ABCA3 p.Asn140Gln
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PMID: 24142515
[PubMed]
Beers MF et al: "Disruption of N-linked glycosylation promotes proteasomal degradation of the human ATP-binding cassette transporter ABCA3."
No.
Sentence
Comment
47
The primers [primer nucleotide sequence is obtained from the National Center for Biotechnology (NCBI) of human ABCA3, data accession number NM_001089] generated for these mutant constructs are as follows: for N53Q: forward, 5=-tcggaaaatgtgccccaggccaccatctacccg-3=, reverse, 5=-cgggtagatggtggcctggggcacattttccga-3=; for N124Q: forward, 5=-ctacattaggtacgaccagtgctcgtccagcgtgc-3=, reverse, 5=-gcacgctggacgag- cactggtcgtacctaatgtag-3=; for N140Q, forward, 5=-tcgagcaccccttccagca- cagcaaggagcc-3=, reverse, 5=-ggctccttgctgtgctggaaggggtgctcga-3=, and for N945Q: forward, 5=-ccctcctggccatccagtactcctcggagct-3=, reverse, 5=- agctccgaggagtactggatggccaggaggg-3=.
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ABCA3 p.Asn140Gln 24142515:47:436
status: NEW122 Since data obtained thus far suggested that glycosylation takes place at N124 and N140, but not at N53, we next generated a double mutant construct containing both N124Q and N140Q mutations.
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ABCA3 p.Asn140Gln 24142515:122:174
status: NEW139 M.W., molecular weight. double mutant (N124Q and N140Q) was distributed in both calnexin (ER)- and CD63-positive compartments, suggestive of alterations in anterograde trafficking of ABCA3 caused by the absence of glycosylation at residues 124 and 140.
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ABCA3 p.Asn140Gln 24142515:139:50
status: NEW153 As was observed in epithelial cell lines, immunoblot analysis of primary human AT2 cells revealed increased electrophoretic mobility of the primary translation products of single and double mutants of N124Q and N140Q but not the single mutant of N53Q (Fig. 7A).
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ABCA3 p.Asn140Gln 24142515:153:211
status: NEW179 Furthermore, the N124Q, N140Q, and N124Qaf9;N140Q substitutions all resulted in reduced total ABCA3 protein expression.
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ABCA3 p.Asn140Gln 24142515:179:24
status: NEW190 Second, the immunoblot bands of single and double mutants of N124Q and N140Q supports the notion that the prominent changes in molecular weights (compared with WT ABCA3) are likely due to the absence of large sugar moiety and not due to the replacement of a single amino acid.
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ABCA3 p.Asn140Gln 24142515:190:71
status: NEW236 As Fig. 5 shows, the level of expression of single glycosylation mutants (N124Q; N140Q) are highly susceptible to MG132 treatment, indicating that as many as half of the glycosylation-deficient isoforms are susceptible to proteasomal degradation.
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ABCA3 p.Asn140Gln 24142515:236:81
status: NEW