Journal
FEBS LETTERS
Volume 526, Issue 1-3, Pages 87-92Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/S0014-5793(02)03134-4
Keywords
cystic fibrosis; cystic fibrosis transmembrane conductance regulator; calnexin; endoplasmic reticulum
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Abnormal retention of DeltaF508 CFTR (cystic fibrosis transmembrane conductance regulator) in the endoplasmic reticulum is a major cause of cystic fibrosis (CF). We show that calnexin Delta185-520 but not calnexin can partially reverse the mislocalization of DeltaF508 CFTR. This 256-amino acid protein has neither the transmembrane domain nor the P domain of calnexin. Calnexin Delta185-520 interacted with CFTR directly, and was secreted into the extracellular compartment over time. Forty-eight hours after transfection into CHO cells, calnexin Delta185-520 increased the conversion of immature DeltaF508 CFTR into mature DeltaF508 CFTR. In immortalized human CF cell lines expressing DeltaF508 CFTR, a halide efflux assay showed that calnexin Delta185-520 partially restored CFTR function. These data indicate that calnexin Delta185-520 may give a clue to develop the therapeutic way of cystic fibrosis with DeltaF508 CFTR. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
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