ABCMdb

PMID: 14596935

Owsianik G, Cao L, Nilius B
Rescue of functional DeltaF508-CFTR channels by co-expression with truncated CFTR constructs in COS-1 cells.
FEBS Lett. 2003 Nov 6;554(1-2):173-8., [PubMed]

Sentences

No. Mutations Sentence Comment

33 ABCC7 p.Arg555Lys ABCC7 p.Arg516Lys ABCC7 p.Arg29Lys The base pair substitutions (underlined) were introduced using following oligonucleotides: for R29K mutation: 5P-GAAAGGATACAAACAGC- GCCTGGA (sense) and 5P-TCCAGGCGCTGTTTGTATCCTTTC (antisense); for R516K mutation: 5P-CTATGATGAATATAAATA- CAGAAGCGTC (sense) and 5P-GACGCTTCTGTATTTATATTC- ATCATAG (antisense); for R555K mutation: 5P-GGTCAACGAG- CAAAAATTTCTTTAGC (sense) and 5P-GCTAAAGAAATTTT- TGCTCGTTGACC (antisense). Login to comment 93 ABCC7 p.Arg555Lys ABCC7 p.Arg516Lys Co-expression of vF508-CFTR with mutated constructs, possessing R516K and R555K mutations either alone or in combination, led to an about two-fold decrease of vF508-CFTR-dependent current when compared to cells that co-expressed vF508-CFTR and WF2 (Table 1). Login to comment 95 ABCC7 p.Arg29Lys Surprisingly, the R29K mutation did not signi'cantly a&#a1;ect the rescuing properties of WF1 as well as WF2 (Table 1), suggesting the presence of another retention/retrieval motif in the N-terminal tail of CFTR. Login to comment 97 ABCC7 p.Arg555Lys The RR2 construct is identical to RR1 except for the presence of R516K and R555K mutations in RXRs. Login to comment 126 ABCC7 p.Trp1282* This is at variance with previously published reports, which showed that similar CFTR truncates can function as cAMP-activated chloride channels in Xenopus oocytes [29,37,38] and IB3-1 cells [29], a human bronchial epithelial cell line derived from a CF patient compound heterozygous for the vF508 mutation (vF508/W1282X) [39]. Login to comment 133 ABCC7 p.Arg555Lys ABCC7 p.Arg516Lys Arginine-to- lysine mutation in NBD1`s RXRs of truncated CFTR constructs (R516K and R555K mutations) strongly impairs their vF508-CFTR rescue properties. Login to comment 153 ABCC7 p.Arg553Gln ABCC7 p.Arg553Met The fact that second-site mutations in NBD1 of vF508-CFTR partially correct processing and functional defects of this mutant channel strongly supports this latter hypothesis (note that R553Q and R553M mutations correspond to the arginine in the RAR motif) [16^18]. Login to comment