Terminal glycosylation in cystic fibrosis (CF): A review emphasizing the airway epithelial cell

Andrew D. Rhim, Lydia Stoykova, Mary Catherine Glick, Thomas F. Scanlin

Research output: Contribution to journalReview articlepeer-review

39 Scopus citations


Altered terminal glycosylation, with increased fucosylation and decreased sialylation is a hallmark of the cystic fibrosis (CF) glycosylation phenotype. Oligosaccharides purified from the surface membrane glycoconjugates of CF airway epithelial cells have the Lewis x, selectin ligand in terminal positions. This review is focused on the investigations of the glycoconjugates of the CF airway epithelial cell surface. Two of the major bacterial pathogens in CF, Pseudomonas aeruginosa and Haemophilus influenzae, have binding proteins which recognize fucose in α-1,3 linkage and asialoglycoconjugates. Therefore, consideration has been given to the possibility that the altered terminal glycosylation of airway epithelial glycoproteins in CF contributes to both the chronic infection and the robust, but ineffective, inflammatory response in the CF lung. Since the glycosylation phenotype of CF airway epithelial cells have been modulated by the expression of wtCFTR, the hypotheses which have been proposed to relate altered function of CFTR to the regulation of the glycosyltransferases are discussed. Understanding the effects of mutant CFTR on glycosylation may provide further insight into the regulation of glycoconjugate processing as well as new approaches to the therapy of CF.

Original languageEnglish (US)
Pages (from-to)649-659
Number of pages11
JournalGlycoconjugate Journal
Issue number9
StatePublished - Sep 1 2001
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology


  • Airway epithelial cells
  • CFTR
  • CFTR transfection
  • Cystic fibrosis
  • Fucose
  • Glycosylation
  • Sialic acid


Dive into the research topics of 'Terminal glycosylation in cystic fibrosis (CF): A review emphasizing the airway epithelial cell'. Together they form a unique fingerprint.

Cite this