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Corrigendum Free access | 10.1172/jci.insight.128935

Thymosin α-1 does not correct F508del-CFTR in cystic fibrosis airway epithelia

Valeria Tomati, Emanuela Caci, Loretta Ferrera, Emanuela Pesce, Elvira Sondo, Deborah M. Cholon, Nancy L. Quinney, Susan E. Boyles, Andrea Armirotti, Roberto Ravazzolo, Luis J.V. Galietta, Martina Gentzsch, and Nicoletta Pedemonte

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Published April 4, 2019 - More info

Published in Volume 4, Issue 7 on April 4, 2019
JCI Insight. 2019;4(7):e128935. https://doi.org/10.1172/jci.insight.128935.
© 2019 American Society for Clinical Investigation
Published April 4, 2019 - Version history
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Related article:

Thymosin α-1 does not correct F508del-CFTR in cystic fibrosis airway epithelia
Valeria Tomati, … , Martina Gentzsch, Nicoletta Pedemonte
Valeria Tomati, … , Martina Gentzsch, Nicoletta Pedemonte
Thymosin α-1 is devoid of activity on mutant CFTR anion channel as well as on the calcium-activated chloride channel, in contrast to previous reports.
Research Article Therapeutics

Thymosin α-1 does not correct F508del-CFTR in cystic fibrosis airway epithelia

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Abstract

In cystic fibrosis (CF), deletion of phenylalanine 508 (F508del) in the cystic fibrosis transmembrane conductance regulator (CFTR) anion channel causes misfolding and premature degradation. Considering the numerous effects of the F508del mutation on the assembly and processing of CFTR protein, combination therapy with several pharmacological correctors is likely to be required to treat CF patients. Recently, it has been reported that thymosin α-1 (Tα-1) has multiple beneficial effects that could lead to a single-molecule-based therapy for CF patients with F508del. Such effects include suppression of inflammation, improvement in F508del-CFTR maturation and gating, and stimulation of chloride secretion through the calcium-activated chloride channel (CaCC). Given the importance of such a drug, we aimed to characterize the underlying molecular mechanisms of action of Tα-1. In-depth analysis of Tα-1 effects was performed using well-established microfluorimetric, biochemical, and electrophysiological techniques on epithelial cell lines and primary bronchial epithelial cells from CF patients. The studies, which were conducted in 2 independent laboratories with identical outcome, demonstrated that Tα-1 is devoid of activity on mutant CFTR as well as on CaCC. Although Tα-1 may still be useful as an antiinflammatory agent, its ability to target defective anion transport in CF remains to be further investigated.

Authors

Valeria Tomati, Emanuela Caci, Loretta Ferrera, Emanuela Pesce, Elvira Sondo, Deborah M. Cholon, Nancy L. Quinney, Susan E. Boyles, Andrea Armirotti, Roberto Ravazzolo, Luis J.V. Galietta, Martina Gentzsch, Nicoletta Pedemonte

×

Original citation: JCI Insight. 2018;3(3):e98699. https://doi.org/10.1172/jci.insight.98699

Citation for this corrigendum: JCI Insight. 2019;4(7):e128935. https://doi.org/10.1172/jci.insight.128935

The unit for the concentration of peptide in the proliferation study was incorrectly reported in the Results and Methods sections and the Figure 4 legend. The corrected sentences, with sections indicated, are below.

Results

Evaluation of Tα-1 sequence and its effect on proliferation and apoptosis of MCF-7 breast cancer cells.

Therefore, we plated MCF-7 at low density on 96-well plates suitable for confocal high-content imaging and evaluated cell proliferation for 72 hours following treatment with Tα-1 (100 μM) or scrambled peptide (100 μM).

Methods

Proliferation study.

MCF-7 cells were plated at low density (10,000 cells/well) on 96-well plates suitable for high-content imaging. After 6 hours, cells were treated with the scrambled peptide (100 μM) or with Tα-1 (100 μM).

Figure 4 legend

(A) Dot plot showing proliferation of MCF-7 cells after 72-hour treatment with Tα-1 (100 μM) or scrambled peptide (100 μM, control). (B) Dot plot showing the number of apoptotic MCF-7 cells after 72-hour treatment with Tα-1 (100 μM) or scrambled peptide (100 μM, control).

The article has been updated to reflect these changes.

The authors regret the errors.

Footnotes

See the related article at Thymosin α-1 does not correct F508del-CFTR in cystic fibrosis airway epithelia.

Version history
  • Version 1 (April 4, 2019): Electronic publication

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