tailieunhanh - Báo cáo y học: " Glycosylation and the cystic fibrosis transmembrane conductance regulator"

Tuyển tập các báo cáo nghiên cứu về y học được đăng trên tạp chí y học 'Respiratory Research cung cấp cho các bạn kiến thức về ngành y đề tài: " Glycosylation and the cystic fibrosis transmembrane conductance regulator. | Available online http content 2 5 276 Commentary Glycosylation and the cystic fibrosis transmembrane conductance regulator Thomas F Scanlin and Mary Catherine Glick Cystic Fibrosis Center and Department of Pediatrics Children s Hospital of Philadelphia and the University of Pennsylvania School of Medicine Abramson Pediatric Research Center Philadelphia Pennsylvania USA Correspondence Thomas F Scanlin MD Children s Hospital of Philadelphia Abramson Pediatric Research Center 3615 Civic Center Blvd Room 402 Philadelphia PA 19104-4318 USA. Tel 1 215 590 3608 fax 1 215 590 4298 e-mail scanlin@ Received 30 May 2001 Revisions requested 13 June 2001 Revisions received 22 June 2001 Accepted 27 June 2001 Published 7 August 2001 Respir Res 2001 2 276-279 2001 BioMed Central Ltd Print ISSN 1465-9921 Online ISSN 1465-993X Abstract 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 et al in Glycobiology. 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 AF508 CFTR. The significance of the glycosylation will be known when endogenous CFTR from primary human tissue is examined. Keywords AF508 cystic fibrosis transmembrane conductance regulator CFTR oligosaccharides polylactosamine Introduction Interest in glycosylation has been rekindled in the field of CF research since the identification of the CF gene which encodes the CFTR membrane glycoprotein 1 . The renewed interest has been stimulated by recent developments resulting from attempts to reconcile the proposed function of CFTR with phenomena that are