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• W2147502668 abstract "The cystic fibrosis gene encodes the cystic fibrosis transmembrane conductance regulator (CFTR) protein whicha is a 1480 amino acid, glycosylated membrane protein that functions as a cAMP-dependent chloride (Cl−) channel. It is mainly expressed in secretory epithelia. The F508del-CFTR protein, resultant from the mutant gene found in 70% of CF chromosomes, is aberrantly folded, mostly blocked for maturation and degraded in the ER by the ubiquitin proteosome pathway. This mutant still functions as a cAMP-dependent Cl− channel to some degree if the protein is directed to the plasma membrane by some strategy that corrects its cellular location. The properties of wild-type and mutant CFTR proteins are studied extensively using different biochemical and biophysical approaches. Although these studies are being developed for more than 15 years, many dark areas in the research field of CFTR protein still need to be unmasked. For example, the production of specific anti-CFTR antibodies was one of the main problems for Western immunoprecipitation and immunocytochemistry experiments. Today, the evaluation of existing antibodies shows that only few anti-CFTR antibodies are suitable for native tissue analysis, but several can be used for cell line experiments. The applicability of existing anti-CFTR antibodies is discussed here [[1]Mendes F. Farinha C.M. Roxo-Rosa M. Fanen P. Edelman A. Dormer R.L. et al.Antibodies for CFTR studies.J. Cyst. Fibros. 2004; 3: 69-72Abstract Full Text Full Text PDF PubMed Scopus (35) Google Scholar], as well as the basic biochemical techniques that are currently used for the study of CFTR protein produced in vivo [[2]Farinha C.M. Penque D. Roxo-Rosa M. Lukacs G. Dormer R.L. McPherson M. et al.Biochemical methods to assess CFTR expression and membrane localization.J. Cyst. Fibros. 2004; 3: 73-77Abstract Full Text Full Text PDF PubMed Scopus (45) Google Scholar] and the techniques for its in vitro study [[3]Benos D.J. Berdiev B.K. Ismailov I.I. Ostedgaard L. Kogan I. Li C. et al.Methods to study CFTR protein in vitro.J. Cyst. Fibros. 2004; 3: 79-83Abstract Full Text Full Text PDF PubMed Scopus (6) Google Scholar]. New studies based on proteomic approaches are reviewed here [[4]Roxo-Rosa M. Davezac N. Bensalem N. Majumder M. Heda G.D. Simas A. et al.Proteomics techniques for cystic fibrosis research.J. Cyst. Fibros. 2004; 3: 85-89Abstract Full Text Full Text PDF PubMed Scopus (16) Google Scholar]. These are being developed to get insights on proteins differentially expressed in CF versus non-CF cells/tissues or on proteins interacting with CFTR/F508del-CFTR that may be involved in the traffic/degradation and or activity of CFTR/F508del-CFTR. The recent elucidation of murine CFTR nucleotide binding domain 1 (NBD1) called for a discussion and review of the CFTR structural aspects [[5]Dorwart M. Thibodeau P. Thomas P. Cystic fibrosis: recent structural insights.J. Cyst. Fibros. 2004; 3: 91-94Abstract Full Text Full Text PDF PubMed Scopus (12) Google Scholar]. The role of normal and mutant CFTR on the glycosylation pattern of other proteins and its consequences for host–bacterial interactions in the light of recently published data are also discussed in this section [[6]Rhim A.D. Stoykova L.I. Trindade A.J. Glick M.C. Scanlin T.F. Altered terminal glycosylation and the pathophysiology of CF lung disease.J. Cyst. Fibros. 2004; 3: 95-96Abstract Full Text Full Text PDF PubMed Scopus (21) Google Scholar]. Novel insights on lipidic alterations in CF and possible consequences for CF deserve our attention and are also reported from a methodological point of view [[7]Ollero M. Methods for the study of lipid metabolites in cystic fibrosis.J. Cyst. Fibros. 2004; 3: 97-98Abstract Full Text Full Text PDF PubMed Scopus (3) Google Scholar]. We believe that we were able to gather in this section (often as authors in one joint manuscript) key groups in each subarea dealt with. All articles are outlines/reviews of various protocols available at the European Working Group on CFTR Expression website [[8]European Working Group on CFTR ExpressionThe Online Virtual Repository of Methods and Reagents for CFTR Expression and Functional Studies (section C).2004Google Scholar] that should be used extensively as supplementary material. Our aim was to provide a series of methodologies that hopefully will be useful to the novice and experienced researcher alike by reducing effort and research time of all with an interest in this field." @default.
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• W2147502668 date "2004-08-01" @default.
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• W2147502668 title "General introduction to section C: Biochemistry and Biophysics of CFTR" @default.
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• W2147502668 doi "https://doi.org/10.1016/j.jcf.2004.05.015" @default.
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