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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
41
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pubmed:dateCreated |
1994-11-17
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pubmed:abstractText |
Mutant (delta F508) and wild-type cystic fibrosis transmembrane conductance regulator (CFTR) were synthesized initially as an approximately 140-kDa core-glycosylated precursor, which, in the case of wild-type CFTR, was chased to an approximately 160 kDa form bearing complex oligosaccharides. Mutant CFTR disappeared from the detergent-soluble cell extract with rapid (t1/2 = 27 min) kinetics. Only approximately 25% of the initially synthesized wild-type 140-kDa CFTR precursor was detected as mature protein; the remaining approximately 75% decayed with kinetics (t1/2 = 33 min) indistinguishable from those of the mutant. Rapid degradation kinetics and inefficient processing of wild-type CFTR were also observed in the colonic carcinoma lines HT29 and T84 and in stably transfected C127 cells, which express 5-50 times lower levels of CFTR. These results suggest that inefficient processing and rapid degradation of wild-type CFTR precursor are an intrinsic property of CFTR in these diverse cell types and are not an artifact of overexpression. Degradation of wild-type and mutant 140-kDa CFTR began without significant lag following synthesis. These data suggest that wild-type and delta F508 CFTR differ in the efficiency of folding of the core-glycosylated primary translation product.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
14
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pubmed:volume |
269
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
25710-8
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:7523390-Amino Acid Sequence,
pubmed-meshheading:7523390-Brefeldin A,
pubmed-meshheading:7523390-Carcinoma,
pubmed-meshheading:7523390-Cell Compartmentation,
pubmed-meshheading:7523390-Colonic Neoplasms,
pubmed-meshheading:7523390-Cyclopentanes,
pubmed-meshheading:7523390-Cystic Fibrosis,
pubmed-meshheading:7523390-Cystic Fibrosis Transmembrane Conductance Regulator,
pubmed-meshheading:7523390-Endoplasmic Reticulum,
pubmed-meshheading:7523390-Glycosylation,
pubmed-meshheading:7523390-Humans,
pubmed-meshheading:7523390-Membrane Proteins,
pubmed-meshheading:7523390-Molecular Sequence Data,
pubmed-meshheading:7523390-Mutation,
pubmed-meshheading:7523390-Protein Biosynthesis,
pubmed-meshheading:7523390-Protein Folding,
pubmed-meshheading:7523390-Protein Precursors,
pubmed-meshheading:7523390-Protein Processing, Post-Translational,
pubmed-meshheading:7523390-Protein Synthesis Inhibitors,
pubmed-meshheading:7523390-Recombinant Proteins,
pubmed-meshheading:7523390-Transfection,
pubmed-meshheading:7523390-Tumor Cells, Cultured
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pubmed:year |
1994
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pubmed:articleTitle |
Intracellular turnover of cystic fibrosis transmembrane conductance regulator. Inefficient processing and rapid degradation of wild-type and mutant proteins.
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pubmed:affiliation |
Department of Biological Sciences, Stanford University, California 94305-5020.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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