Identification of human tracheo-bronchial mucin precursors

Bronchial mucin peptide chains were obtained by performing a two-step chemical deglycosylation of the highly glycosylated regions (or glycopeptides) which are the most characteristic part of bronchial mucins. The deglycosylated preparation was used to prepare an antiserum directed against mucin peptide epitopes. This antiserum reacted with the area containing rough endoplasmic reticulum of goblet cells and of mucous gland of human bronchial mucosa but not with secretory vesicles. The antiserum was used for immunoprecipitation of radiolabelled mucin precursors in pulse-chase experiments with explants of human bronchial mucosa. SDS-polyacrylamide gel electrophoresis followed by fluorography revealed precursors with a molecular mass in the range of 200 to 400 kDa as early as after 10 min pulse labeling with [3H]threonine. These results suggest that the mucin polydispersity previously visualized by electron microscopy may be explained by the synthesis of several respiratory mucin peptide precursors with different molecular sizes and/or that precursors with different amounts of carbohydrate are rapidly formed.