Objective: To investigate the expression of HMGB1 and RAGE mRNA in the lungs of asthmatic mice and the effect of N-acetylcysteine (NAC) on their expression.
Methods: Twenty-one female BALB/c mice were randomly divided into control group, asthma group and NAC group (n=7). The expressions of HMGB1 and RAGE mRNA and their distributions in the lungs were detected by RT-PCR and immunohistochemical method.
Results: The expression levels of HMGB1 and RAGE mRNA were not significantly different between the control group (0.88-/+0.02 and 1.20-/+0.20, respectively) and the asthma model group (0.86-/+0.05 and 1.21-/+0.08, P>0.05). After NAC treatment, both of HMGB1 and RAGE mRNA levels (0.98-/+0.05 and 1.58-/+0.21) were significantly higher than those in the other two groups (P<0.05). HMGB1 was found in the nuclei and membrane of the bronchial and alveolar epithelial cells, and RAGE was located on the membrane of the alveolar epithelial cells.
Conclusion: HMGB1 and RAGE may play a role in the oxidative stress during asthma, but the exact mechanism needs further investigation.
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Int J Mol Sci
January 2025
School of Pharmacy, Chengdu University of Traditional Chinese Medicine, Chengdu 611137, China.
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Department of Pathology, University of Illinois Chicago, Chicago, Illinois, USA.
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The aim of this study was to reveal the mechanism of cold stimulation (CS)-bronchial epithelial cells (BECs) derived exosomes (CS-BECs-exo) aggravated sepsis induced acute lung injury (SALI). CS-BECs-exo were separated by differential centrifugation and were characterized. Proteomics, immunoprecipitation, and RAGE knockout (RAGE) mice were used to investigate the mechanism of CS-BECs-exo aggravated SALI.
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Department of Pharmacological and Pharmaceutical Sciences, College of Pharmacy, University of Houston, Houston, TX 77204, USA.
High Mobility Group Box 1 (HMGB1) is a highly conserved non-histone chromatin-associated protein across species, primarily recognized for its regulatory impact on vital cellular processes, like autophagy, cell survival, and apoptosis. HMGB1 exhibits dual functionality based on its localization: both as a non-histone protein in the nucleus and as an inducer of inflammatory cytokines upon extracellular release. Pathophysiological insights reveal that HMGB1 plays a significant role in the onset and progression of a vast array of diseases, viz.
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