Journal article
Dysfunction of CFTR bearing the delta F508 mutation
Journal of cell science., Vol.1993(Suppl 17), pp.235-239
1993
DOI: 10.1242/jcs.1993.Supplement_17.33
PMID: 7511616
Abstract
The cystic fibrosis transmembrane conductance regulator (CFTR) is mutated in patients with cystic fibrosis (CF). The most common CF-associated mutation is deletion of phenylalanine at residue 508, CFTR delta F508. When expressed in heterologous cells, CFTR bearing the delta F508 mutation fails to progress through the normal biosynthetic pathway and fails to traffic to the plasma membrane. As a result, CFTR delta F508 is mislocalized and is not present in the apical membrane of primary cultures of airway epithelia. Consequently, the apical membrane of CF airway epithelia is Cl- -impermeable, a defect that probably contributes to the pathogenesis of the disease.
Details
- Title: Subtitle
- Dysfunction of CFTR bearing the delta F508 mutation
- Creators
- Michael J Welsh - University of Iowa, Internal MedicineGerene M Denning - University of Iowa, Emergency MedicineLynda S Ostedgaard - University of Iowa, Internal MedicineMatthew P Anderson - University of Iowa
- Resource Type
- Journal article
- Publication Details
- Journal of cell science., Vol.1993(Suppl 17), pp.235-239
- DOI
- 10.1242/jcs.1993.Supplement_17.33
- PMID
- 7511616
- NLM abbreviation
- J Cell Sci
- ISSN
- 0021-9533
- eISSN
- 1477-9137
- Publisher
- Company of Biologists
- Language
- English
- Date published
- 1993
- Academic Unit
- Neurology; Molecular Physiology and Biophysics; Pulmonary, Critical Care, and Occupational Medicine; Emergency Medicine; Fraternal Order of Eagles Diabetes Research Center; Neurosurgery; Internal Medicine
- Record Identifier
- 9984203345802771
Metrics
11 Record Views