A novel fluorogenic substrate for the measurement of endothelial lipase activity

阅读量:

19

摘要:

Endothelial lipase (EL) is a phospholipase A1 (PLA1) enzyme that hydrolyzes phospholipids at the sn-1 position to produce lysophospholipids and free fatty acids. Measurement of the PLA1 activity of EL is usually accomplished by the use of substrates that are also hydrolyzed by lipases in other subfamilies such as PLA2 enzymes. In order to distinguish PLA1 activity of EL from PLA2 enzymatic activity in cell-based assays, cell supernatants, and other nonhomogeneous systems, a novel fluorogenic substrate with selectivity toward PLA1 hydrolysis was conceived and characterized. This substrate was preferred by PLA1 enzymes, such as EL and hepatic lipase, and was cleaved with much lower efficiency by lipases that exhibit primarily triglyceride lipase activity, such as LPL or a lipase with PLA2 activity. The phospholipase activity detected by the PLA1 substrate could be inhibited with the small molecule esterase inhibitor ebelactone B. Furthermore, the PLA1 substrate was able to detect EL activity in human umbilical vein endothelial cells in a cell-based assay. This substrate is a useful reagent for identifying modulators of PLA1 enzymes, such as EL, and aiding in characterizing their mechanisms of action.

展开

关键词:

phospholipase A1

DOI:

10.1194/jlr.D007971

被引量:

43

年份:

2011

通过文献互助平台发起求助,成功后即可免费获取论文全文。

相似文献

参考文献

引证文献

辅助模式

0

引用

文献可以批量引用啦~
欢迎点我试用!

关于我们

百度学术集成海量学术资源,融合人工智能、深度学习、大数据分析等技术,为科研工作者提供全面快捷的学术服务。在这里我们保持学习的态度,不忘初心,砥砺前行。
了解更多>>

友情链接

百度云百度翻译

联系我们

合作与服务

期刊合作 图书馆合作 下载产品手册

©2025 Baidu 百度学术声明 使用百度前必读

引用