Increased nucleolar localization of SpiA3G in classically but not alternatively activated macrophages

被引:8
作者
Konjar, Spela [1 ]
Yin, Fangfang [2 ]
Bogyo, Matthew [2 ]
Turk, Boris [1 ]
Kopitar-Jerala, Natasa [1 ]
机构
[1] Jozef Stefan Inst, Dept Biochem Mol & Struct Biol, Ljubljana 1000, Slovenia
[2] Stanford Univ, Dept Pathol, Stanford, CA 94305 USA
关键词
Cathepsin L; Macrophage activation; Nucleolus; Serpin A3G; PROTEASE INHIBITOR 2A; CATHEPSIN-L; CYSTEINE PROTEINASES; HUMAN MONOCYTES; CELLS; IDENTIFICATION; CYSTATINS; PROTECTS; PATHWAY; MENT;
D O I
10.1016/j.febslet.2010.03.031
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
Macrophages play a key role in innate immune response to pathogens and in tissue homeostasis, inflammation and repair. A serpin A3G (SpiA3G) is highly induced in classically activated macrophages. We show increased localization of SpiA3G in the nucleolus and co-localization with cathepsin L, upon classical, but not alternative activation of macrophages. Despite the increased expression of cathepsin L in the nuclei of classically activated macrophages, no cathepsin activity was detected. Since only pro-inflammatory, but not anti-inflammatory stimuli induce increased nucleolar localization of SpiA3G, we propose that SpiA3g translocation into the nucleolus is important in host defense against pathogens. Structured summary: MINT-7714245: fibrillarin (uniprotkb:P35550) and SpiA3G(uniprotkb: Q5I2A0)co-localize (MI:0403) by fluorescence microscopy(MI: 0416) MINT-7714241: SpiA3G (uniprotkb: Q5I2A0) and cathepsin L(uniprotkb:P06797) co-localize (MI:0403) by fluorescence microscopy (MI: 0416) (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
引用
收藏
页码:2201 / 2206
页数:6
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