Terminal glycosylation in cystic fibrosis

Thomas F. Scanlin, Mary Catherine Glick

Research output: Contribution to journalReview articlepeer-review

80 Scopus citations


Cystic fibrosis (CF) is a common genetic disease for which the gene was identified within the last decade. Pulmonary disease predominates in this ultimately fatal disease and current therapy only slows the progression. CF transmembrane regulator (CFTR), the gene product, is an integral membrane glycoprotein that normally functions as a chloride channel in epithelial cells. The most common mutation, ΔF508, results in mislocalization and altered glycosylation of CFTR. Altered fucosylation and sialylation are hallmarks of both membrane and secreted glycoproteins in CF and the focus here is on these investigations. Oligosaccharides from CF membrane glycoproteins have the Lewis x, selectin ligand in terminal positions. In addition, two major bacterial pathogens in CF, Pseudomonas aeruginosa and Haemophilus influenzae, have binding proteins, which recognize fucose in α1,3 linkage and asialoglycoconjugates. We speculate that the altered terminal glycosylation of airway epithelial glycoproteins in CF contributes to the chronic infection and robust inflammatory response in the CF lung. Understanding the effects of mutant CFTR on glycosylation may provide further insight into the regulation of glycoconjugate processing as well as therapy for CF. Copyright (C) 1999 Elsevier Science B.V.

Original languageEnglish (US)
Pages (from-to)241-253
Number of pages13
JournalBiochimica et Biophysica Acta - Molecular Basis of Disease
Issue number2-3
StatePublished - Oct 8 1999
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Molecular Medicine
  • Molecular Biology


  • Cystic fibrosis
  • Cystic fibrosis transmembrane regulator
  • Glycosylation in cystic fibrosis
  • Terminal glycosylation


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