Altered terminal glycosylation and the pathophysiology of CF lung disease

Andrew D Rhim; Lidia I Stoykova; Arvind J Trindade; Mary Catherine Glick; Thomas F Scanlin

doi:10.1016/j.jcf.2004.05.021

Altered terminal glycosylation and the pathophysiology of CF lung disease

J Cyst Fibros. 2004 Aug:3 Suppl 2:95-6. doi: 10.1016/j.jcf.2004.05.021.

Authors

Andrew D Rhim¹, Lidia I Stoykova, Arvind J Trindade, Mary Catherine Glick, Thomas F Scanlin

Affiliation

¹ 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.

PMID: 15463936
DOI: 10.1016/j.jcf.2004.05.021

Abstract

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.

Publication types

Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.

MeSH terms

Cystic Fibrosis / genetics
Cystic Fibrosis / metabolism*
Cystic Fibrosis / physiopathology*
Cystic Fibrosis Transmembrane Conductance Regulator / biosynthesis
Cystic Fibrosis Transmembrane Conductance Regulator / genetics*
Epithelial Cells / metabolism
Glycosylation
Humans
Mutation
Respiratory Mucosa / metabolism*
Respiratory Mucosa / physiopathology

Substances

CFTR protein, human
Cystic Fibrosis Transmembrane Conductance Regulator

Grants and funding

DK-07748/DK/NIDDK NIH HHS/United States