ArticlePloS one2010
Vacuolar ATPase regulates surfactant secretion in rat alveolar type II cells by modulating lamellar body calcium.
Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 33 citations in OpenAlex.
- Maturation stage-specific V-ATPase disassembly explains the neutral pH of mature mucocyst lysosome-related organelles in Tetrahymena thermophila.Journal of cell science · 2025Article
- Acidic Enough for a Healthy Breath.American journal of respiratory cell and molecular biology · 2024Article
- Article
- Novel opportunities from bioimaging to understand the trafficking and maturation of intracellular pulmonary surfactant and its role in lung diseases.Frontiers in immunology · 2023Review
- SARS-CoV-2 treatment effects induced by ACE2-expressing microparticles are explained by the oxidized cholesterol-increased endosomal pH of alveolar macrophages.Cellular & molecular immunology · 2022Article
- Review
- Adhesion-GPCR Gpr116 (ADGRF5) expression inhibits renal acid secretion.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- HJournal of bioenergetics and biomembranes · 2017Article
- Sustained treatment of sickle cell mice with haptoglobin increases HO-1 and H-ferritin expression and decreases iron deposition in the kidney without improvement in kidney function.British journal of haematology · 2016Article
- Oxidized Ferric and Ferryl Forms of Hemoglobin Trigger Mitochondrial Dysfunction and Injury in Alveolar Type I Cells.American journal of respiratory cell and molecular biology · 2016Article
- CaMKII inhibition in type II pneumocytes protects from bleomycin-induced pulmonary fibrosis by preventing Ca2+-dependent apoptosis.American journal of physiology. Lung cellular and molecular physiology · 2016Article
- Haptoglobin attenuates hemoglobin-induced heme oxygenase-1 in renal proximal tubule cells and kidneys of a mouse model of sickle cell disease.Blood cells, molecules & diseases · 2015Article
- MicroRNA-206 regulates surfactant secretion by targeting VAMP-2.FEBS letters · 2015Article
- Long-chain acyl-CoA dehydrogenase deficiency as a cause of pulmonary surfactant dysfunction.The Journal of biological chemistry · 2014Article
- Regulation of luminal acidification by the V-ATPase.Physiology (Bethesda, Md.) · 2013Review
- Surfactant phospholipid metabolism.Biochimica et biophysica acta · 2013Review
- Targeting reversible disassembly as a mechanism of controlling V-ATPase activity.Current protein & peptide science · 2012Review
- Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Lung surfactant reduces surface tension and maintains the stability of alveoli. How surfactant is released from alveolar epithelial type II cells is not fully understood. Vacuolar ATPase (V-ATPase) is the enzyme responsible for pumping H(+) into lamellar bodies and is required for the processing of surfactant proteins and the packaging of surfactant lipids. However, its role in lung surfactant secretion is unknown. Proteomic analysis revealed that vacuolar ATPase (V-ATPase) dominated the alveolar type II cell lipid raft proteome. Western blotting confirmed the association of V-ATPase a1 and B1/2 subunits with lipid rafts and their enrichment in lamellar bodies. The dissipation of lamellar body pH gradient by Bafilomycin A1 (Baf A1), an inhibitor of V-ATPase, increased surfactant secretion. Baf A1-stimulated secretion was blocked by the intracellular Ca(2+) chelator, BAPTA-AM, the protein kinase C (PKC) inhibitor, staurosporine, and the Ca(2+)/calmodulin-dependent protein kinase II (CaMKII), KN-62. Baf A1 induced Ca(2+) release from isolated lamellar bodies. Thapsigargin reduced the Baf A1-induced secretion, indicating cross-talk between lamellar body and endoplasmic reticulum Ca(2+) pools. Stimulation of type II cells with surfactant secretagogues dissipated the pH gradient across lamellar bodies and disassembled the V-ATPase complex, indicating the physiological relevance of the V-ATPase-mediated surfactant secretion. Finally, silencing of V-ATPase a1 and B2 subunits decreased stimulated surfactant secretion, indicating that these subunits were crucial for surfactant secretion. We conclude that V-ATPase regulates surfactant secretion via an increased Ca(2+) mobilization from lamellar bodies and endoplasmic reticulum, and the activation of PKC and CaMKII. Our finding revealed a previously unrealized role of V-ATPase in surfactant secretion.
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Registered trials
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