Fucosylation in cystic fibrosis airway epithelial cells

Jovin O. Lazatin, Mary Catherine Glick, Thomas F. Scanlin

Research output: Contribution to journalArticlepeer-review

14 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)263-270
Number of pages8
JournalGlycosylation & Disease
Issue number4
StatePublished - Sep 1994
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biochemistry


  • CFTR
  • airway epithelial cells
  • cystic fibrosis
  • fucosylation
  • α-l-fucosidase


Dive into the research topics of 'Fucosylation in cystic fibrosis airway epithelial cells'. Together they form a unique fingerprint.

Cite this