Phospholipase A2 augments contraction and intracellular calcium mobilization through thromboxane A2 in bovine tracheal smooth muscle

Y. Takata, Y. Nishimura, H. Maeda, M. Yokoyama
1999 European Respiratory Journal  
A series of monoclonal antibodies which bind to a mucin known as M1 (anti-M1 MAbs) have also been shown to detect the product of the human gene MUC5AC. The aim of this investigation was to determine the concentration of the M1 mucin in the surface epithelium of human bronchial preparations by means of immunohistochemistry and in the bronchial fluid derived from human airways by means of an immunoradiometric assay. Human bronchial ring preparations from the resection material of 20 patients were
more » ... of 20 patients were challenged with methacholine, leukotriene D 4 , or anti-immunoglobulin E. Experiments were performed in preparations with an intact epithelium as well as in tissues in which the epithelium had been mechanically removed. The anti-M1 MAbs stained the goblet cells in the epithelium intensely and there was also light and less uniform staining in the submucosa. The M1/MUC5AC mucin in the fluids secreted by the bronchial preparations was not modified during either the experimental protocol or stimulation with the different secretagogues. However, in preparations in which the epithelium had been removed, there was a significant reduction in the amount of M1/MUC5AC mucin detected. These data suggest that the M1/MUC5AC mucin detected in the biological fluids produced by human airways in vitro may be released constantly, and principally from the goblet cells in the epithelial layer. Eur Respir J 1999; 14: 390±395.
doi:10.1183/09031936.99.14239699 fatcat:xb6jrae4xjar3du6bkebjj7vdi