ArticlePloS one2016
Analysis of the Proteolytic Processing of ABCA3: Identification of Cleavage Site and Involved Proteases.
Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed.
- Lentiviral-mediated gene complementation to rescue pathogenic ABCA3 variants.American journal of respiratory cell and molecular biology · 2026Article
- Lentiviral-mediated gene complementation rescues pathogenicbioRxiv : the preprint server for biology · 2025Article
- Cyclosporine A in children with ABCA3 deficiency.Pediatric pulmonology · 2024Article
- Structure of a dimeric full-length ABC transporter.Nature communications · 2024Article
- ABCA3 Deficiency-Variant-Specific Response to Hydroxychloroquine.International journal of molecular sciences · 2023Article
- Quantifying Functional Impairment ofInternational journal of molecular sciences · 2023Article
- Cryo-EM structures of the human surfactant lipid transporter ABCA3.Science advances · 2022Article
- Functional characterization of four ATP-binding cassette transporter A3 gene (ABCA3) variants.Human mutation · 2020Article
- Potentiation of ABCA3 lipid transport function by ivacaftor and genistein.Journal of cellular and molecular medicine · 2019Article
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
rationaleABCA3 is a lipid transporter in the limiting membrane of lamellar bodies in alveolar type II cells. Mutations in the ABCA3 gene cause respiratory distress syndrome in new-borns and childhood interstitial lung disease. ABCA3 is N-terminally cleaved by an as yet unknown protease, a process believed to regulate ABCA3 activity.
methodsThe exact site where ABCA3 is cleaved was localized using mass spectrometry (MS). Proteases involved in ABCA3 processing were identified using small molecule inhibitors and siRNA mediated gene knockdown. Results were verified by in vitro digestion of a synthetic peptide substrate mimicking ABCA3's cleavage region, followed by MS analysis.
resultsWe found that cleavage of ABCA3 occurs after Lys174 which is located in the proteins' first luminal loop. Inhibition of cathepsin L and, to a lesser extent, cathepsin B resulted in attenuation of ABCA3 cleavage. Both enzymes showed activity against the ABCA3 peptide in vitro with cathepsin L being more active.
conclusionWe show here that, like some other proteins of the lysosomal membrane, ABCA3 is a substrate of cathepsin L. Therefore, cathepsin L may represent a potential target to therapeutically influence ABCA3 activity in ABCA3-associated lung disease.
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