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- W4285132537 abstract "Objectives Acute liver failure (ALF) is a rare life-threatening condition that leads to rapid deterioration of liver function. Although global awareness of ALF consequences is increasing, the precise molecular mechanisms associated with its rapid progression remain unclear. In the present study, we established a rat model of ALF using Lipopolysaccharide (LPS)/D-galactosamine (D-Gal) and explored the potential molecular mechanism of ALF. Methods Multiplexed isobaric tandem mass tag labelling combined with liquid chromatography-mass spectrometry was used to thoroughly screen for differentially expressed proteins in liver samples from LPS/D-Gal-induced ALF rat models. Results We identified 175 proteins, whose expression was altered by at least 1.5-fold, between the liver samples of ALF and control groups. Of these, 14 dysregulated proteins mainly participated in the regulation of neutrophil extracellular trap (NET) formation. Furthermore, rats with severe ALF showed elevated levels of cathelicidin antimicrobial peptide, myeloperoxidase, and fibrinogen gamma chain, consistent with NET formation. These findings suggest that the NET formation pathway may have contributed to the regulation of the clinical features and progression of liver injury in ALF rats. Conclusion To our knowledge, this study is the first to report a global differential protein expression profile of liver samples from rats with LPS/D-Gal-induced ALF. Our TMT-based quantitative proteomic analysis revealed molecular differences involved in NET formation between the ALF and control rat groups, potential therapeutic targets for ALF treatment as well as fundamental information for further detailed experimental research." @default.
- W4285132537 created "2022-07-14" @default.
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- W4285132537 date "2022-01-01" @default.
- W4285132537 modified "2023-09-30" @default.
- W4285132537 title "Liver proteomic analysis reveals acute liver failure induced by lipopolysaccharide/D-galactosamine in rats involved in neutrophil extracellular trap formation" @default.
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- W4285132537 doi "https://doi.org/10.1177/1721727x221110989" @default.
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