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Updated: May 8, 2026

In Vitro Assay to Measure Phosphatidylethanolamine Methyltransferase Activity
Published on: January 5, 2016
Phosphatidylethanolamine binding protein 1 in vacular endothelial cell autophagy and atherosclerosis
Li Wang1, HaiYing Li, JinFeng Zhang
1J. Y. Miao and B. X. Zhao: Institute of Developmental Biology, School of Life Science, Shandong University, Jinan 250100, China. Emails: miaojy@sdu.edu.cn and bxzhao@sdu.edu.cn.
Abstract:
We previously found that phosphatidylcholine-specific phospholipase C (PC-PLC) was a key inducing element of atherosclerosis, and might negatively regulate human umbilical vein endothelial cell (HUVEC) autophagy. To further investigate the mechanism of PC-PLC action, we initially identified phosphatidylethanolamine binding protein 1 (PEBP1) as a binding partner of PC-PLC by using mass spectrometry (MS, MALDI-TOF/TOF). We found that PEBP1 positively regulated PC-PLC activity in HUVECs, and inhibition of PC-PLC by its inhibitor D609 suppressed PEBP1 expression dramatically. Moreover, both PC-PLC and PEBP1 negatively regulated HUVEC autophagy independently of mammalian target of rapamycin (mTOR). Furthermore, the PEBP1 level was elevated during the development of atherosclerosis, while D609 significantly decreased the upregulated PEBP1 level in apoE(-/-) mice.
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