| Baicalein inhibits nuclear factor-κB and apoptosis via c-FLIP and MAPK in D-GalN/LPS induced acute liver failure in murine models. | |
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MedLine Citation:
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PMID: 20850421 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The hepatoprotective effects and molecular mechanisms of baicalein on acute liver failure induced by d-galactosamine (d-GalN)/lipopolysaccharides (LPS) were investigated in vivo. Mice were administered with different doses of baicalein (50, 100 or 150mg/kg, p.o.) 1h before injection of d-GalN (700mg/kg)/LPS (10μg/kg) and then sacrificed 6h after treatment with d-GalN/LPS. Pretreatment with baicalein prevented d-GalN/LPS-induced liver damage by preventing associated increases of serum aspartate aminotransferase (AST) and alanine aminotransferase (ALT) and by reducing serum tumor necrosis factor α (TNF-α), nitric oxide (NO) or inducible nitric oxide synthase (iNOS) expressions. The molecular mechanisms involved in baicalein-induced inhibition of d-GalN/LPS-caused apoptosis were associated with the protection of mitochondria, increasing the Bcl-2/Bax ratio, blocking the release of cytochrome c, and suppressing the phosphorylation of IκBα, ERK and JNK. Moreover, baicalein activated c-FLIP(L), XIAP and cIAP2 proteins, potentially blocking the recruitment of NF-κB signaling molecules. The results support the investigation of baicalein as a therapeutic candidate for acute liver apoptosis or injury and indicate that baicalein might inhibit liver apoptosis by mediating one or more of these pathways. |
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Authors:
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Yan-Ling Wu; Li-Hua Lian; Ying Wan; Ji-Xing Nan |
Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2010-09-17 |
Journal Detail:
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Title: Chemico-biological interactions Volume: 188 ISSN: 1872-7786 ISO Abbreviation: Chem. Biol. Interact. Publication Date: 2010 Dec |
Date Detail:
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Created Date: 2010-11-12 Completed Date: 2010-12-21 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0227276 Medline TA: Chem Biol Interact Country: Ireland |
Other Details:
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Languages: eng Pagination: 526-34 Citation Subset: IM |
Copyright Information:
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Copyright © 2010 Elsevier Ireland Ltd. All rights reserved. |
Affiliation:
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College of Pharmacy, Yanbian University, Yanji, 133002, Jilin Province, China. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Alanine Transaminase
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blood Animals Apoptosis / drug effects* Aspartate Aminotransferases / blood CASP8 and FADD-Like Apoptosis Regulating Protein / metabolism* Caspase 3 / metabolism Cytochromes c / metabolism Cytoprotection / drug effects Disease Models, Animal Flavanones / pharmacology* Galactosamine / toxicity Gene Expression Regulation, Enzymologic / drug effects Lipopolysaccharides / toxicity Liver / drug effects, metabolism, pathology Liver Failure / chemically induced*, metabolism, pathology* Male Mice Mice, Inbred C57BL Mitogen-Activated Protein Kinases / metabolism* NF-kappa B / antagonists & inhibitors*, metabolism Nitric Oxide / biosynthesis Nitric Oxide Synthase Type II / metabolism Proto-Oncogene Proteins c-bcl-2 / metabolism Tumor Necrosis Factor-alpha / biosynthesis X-Linked Inhibitor of Apoptosis Protein / metabolism |
| Chemical | |
Reg. No./Substance:
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0/CASP8 and FADD-Like Apoptosis Regulating Protein; 0/Cflar protein, mouse; 0/Flavanones; 0/Lipopolysaccharides; 0/NF-kappa B; 0/Proto-Oncogene Proteins c-bcl-2; 0/Tumor Necrosis Factor-alpha; 0/X-Linked Inhibitor of Apoptosis Protein; 10102-43-9/Nitric Oxide; 491-67-8/baicalein; 7535-00-4/Galactosamine; 9007-43-6/Cytochromes c; EC 1.14.13.39/Nitric Oxide Synthase Type II; EC 2.6.1.1/Aspartate Aminotransferases; EC 2.6.1.2/Alanine Transaminase; EC 2.7.11.24/Mitogen-Activated Protein Kinases; EC 3.4.22.-/Caspase 3 |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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