Potential mechanism underlying down-regulation of albumin expression induced by lipopolysaccharide in rat hepatocytes.
- Author:
Xin-ying WANG
1
;
Ning LI
;
Wei-qin LI
;
Jie-shou LI
Author Information
- Publication Type:Journal Article
- MeSH: Albumins; genetics; metabolism; Animals; Calcium-Calmodulin-Dependent Protein Kinases; antagonists & inhibitors; Dose-Response Relationship, Drug; Down-Regulation; Enzyme Inhibitors; pharmacology; Enzyme-Linked Immunosorbent Assay; Flavonoids; pharmacology; Hepatocytes; drug effects; metabolism; Imidazoles; pharmacology; Lipopolysaccharides; toxicity; Male; Mitogen-Activated Protein Kinases; antagonists & inhibitors; Pyridines; pharmacology; RNA, Messenger; genetics; metabolism; Rats; Reverse Transcriptase Polymerase Chain Reaction; Time Factors; p38 Mitogen-Activated Protein Kinases
- From: Chinese Journal of Surgery 2004;42(6):362-365
- CountryChina
- Language:Chinese
-
Abstract:
OBJECTIVETo investigate the potential molecular mechanism underlying down-regulation of albumin expression induced by lipopolysaccharide (LPS) in rat hepatocytes.
METHODSThe albumin mRNA expression and albumin protein levels in the supernatant were observed at 0, 2, 8, 12 and 24 hours after 1 micro g/ml LPS treatment. The albumin mRNA expression was determined by RT-PCR, and albumin protein levels were assayed with EIA in the supernatant of hepatocytes pretreated with specific inhibitors of extracellular signal-regulated kinase (PD98059) and p38 kinase (SB203580).
RESULTSThe albumin mRNA expression was reduced to 70% of baseline value, meanwhile, the albumin protein concentration in the supernatant was reduced by 50% compared with the controls after 24 hours of LPS treatment. Pretreatment with PD98059 and SB203580 did significantly inhibit the reduction of albumin by LPS at the given dose.
CONCLUSIONThe results indicate that LPS can induce the reduction of albumin synthesis by down-regulation of albumin mRNA expression at transcription level, and the process may be related to the signal transducation of extracellular signal-regulated kinase and p38 kinase.
