Altered glycosylation is a phenotypic characteristic of cystic fibrosis (CF), and some of the alterations are summarized. The lungs are the site of the lethal pathology of the disease. Therefore, two of the characteristics were examined in CF and non-CF immortalized airway epithelial cell lines (AEC). The activity of α-l-fucosidase was elevated (280%) in CF AEC when compared with non-CF AEC, whereas the activities of the other lysosomal enzymes which were examined were similar in both cell types. α-l-Fucosidase activity was transiently increased in the non-CF cells after treatment with Brefeldin A (BFA) for 6 h. Thus BFA caused the normal cells to express a phenotypic characteristic of CF. Glycopeptides from the CF and non-CF AECs metabolically labeled with l-[3H]fucose were examined for binding to lentil lectin-Sepharose. A higher percentage of CF glycopeptides bound to lentil lectin, 43% compared with 23% for non-CF control. In addition a higher percentage of CF glycopeptides were bound tightly to lentil lectin and required 0.2M α-methylmannoside to be eluted. This species of tightly bound glycopeptides increased dramatically to 77% from 46% when the CF AEC were treated with BFA. In contrast, the non-CF cell glycopeptides had a minor decrease in tightly bound glycopeptides to 26% from 33% after BFA treatment. Thus, the CF AEC showed fucosylation alteration observed previously for other CF cells and tissue.
All Science Journal Classification (ASJC) codes
- airway epithelial cells
- cystic fibrosis