相关实验视频

Updated: Jul 12, 2026

Mouse Fetal Liver Culture System to Dissect Target Gene Functions at the Early and Late Stages of Terminal Erythropoiesis

Mouse Fetal Liver Culture System to Dissect Target Gene Functions at the Early and Late Stages of Terminal Erythropoiesis

Published on: September 9, 2014

布法林通过p38 MAPK和Rac1 GTPase重编程红细胞寿命

Mohammad A Alfhili¹, Jawaher Alsughayyir²

¹Chair of Medical and Molecular Genetics Research, Department of Clinical Laboratory Sciences, College of Applied Medical Sciences, King Saud University, Riyadh, 12372, Saudi Arabia.

Toxicon : official journal of the International Society on Toxinology

|February 5, 2024

概括

布法林 (BFN) 是一种癌症药物,会导致红细胞过早死亡,并损害其他血液细胞. 这表明在使用BFN用于抗癌疗法时应谨慎,因为它对红细胞和其他细胞有毒.

科学领域:

生物化学生物化学
毒理学毒理学毒理学
血液学血液学血液学

背景情况:

布法林 (BFN) 是来自Bufo毒素的心性类固醇,通过诱导亡,表现出抗癌性质.
人体红血细胞 (RBC) 经历了红色化,这是一种与各种病理相关的过程.
BFN对红细胞的潜在毒性仍然没有被描述.

研究的目的:

研究BFN对红细胞生理学和寿命的影响的基础生物化学机制.
在抗癌度下评估BFN对人类红细胞的毒性.

主要方法:

隔离的人体红细胞被暴露在BFN (10-200μM) 中24小时.
用光度测试测量血液溶解和血液溶解标志物.
流式细胞计检测出了瘤标记物,包括酸胺外化,细胞收缩,细胞溶液Ca2+和活性氧物种 (ROS).

主要成果:

BFN诱导了Ca2+独立的血液溶解和LDH,AST,CK和K+的释放.
在红细胞中,BFN增加了氨酸氨酸外化,细胞 Ca2+水平,细胞缩和ROS产生.
BFN干扰了Na+和Mg2+运输,使血红蛋白耗尽,红细胞碎片化,并对网状细胞,淋巴细胞和血小板产生选择性毒性.

结论:

BFN诱导红细胞过早死亡,由p38 MAPK和Rac1 GTPase调节.
BFN对各种外围血液细胞表现出有害影响.
这些发现需要在抗癌治疗策略中对布法林进行谨慎考虑,因为它具有毒性.

关键词:

这是一种抗癌药物.布法林是布法林的一个词.埃里普托斯症 (Eryptosis) 是一种疾病.血液溶解血液溶解氧化应激是一种氧化应激.p38 MAPKK 的时间.

更多相关视频

Molecular Modulation by Lentivirus-Delivered Specific shRNAs in Endoplasmic Reticulum Stressed Neurons

Molecular Modulation by Lentivirus-Delivered Specific shRNAs in Endoplasmic Reticulum Stressed Neurons

Published on: April 24, 2021

Ferritinophagy: Assessing the Selective Degradation of Iron by Autophagy in Human Fibroblasts

Ferritinophagy: Assessing the Selective Degradation of Iron by Autophagy in Human Fibroblasts

Published on: February 23, 2024

相关概念视频

The Unfolded Protein Response

The Unfolded Protein Response

The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...