清凯林颗粒通过抑制PI3K/AKT和SRC/STAT3信号通路来缓解肺纤维化
Hong Li1, Guang Xin1, Qilong Zhou1
1Department of Emergency Medicine, Laboratory of Ethnopharmacology, Tissue-Orientated Property of Chinese Medicine Key Laboratory of Sichuan Province, West China School of Medicine, West China Hospital, Sichuan University, Chengdu 610041, China.
Bioorganic chemistry
|March 27, 2024
概括
青凯林颗粒 (QKL) 显示出治疗肺纤维化 (PF) 的潜力. 这项研究发现,QKL通过影响关键信号通路来减少炎症和纤维化,为PF提供了新的治疗可能性.
科学领域:
- 药理学 药理学是指药理学的学科.
- 生物医学科学 生物医学科学
- 传统中国医药 传统中国医药
背景情况:
- 肺纤维化 (PF) 是一种严重的肺病,治疗选择有限,死亡率高.
- 来自Angong Niuhuang药丸的Qingkailing颗粒 (QKL) 正在研究其在肺部疾病中的治疗潜力.
研究的目的:
- 首次研究青凯林颗粒 (QKL) 对肺纤维化 (PF) 的治疗作用和机制.
- 将网络药理与实验验证相结合,以阐明QKL对PF的作用.
主要方法:
- 使用白素诱导的PF小鼠模型进行体内验证.
- 使用TGF-β1诱导的肺纤维化细胞模型进行了体外研究.
- 采用了网络药理学,分子对接和西部涂抹来识别机制.
主要成果:
- 在体内,QKL显著降低了原沉积,并抑制了促炎性细胞因子.
- 在体外,QKL保护细胞免受损伤,减少原的积累,并抑制细胞迁移.
- 网络药理学和西部涂抹证实QKL调节PI3K/AKT和SRC/STAT3信号通路.
结论:
- QKL在缓解肺炎和纤维化方面具有显著的治疗潜力.
- 该研究强调了PI3K/AKT和SRC/STAT3信号通路的下调作为QKL作用的关键机制.
- 在QKL中的活性化合物在其抗纤维和抗炎作用中起着关键作用.
更多相关视频
13:18Network Pharmacology Prediction and Experimental Validation of Trichosanthes-Fritillaria thunbergii Action Mechanism Against Lung Adenocarcinoma
Published on: March 3, 2023
1.2K
05:03Establishing a Silicosis Rat Model via Exposure of Whole-Body to Respirable Silica
Published on: October 28, 2022
1.2K
相关概念视频
PI3K/mTOR/AKT Signaling Pathway
3.5K
The mammalian target of rapamycin (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1 (mTORC1) and mTOR complex 2 (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast, mTORC2 consists of a...
3.5K
The JAK-STAT Signaling Pathway
8.9K
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...
8.9K
