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Liu C.,University of California at San Diego | Liu C.,Pacific Research Fisheries Center | Liu C.,Shanghai Public Clinical Health Center | Chen X.,Shanghai Public Clinical Health Center | And 4 more authors.
Journal of Biological Chemistry | Year: 2014

Background: Toll-like receptor 4 (TLR4) mediates BAMBI down-regulation, which activates hepatic stellate cells (HSCs). Results: LPS and TNF-β induced binding of NF-κBp50 to HDAC1, which suppressed BAMBI promoter activity and mRNA expression in HSCs. Conclusion: TLR4-mediated HSC activation is regulated by promoter regulation of BAMBI. Significance: Studying the regulation of BAMBI expression by TLR4 is important for understanding liver fibrosis. © 2014 by The American Society for Biochemistry and Molecular Biology, Inc.

Deng Y.,Fudan University | Liu R.,Fudan University | Liu R.,Shanghai Public Clinical Health Center | Yang P.,Fudan University | Liang J.,Fudan University
Journal of Separation Science | Year: 2015

An in vivo study of efavirenz metabolites in rats and human patients with ultra high performance liquid chromatography coupled with quadrupole time-of-flight tandem mass spectrometry combined with MetabolitePilotMT software is reported for the first time. Considering the polarity differences between the metabolites, solid-phase extraction and protein precipitation were both applied as a part of the sample preparation method. The structures of the metabolites and their fragment ions were identified or tentatively characterized based on the accurate mass and MS2 data. As a result, a total of 15 metabolites, including 11 from rat samples and 13 from human samples, were identified or tentatively characterized. Two metabolites and several new metabolism pathways are reported for the first time. This study provides a practical approach for identifying complicated metabolites through the rapid and reliable ultra high performance liquid chromatography coupled with quadrupole time-of-flight tandem mass spectrometry technique, which could be widely used for the investigation of drug metabolites. © 2015 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

Chen Q.-Y.,Shanghai Public Clinical Health Center | Wan Y.-M.,Shanghai Public Clinical Health Center | Zhang X.-Y.,Shanghai Public Clinical Health Center
Chinese Journal of Biologicals | Year: 2015

IgG-Fc fusion proteins are molecules in which biologically active proteins are fused genetically to the hinge region and Fc fragment of immunoglobulin G. IgG-Fc fusion proteins can exert biological functions of fused peptides or proteins and endow IgG-like properties including long plasma half-life and additional Fc fragment properties, which have been widely used for clinical therapy, biomedical research and other fields. Reasonable optimization of IgG-Fc fusion proteins is a trend in future. Selection of appropriate IgG subclasses as carriers as well as modification of amino acid sequences and glycosylation of Fc fragment can prolong the plasma half-life and optimize the effector function of fusion protein so as to obtain an ideal immunotherapeutic effect. This paper summarizes the function and optimization strategy of IgG-Fc fusion proteins and introduce their current status in clinical research.

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