ABSTRACT
BACKGROUND Idiopathic pulmonary fibrosis (IPF) can severely damage lung function, which may result in death. Emodin is a major ingredient of rhubarb and has been proven to protect against lung disruptions. Our study focused on the potential medicinal effect of emodin against IPF. MATERIAL AND METHODS The experiment subjects were fully-grown male Sprague-Dawley rats with average weight of 180-220 kg. Histological analyses, Western blotting analysis, quantitative real-time PCR, and statistical analysis were used in the study. RESULTS We found that emodin significantly reduced lung structural distortion, collagen overproduction, massive inflammatory cells infiltration, proinflammatory cytokines expansion, and injuries caused by administration of bleomycin (BLM). Additionally, emodin suppressed the accumulation of p-IκBα and NF-κB, while stimulating the Nrf2-antioxidant signaling process in damaged lungs. Emodin inhibited epithelial-mesenchymal transition (EMT) induced by BLM in the lungs. Moreover, emodin suppressed the TGF-ß1 expression and the downstream signal molecules p-Smad-2 and p-Smad-3, which are reinforced by BLM. Emodin can also reverse EMT-like shifts induced by recombinant TGF-ß1 in alveolar epithelial cultured cells. CONCLUSIONS The effect of emodin in fibrotic lung injury is closely related to its favorable properties of anti-inflammation and anti-oxidation.
Subject(s)
Emodin/pharmacology , Idiopathic Pulmonary Fibrosis/drug therapy , A549 Cells/drug effects , Animals , Anti-Inflammatory Agents/therapeutic use , Antioxidants/pharmacology , Bleomycin , Cell Culture Techniques , Cytokines/metabolism , Disease Models, Animal , Humans , Idiopathic Pulmonary Fibrosis/physiopathology , Inflammation/pathology , Lung/pathology , Male , NF-E2-Related Factor 2/drug effects , NF-KappaB Inhibitor alpha/drug effects , NF-kappa B/drug effects , Oxidative Stress/drug effects , Pulmonary Fibrosis/drug therapy , Rats , Rats, Sprague-Dawley , Signal Transduction/drug effects , Smad Proteins/drug effectsABSTRACT
Recent reports showed that patients could be sensitized to fish tropomyosin (TM), who exhibited clinical symptoms. However, little information is available on differences in TM immune cross-reactivity among fish, shrimp and clam. Moreover, allergenicity might change during the food processing owing to the change of protein structure. In this study, we developed a nonthermal extraction technique to purified TM, IgG/IgE binding, cross-reactivity and structures were compared. Results showed that raw and boiled fish-TM were not cross reactive and had weak recognition of shrimp, while, shrimp-TM and clam-TM were cross reactive. The ELISA further confirmed that fish-TM was not able to trigger allergic immune response in shrimp sensitive subjects, while, surface hydrophobicity of fish-TM was higher. The study demonstrated that fish-TM, being with high sequence similarity, did not have cross-reactivity with shrimp and clam-TM. They could have a variable degree of IgE binding depending on subject sensitivity and allergenicity.