Binding of abscisic acid to human LANCL2

被引:41
|
作者
Sturla, Laura [1 ,2 ]
Fresia, Chiara [2 ,3 ]
Guide, Lucrezia [2 ]
Grozio, Alessia [2 ]
Vigliarolo, Tiziana [2 ]
Mannino, Elena [2 ]
Millo, Enrico [2 ]
Bagnasco, Luca [4 ]
Bruzzone, Santina [2 ,3 ]
De Flora, Antonio [2 ]
Zocchi, Elena [2 ]
机构
[1] Univ Genoa, Dept Expt Med, Ctr Excellence Biomed Res, I-16132 Genoa, Italy
[2] Univ Genoa, Dept Expt Med DIMES, Biochem Sect, I-16132 Genoa, Italy
[3] Adv Biotechnol Ctr, Genoa, Italy
[4] Univ Genoa, Dept Internal Med DIMI, I-16132 Genoa, Italy
关键词
Specific binding; Abscisic acid; Human LANCL2; CYCLIC ADP-RIBOSE; SCINTILLATION PROXIMITY ASSAY; CHELATASE H-SUBUNIT; 2ND-MESSENGER; ARABIDOPSIS; RECEPTORS; SIGNAL;
D O I
10.1016/j.bbrc.2011.10.079
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The phytohormone abscisic acid (ABA) is the central regulator of abiotic stress in plants and plays important roles during plant growth and development. In animal cells, ABA was shown to be an endogenous hormone, acting as a stress signal and stimulating cell functions involved in inflammatory responses and in insulin release. Recently, we demonstrated that Lanthionine synthetase component C-like protein 2 (LANCL2) is required for ABA binding to the plasmamembrane of granulocytes and for the activation of the signaling pathway triggered by ABA in human granulocytes and in rat insulinoma cells. In order to investigate whether ABA activates LANCL2 via direct interaction, we performed specific binding studies on human LANCL2 recombinant protein using different experimental approaches (saturation binding, scintillation proximity assays, dot blot experiments and affinity chromatography). Altogether, results indicate that human recombinant LANCL2 binds ABA directly and provide the first demonstration of ABA binding to a mammalian ABA receptor. (C) 2011 Elsevier Inc. All rights reserved.
引用
收藏
页码:390 / 395
页数:6
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