Altered protein folding may be the molecular basis of most cases of cystic fibrosis

Philip J. Thomas, Young H. Ko, Peter L. Pedersen

Research output: Contribution to journalArticle

Abstract

Experiments have demonstrated that the cystic fibrosis transmembrane conductance regulator protein (CFTR), containing the most common cystic fibrosis (CF)-causing mutation (ΔF508), reaches the plasma membrane in reduced amounts. Studies of a peptide model of CFTR indicate that the ΔF508 mutated region is more sensitive to denaturating conditions. This paper proposes that altered protein folding accounts for these findings, and, thus, most cases of CF. Significantly, the hypothesis makes specific predictions about the effect of stabilizing conditions on mutant CFTR, and, further, suggests a new class of pharmaceuticals that may prove effective in the treatment of this important genetic disease.

Original languageEnglish (US)
Pages (from-to)7-9
Number of pages3
JournalFEBS Letters
Volume312
Issue number1
DOIs
StatePublished - Nov 2 1992

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Keywords

  • Cystic fibrosis
  • Cystic fibrosis transmembrane conductance regulator (CFTR)
  • Genetic disease
  • Protein folding

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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