Osteopontin induces ubiquitin-dependent degradation of STAT1 in RAW264.7 murine macrophages.

Osteopontin induces ubiquitin-dependent degradation of STAT1 in RAW264.7 murine macrophages. Research Abstract Details 

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Osteopontin induces ubiquitin-dependent degradation of STAT1 in RAW264.7 murine macrophages. Abstract Text:

Chengjiang Gao,Hongtao Guo,Zhiyong Mi,Michael J Grusby,Paul C Kuo,

In systemic inflammation induced by endotoxin (LPS), the macrophage produces the majority of the circulating NO metabolites. However, while the molecular pathways which up-regulate iNOS expression have been extensively studied in the macrophage, little is known of the parallel counterregulatory pathways which repress or inhibit macrophage iNOS expression. Using both in vivo and in vitro murine models of endotoxin (LPS) stimulation, we have previously demonstrated that NO feedback inhibits its own synthesis by increasing transcription of osteopontin (OPN), a potent transrepressor of inducible NO synthase expression. In this current study, using a system of LPS-treated RAW264.7 macrophages, we go on to demonstrate that OPN increases STAT1 ubiquitination and subsequent 26s proteasome-mediated degradation to inhibit STAT1 dependent iNOS promoter activity, transcription, and protein expression. In addition, we identify STAT-interacting LIM protein as the critical STAT ubiquitin E3 ligase critical for STAT1 degradation in this setting. OPN has not been linked previously to STAT1 degradation. This regulation of STAT1 degradation underlies OPN's effect as an inhibitor of iNOS gene transcription. These are novel findings and define OPN as a unique and as yet, poorly characterized, transactivator of STAT1 degradation by the ubiquitin-proteasome system.

Osteopontin induces ubiquitin-dependent degradation of STAT1 in RAW264.7 murine macrophages. Publishing Authors By Initials

C Gao,H Guo,Z Mi,MJ Grusby,PC Kuo,

For similar enzymes and coenzymes: enzymes: ligases: ubiquitin-protein ligase complexes: ubiquitin-protein ligases research abstracts see: enzymes and coenzymes: enzymes: ligases: ubiquitin-protein ligase complexes: ubiquitin-protein ligases research

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Osteopontin induces ubiquitin-dependent degradation of STAT1 in RAW264.7 murine macrophages. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: Journal of immunology (Baltimore, Md. : 1950)

VOLUME: 178

Page Numbers: 1870-81

Journal Abbreviation: J. Immunol.

ISSN: 0022-1767

DAY: 1

MONTH: Feb

YEAR: 2007

Osteopontin induces ubiquitin-dependent degradation of STAT1 in RAW264.7 murine macrophages. Information

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LANGUAGE: eng

NlmUniqueID: 2985117

Osteopontin induces ubiquitin-dependent degradation of STAT1 in RAW264.7 murine macrophages. Keywords Mesh Terms:

KEYWORDS: Ubiquitin-Protein Ligases

MESH TERMS: metabolism

Chemical & Substance for Abstract: Osteopontin induces ubiquitin-dependent degradation of STAT1 in RAW264.7 murine macrophages. Information

Substance Name: Ubiquitin-Protein Ligases

Registry Number: EC 6.3.2.19

Grant and Affiliation Information for Osteopontin induces ubiquitin-dependent degradation of STAT1 in RAW264.7 murine macrophages.

AFFILIATION: Department of Surgery, Duke University Medical Center, Durham, NC 27710, USA.

Country: United States

AGENCY: United States NIGMS

GRANT: R01-GM65113

ACRONYM: GM

MEDLINETA: J Immunol

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