Altered terminal glycosylation and the pathophysiology of CF lung disease.
Altered terminal glycosylation, with increased fucosylation and decreased sialylation, is a hallmark of the cystic fibrosis (CF) glycosylation phenotype. The glycosylation phenotype of CF airway epithelial cells has been modulated by the expression of wtCFTR. 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.
Cystic Fibrosis Center and Department of Pediatrics, Children's Hospital of Philadelphia and University of Pennsylvania School of Medicine, ARB 402, 34th and Civic Center Blvd., Philadelphia, PA 19104, USA.
Andrew D
AD
Rhim
Lidia I
LI
Stoykova
Arvind J
AJ
Trindade
Mary Catherine
MC
Glick
Thomas F
TF
Scanlin
D003550:Cystic Fibrosis / Q000235:genetics / Q000378:metabolism* / Q000503:physiopathology*; D019005:Cystic Fibrosis Transmembrane Conductance Regulator / Q000096:biosynthesis / Q000235:genetics*; D004847:Epithelial Cells / Q000378:metabolism; D006031:Glycosylation; D006801:Humans; D009154:Mutation; D020545:Respiratory Mucosa / Q000378:metabolism* / Q000503:physiopathology
C505032:CFTR protein, human; D019005:Cystic Fibrosis Transmembrane Conductance Regulator