF-κB binding to iNOS promot-ers was measured by chromatin immunoprecipitation ( ChIP ) assays. Results SW02 significantly blocked the protein and mRNA expression of iNOS as well as the production of NO in LPS-stimulated RAW264 . 7 cells(P<0. 01 or P<0. 05,SW02+LPS group vs DM-SO+LPS group) . SW02 did not affect the LPS-induced degradation of IκB-α( P>0. 05 , SW02 +LPS group vs DMSO+LPS group ) and nuclear translocation of NF-κB ( P > 0. 05 , SW02 + LPS group vs DMSO + LPS group) . However,SW02 reduced the NF-κB binding to iNOS promoters inside the cell( P<0. 05,SW02+LPS group vs DMSO+LPS group) . Conclusion These re-sults show that SW02 prevents iNOS expression and NO induction likely through attenuation of the NF-κB bind-ing to iNOS promoters in macrophages.

关键词

SW02/热休克蛋白70/脂多糖/诱导型一氧化氮合酶/RAW264. 7细胞/核因子κB/κB-α抑制子

Key words

SW02/Hsp70/LPS/iNOS/RAW264 . 7 cells/NF-κB/IκB-α

分类

医药卫生

引用本文复制引用

花慧莲,黄超..热休克蛋白70激动剂SW02对脂多糖诱导的巨噬细胞iNOS表达的调控及机制[J].中国药理学通报,2016,(2):279-284,6.

基金项目

国家自然科学基金资助项目( No 81102428) ( No 81102428)

江苏省自然科学基金面上项目(No BK20141240) (No BK20141240)

中国药理学通报

OA北大核心CSCDCSTPCD

1001-1978

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