相关实验视频

Updated: May 2, 2026

Modifications of the Langendorff Method for Simultaneous Isolation of Atrial and Ventricular Myocytes from Adult Mice

Modifications of the Langendorff Method for Simultaneous Isolation of Atrial and Ventricular Myocytes from Adult Mice

Published on: May 13, 2021

拜卡莱因通过抑制JAK-STAT1/4信号通路来缓解EAM小鼠中的心肌细胞死亡

Tiantian Wang¹, Shuang Wang², Xihui Jia²

¹Department of Human Anatomy, Histology and Embryology, School of Basic Medical, Qingdao University, 308 Ningxia Road, Qingdao, Shandong 266071, China.

Phytomedicine : international journal of phytotherapy and phytopharmacology

|March 28, 2024

概括

拜卡林 (BAI) 通过向JAK-STAT1/4通路,抑制实验性自身免疫心肌炎 (EAM) 中的M1巨分化和Th1细胞分化. 这减少了促炎性细胞因子,保护心脏细胞免受亡.

科学领域:

免疫学免疫学免疫学
心血管研究研究心血管研究
药理学药理学是指药理学的学科.

背景情况:

实验性自身免疫性心肌炎 (EAM) 病原发生涉及M1巨细胞和CD4+ T细胞.
拜卡莱因 (BAI) 是一种来自Scutellaria baicalensis的黄类化合物,具有抗炎和抗氧化特性.
在EAM中BAI的治疗潜力需要进一步调查.

研究的目的:

研究BAI对M1巨分化和Th1细胞分化的抑制作用.
为了确定BAI是否调节JAK-STAT1/4信号通路.
评估BAI对促炎性细胞因子分泌和心肌细胞亡在EAM中的影响.

主要方法:

使用了流细胞计,免疫光学,qPCR和西部涂抹.
在体内和体外评估BAI对M1/Th1极化和JAK-STAT1/4通路的影响.
在EAM小鼠中测量了TNF-α,IFN-γ水平和心肌细胞亡.

主要成果:

BAI干预减少了炎症透和M1巨细胞两极分化.
BAI抑制了JAK-STAT1信号传递,降低了TNF-α的分泌.
BAI抑制了CD4+T细胞分化成Th1细胞,减少IFN-γ分泌和心肌细胞亡.

结论:

BAI通过抑制JAK-STAT1/4通路来缓解EAM中M1/Th1介导的心肌细胞死亡.
BAI通过减少炎症和亡来证明自身免疫性心肌炎的治疗潜力.

关键词:

贝尔 (BAI) 是一个国际酒店.在EAMAM中,EAMAM是EAM.M1类型的巨细胞.肌细胞死亡肌细胞死亡在 Th1 细胞中.

更多相关视频

Mouse Electroacupuncture Fixation Device Fabrication for Electroacupuncture Pretreatment in Diabetic Cardiomyopathy Mouse Model

Mouse Electroacupuncture Fixation Device Fabrication for Electroacupuncture Pretreatment in Diabetic Cardiomyopathy Mouse Model

Published on: April 18, 2025

Evaluating Cell Death Signaling by Immunofluorescence in a Rat Model of Ischemic Stroke

Evaluating Cell Death Signaling by Immunofluorescence in a Rat Model of Ischemic Stroke

Published on: January 3, 2025

相关概念视频

The JAK-STAT Signaling Pathway

The JAK-STAT Signaling Pathway

Several cytokine receptors have tightly bound Janus kinase or JAK proteins attached at their cytosolic tail. Small signaling molecules such as cytokines, growth hormones, or prolactins bind to the cytokine receptors and initiate their dimerization. The dimerization brings the cytosolic JAKs together that trans-phosphorylate and activates each other. The activated JAKs now phosphorylate cytosolic tails of the cytokine receptors, which serve as binding sites for adaptor proteins such as SH2...