Abstract:
:In order to get a better insight into the function of amino acid residues located in the second transmembrane domain of the cystic fibrosis transmembrane conductance regulator (CFTR) protein, all exon 18 mutations found in cystic fibrosis (CF) patients were characterized at the protein and at the electrophysiological level. Of the different mutations present in transmembrane helix 12 (M1137V, M1137R, I11139V and deltaM1140), and the intracytoplasmic loop connecting TM12 and NBD2 (D1152H and D1154G), only M1137R interfered with the proper maturation of the protein. Permeability studies performed after injection of the different wild-type and mutant cRNAs in Xenopus laevis oocytes indicated that the mutations did not alter the permeability sequence of the CFTR channels. The whole cell cAMP activated chloride currents, however, were significantly reduced for M1137V, I1139V, D1152H and D1154G and close to zero for deltaM1140, indicating that these mutations interfere with the proper gating of the chloride channels.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Vankeerberghen A,Wei L,Teng H,Jaspers M,Cassiman JJ,Nilius B,Cuppens Hdoi
10.1016/s0014-5793(98)01042-4subject
Has Abstractpub_date
1998-10-16 00:00:00pages
1-4issue
1-2eissn
0014-5793issn
1873-3468pii
S0014-5793(98)01042-4journal_volume
437pub_type
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