Glycosylation and the cystic fibrosis transmembrane conductance regulator

Thomas F. Scanlin, Mary Catherine Glick

Research output: Contribution to journalArticle

12 Scopus citations

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 ΔF508 CFTR. The significance of the glycosylation will be known when endogenous CFTR from primary human tissue is examined.

Original languageEnglish (US)
Pages (from-to)276-279
Number of pages4
JournalRespiratory Research
Volume2
Issue number5
DOIs
StatePublished - Dec 1 2001

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All Science Journal Classification (ASJC) codes

  • Pulmonary and Respiratory Medicine

Keywords

  • Oligosaccharides
  • Polylactosamine
  • ΔF508 cystic fibrosis transmembrane conductance regulator (CFTR)

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