Abstract:
:Abnormal retention of Delta F508 CFTR (cystic fibrosis transmembrane conductance regulator) in the endoplasmic reticulum is a major cause of cystic fibrosis (CF). We show that calnexin Delta 185-520 but not calnexin can partially reverse the mislocalization of Delta F508 CFTR. This 256-amino acid protein has neither the transmembrane domain nor the P domain of calnexin. Calnexin Delta 185-520 interacted with CFTR directly, and was secreted into the extracellular compartment over time. Forty-eight hours after transfection into CHO cells, calnexin Delta 185-520 increased the conversion of immature Delta F508 CFTR into mature Delta F508 CFTR. In immortalized human CF cell lines expressing Delta F508 CFTR, a halide efflux assay showed that calnexin Delta 185-520 partially restored CFTR function. These data indicate that calnexin Delta 185-520 may give a clue to develop the therapeutic way of cystic fibrosis with Delta F508 CFTR.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Okiyoneda T,Wada I,Jono H,Shuto T,Yoshitake K,Nakano N,Nagayama S,Harada K,Isohama Y,Miyata T,Kai Hdoi
10.1016/s0014-5793(02)03134-4keywords:
subject
Has Abstractpub_date
2002-08-28 00:00:00pages
87-92issue
1-3eissn
0014-5793issn
1873-3468pii
S0014579302031344journal_volume
526pub_type
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