title: CFTR protein analysis of splice site mutation 2789+5 G-A.
abstract: Ex vivo biochemical analysis of rectal biopsies of a carrier of the mild 2789+5 G-A CFTR frameshift splice site mutation revealed mutant truncated CFTR of expected size and an imbalance of more core-glycosylated and less mature full-length CFTR. This first immunoblot analysis of a non-F508del CFTR mutant protein derived from human tissue demonstrates that splice site mutations should not only be investigated at the mRNA, but also at the protein level to properly interpret the associations between genotype, molecular pathology and disease.
authors: Department of Pediatric Pneumology and Neonatology, OE 6710, Medizinische Hochschule Hannover, D30625 Hannover, Germany.
authors: Andrea
authors: A
authors: van Barneveld
authors: Frauke
authors: F
authors: Stanke
authors: Andreas
authors: A
authors: Claass
authors: Manfred
authors: M
authors: Ballmann
authors: Burkhard
authors: B
authors: Tümmler
mesh_terms: D001706:Biopsy; D002648:Child; D003550:Cystic Fibrosis / Q000235:genetics* / Q000378:metabolism / Q000473:pathology; D019005:Cystic Fibrosis Transmembrane Conductance Regulator / Q000235:genetics* / Q000378:metabolism; D004252:DNA Mutational Analysis / Q000379:methods; D005838:Genotype; D006801:Humans; D015151:Immunoblotting; D008297:Male; D009154:Mutation; D012333:RNA, Messenger / Q000032:analysis / Q000235:genetics*; D012007:Rectum / Q000378:metabolism / Q000473:pathology
chemical_list: C505032:CFTR protein, human; D012333:RNA, Messenger; D019005:Cystic Fibrosis Transmembrane Conductance Regulator