1. Increased nucleolar localization of SpiA3G in classically but not alternatively activated macrophages
- Author
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Boris Turk, Špela Konjar, Matthew Bogyo, Fang-Fang Yin, and Nataša Kopitar-Jerala
- Subjects
Nucleolus ,Cathepsin L ,Anti-Inflammatory Agents ,Biophysics ,Inflammation ,Biochemistry ,Cell Line ,Mice ,Structural Biology ,Genetics ,medicine ,Animals ,Macrophage activation ,Myeloid and erythroid nuclear termination stage-specific protein ,Molecular Biology ,Serpins ,Tissue homeostasis ,Interleukin 4 ,Cathepsin ,Innate immune system ,biology ,Macrophages ,Serpin A3G ,Cell Biology ,Cathepsins ,Cell biology ,Immunology ,biology.protein ,medicine.symptom ,Cell Nucleolus - Abstract
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 summaryMINT-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)
- Published
- 2010
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