Glycosylation and the cystic fibrosis transmembrane conductance regulator

• Main Authors: Glick Mary Catherine, Scanlin Thomas F
• Format: Article
• Language: English
• Published: BMC 2001-08-01
• Series: Respiratory Research
• Subjects: ΔF508 cystic fibrosis transmembrane conductance regulator (CFTR); oligosaccharides; polylactosamine
• Online Access: http://respiratory-research.com/content/2/5/276

<p>Abstract</p> <p>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 <it>et al</it> in <it>Glycobiology</it>. 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.</p>