FEBS Letters
Volume 584, Issue 11 , Pages 2201-2206, 3 June 2010

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

Edited by Beat Imhof

  • Špela Konjar

      Affiliations

    • Department of Biochemistry, Molecular and Structural Biology, Jozef Stefan Institute, 1000 Ljubljana, Slovenia
  • ,
  • Fangfang Yin

      Affiliations

    • Department of Pathology, Stanford University, Stanford, CA 94305, USA
  • ,
  • Matthew Bogyo

      Affiliations

    • Department of Pathology, Stanford University, Stanford, CA 94305, USA
  • ,
  • Boris Turk

      Affiliations

    • Department of Biochemistry, Molecular and Structural Biology, Jozef Stefan Institute, 1000 Ljubljana, Slovenia
  • ,
  • Nataša Kopitar-Jerala

      Affiliations

    • Department of Biochemistry, Molecular and Structural Biology, Jozef Stefan Institute, 1000 Ljubljana, Slovenia
    • Corresponding Author InformationCorrespondence to: Nataša Kopitar-Jerala, Department of Biochemistry Molecular and Structural Biology, Jozef Stefan Institute, Jamova 39, 1000 Ljubljana, Slovenia. Fax: + 386 1 477 3984.

Received 14 January 2010; received in revised form 5 March 2010; accepted 17 March 2010. published online 23 March 2010.

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 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)

Abbreviations: ABP, activity based probe, IFN-γ, interferon gamma, IL-4, interleukin-4, LPS, lipopolysaccharide, MHC, major histocompatibility complex, MENT, myeloid and erythroid nuclear termination stage-specific protein, SpiA3G, serpin A3G, TLR 4, toll-like receptor 4

Keywords: Cathepsin L, Macrophage activation, Nucleolus, Serpin A3G

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PII: S0014-5793(10)00243-7

doi:10.1016/j.febslet.2010.03.031

FEBS Letters
Volume 584, Issue 11 , Pages 2201-2206, 3 June 2010