Tuberculosis and Respiratory Diseases

  • 제70권2호
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  • Pages.113-124
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  • 2011
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  • 1738-3536(pISSN)
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  • 2005-6184(eISSN)
대한결핵및호흡기학회 (The Korean Academy of Tuberculosis and Respiratory Diseases)
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The Macrophage-Specific Transcription Factor Can Be Modified Posttranslationally by Ubiquitination in the Lipopolysaccharide-Treated Macrophages

  • Jung, Jae-Woo (Division of Allergy, Respiratory and Critical Care Medicine, Department of Internal Medicine, Chung-Ang University College of Medicine) ;
  • Choi, Jae-Chol (Division of Allergy, Respiratory and Critical Care Medicine, Department of Internal Medicine, Chung-Ang University College of Medicine) ;
  • Kim, Jae-Yeol (Division of Allergy, Respiratory and Critical Care Medicine, Department of Internal Medicine, Chung-Ang University College of Medicine) ;
  • Park, In-Won (Division of Allergy, Respiratory and Critical Care Medicine, Department of Internal Medicine, Chung-Ang University College of Medicine) ;
  • Choi, Byoung-Whui (Division of Allergy, Respiratory and Critical Care Medicine, Department of Internal Medicine, Chung-Ang University College of Medicine) ;
  • Shin, Jong-Wook (Division of Allergy, Respiratory and Critical Care Medicine, Department of Internal Medicine, Chung-Ang University College of Medicine) ;
  • Christman, John William (Department of Pulmonary, Critical Care and Sleep Medicine, University of Illinois College of Medicine)
  • 투고 : 2011.01.17
  • 심사 : 2011.01.19
  • 발행 : 2011.02.28
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초록

Background: Macrophages are one of the most important inflammatory cells in innate immunity. PU.1 is a macrophage-specific transcription factor. Ubiquitins are the ultimate regulator of eukaryotic transcription. The ubiquitination process for PU.1 is unknown. This study investigated the lipopolysaccharide (LPS)-induced activation of PU.1 and its relation to ubiquitins in the macrophages. Methods: Raw264.7 cells, the primary cultured alveolar, pulmonary, and bone marrow derived macrophages were used. The Raw264.7 cells were treated with MG-132, $NH_4Cl$, lactacytin and LPS. Nitric oxide and prostaglandin D2 and E2 were measured. Immunoprecipitation and Western blots were used to check ubiquitination of PU.1. Results: The PU.1 ubiquitination increased after LPS ($1{\mu}g$/mL) treatment for 4 hours on Raw264.7 cells. The ubiquitination of PU.1 by LPS was increased by MG-132 or $NH_4Cl$ pretreatment. Two hours of LPS treatment on macrophages, PU.1 activation was not induced nor increased with the inhibition of proteasomes and/or lysosomes. The ubiquitination of PU.1 was increased in LPS-treated Raw264.7 cells at 12- and at 24 hours. LPS-treated cells increased nitric oxide production, which was diminished by MG-132 or $NH_4Cl$. LPS increased the production of $PGE_2$ in the alveolar and peritoneal macrophages of wild type mice; however, $PGE_2$ was blocked or diminished in Rac2 null mice. Pretreatment of lactacystin increased $PGE_2$, however it decreased the $PGD_2$ level in the macrophages derived from the bone marrow of B57/BL6 mice. Conclusion: LPS treatment in the macrophages ubiquitinates PU.1. Ubiquitination of PU.1 may be involved in synthesis of nitric oxide and prostaglandins.

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