自交轴蛋白
化学
计算生物学
生物化学
纳米技术
生物
溶血磷脂酸
材料科学
受体
作者
Silvia Cavalli,Anna J.S. Houben,Harald M. H. G. Albers,Erica W. van Tilburg,Arnoud de Ru,Junken Aoki,Peter A. van Veelen,Wouter H. Moolenaar,Huib Ovaa
出处
期刊:ChemBioChem
[Wiley]
日期:2010-10-12
卷期号:11 (16): 2311-2317
被引量:12
标识
DOI:10.1002/cbic.201000349
摘要
Abstract Autotaxin (ATX), or ecto‐nucleotide pyrophosphatase/phosphodiesterase 2 (ENPP2), is a secreted lysophospholipase D that hydrolyses lysophosphatidylcholine into the lipid mediator lysophosphatidic acid (LPA), a mitogen and chemoattractant for many cell types. ATX has been implicated in tumour progression and inflammation, and might serve as a biomarker. Here we describe the development of a fluorescent activity‐based probe that covalently binds to the active site of ATX. The probe consists of a lysophospholipid‐based backbone linked to a trapping moiety that becomes reactive after phosphate ester hydrolysis, and a Cy5 fluorescent dye to allow visualisation of active ATX. The probe reacts specifically with the three known isoforms of ATX, it competes with small‐molecule inhibitors for binding to ATX and allows ATX activity in plasma to be determined. Our activity‐based reporter will be useful for monitoring ATX activity in biological fluids and for inhibitor screening.
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