title: Glycosylation and the cystic fibrosis transmembrane conductance regulator.
abstract: The cystic fibrosis transmembrane conductance regulator (CFTR) has been known for the past 11 years to be a membrane glycoprotein with chloride channel activity. Only recently has the glycosylation of CFTR been examined in detail, by O'Riordan et al in Glycobiology. Using cells that overexpress wild-type (wt)CFTR, the presence of polylactosamine was noted on the fully glycosylated form of CFTR. In the present commentary the results of that work are discussed in relation to the glycosylation phenotype of cystic fibrosis (CF), and the cellular localization and processing of DeltaF508 CFTR. The significance of the glycosylation will be known when endogenous CFTR from primary human tissue is examined.
authors.affiliation: Cystic Fibrosis Center and Department of Pediatrics, Abramson Pediatric Research Center, Children's Hospital of Philadelphia, 3615 Civic Center Blvd., Philadelphia, PA 19104-4318, USA. scanlin@email.chop.edu
authors.forename: T F
authors.initials: TF
authors.lastname: Scanlin
authors.forename: M C
authors.initials: MC
authors.lastname: Glick
mesh_terms: D000818:Animals; D019005:Cystic Fibrosis Transmembrane Conductance Regulator / Q000096:biosynthesis*; D006031:Glycosylation; D006801:Humans; D009844:Oligosaccharides / Q000502:physiology
chemical_list: C505032:CFTR protein, human; D009844:Oligosaccharides; D019005:Cystic Fibrosis Transmembrane Conductance Regulator