Journal
INTERNATIONAL IMMUNOPHARMACOLOGY
Volume 14, Issue 2, Pages 138-144Publisher
ELSEVIER
DOI: 10.1016/j.intimp.2012.06.017
Keywords
Arctigenin Inducible nitric oxide synthase (iNOS); Carboxyl terminus of HSC70-interacting protein (CHIP); Lipopolysaccharide (LPS); Ubiquitination; Phosphorylation
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Funding
- National Nature Science Foundation of China [81072433, 31071000]
- Natural Science Foundation of the Anhui Higher Education Institutions of China [KJ2012ZD10]
- Natural Science Foundation of Bengbu College [2011ZR02zd]
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Arctigenin, a natural dibenzylbutyrolactone lignan compound, has been reported to possess anti-inflammatory properties. Previous works showed that arctigenin decreased lipopolysaccharide (LPS)-induced iNOS at transcription level. However, whether arctigenin could regulate iNOS at the post-translational level is still unclear. In the present study, we demonstrated that arctigenin promoted the degradation of iNOS which is expressed under LPS stimulation in murine macrophage-like RAW 264.7 cells. Such degradation of iNOS protein is due to CHIP-associated ubiquitination and proteasome-dependency. Furthermore, arctigenin decreased iNOS phosphorylation through inhibiting ERK and Src activation, subsequently suppressed iNOS enzyme activity. In conclusion, our research displays a new finding that arctigenin can promote the ubiqitination and degradation of iNOS after LPS stimulation. iNOS activity regulated by arctigenin is likely to involve a multitude of crosstalking mechanisms. (C) 2012 Elsevier B.V. All rights reserved.
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