Induction of HSP70 promotes ΔF508 CFTR trafficking

Lee R. Choo-Kang, Pamela L. Zeitlin

Research output: Contribution to journalReview articlepeer-review


The ΔF508 cystic fibrosis transmembrane conductance regulator (CFTR) is a temperature-sensitive trafficking mutant that is detected as an immature 160-kDa form (band B) in gel electrophoresis. The goal of this study was to test the hypothesis that HSP70, a member of the 70-kDa heat shock protein family, promotes ΔF508 CFTR processing to the mature 180-kDa form (band C). Both pharmacological and genetic techniques were used to induce HSP70. IB3-1 cells were treated with sodium 4-phenylbutyrate (4PBA) to promote maturation of ΔF508 CFTR to band C. A dose-dependent increase in band C and total cellular HSP70 was observed. Under these conditions, HSP70-CFTR complexes were increased and 70-kDa heat shock cognate protein-CFTR complexes were decreased. Increased ΔF508 CFTR maturation was also seen after transfection with an HSP70 expression plasmid and exposure to glutamine, an inducer of HSP70. With immunofluorescence techniques, the increased appearance of CFTR band C correlated with CFTR distribution beyond the perinuclear regions. These data suggest that induction of HSP70 promotes ΔF508 CFTR maturation and trafficking.

Original languageEnglish (US)
Pages (from-to)L58-L68
JournalAmerican Journal of Physiology - Lung Cellular and Molecular Physiology
Issue number1 25-1
StatePublished - 2001


  • 70-Kilodalton heat shock protein chaperones
  • Cystic fibrosis
  • Cystic fibrosis transmembrane conductance regulator
  • Glutamine
  • Phenylbutyrate
  • Plasmid transfection

ASJC Scopus subject areas

  • Physiology
  • Pulmonary and Respiratory Medicine
  • Physiology (medical)
  • Cell Biology


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