Data from: ATP13A2 is involved in intracellular polyamine transport in lung epithelial cells
Data files
Apr 09, 2026 version files 759.25 KB
-
ATP13A2overexpressionMOItitrationUncroppedimage.TIF
72.81 KB
-
EndogenousATP13A1and2matrixUncroppedimage.TIF
211.10 KB
-
EndogenousATP13A2inH441Uncroppedimage.TIF
121.52 KB
-
Mo-blue_OD660_20240217_223008_ATPaseactTimecourse_page1.csv
2.79 KB
-
Mo-blue_OD660_20240217_223008_ATPaseactTimecourse_page2.csv
1.73 KB
-
Mo-blue_OD660_20240313_145945_ATP13A2_page1.csv
2.67 KB
-
Mo-blue_OD660_20240313_145945_ATP13A2_page2.csv
1.73 KB
-
Mo-blue_OD660_20240313_145945_ATP13A2_page3.csv
316 B
-
Mo-blue_OD660_20240314_175736_Mock_page1.csv
2.07 KB
-
Mo-blue_OD660_20240314_175736_Mock_page2.csv
1.73 KB
-
Mock_vs_13A2.prism
81.06 KB
-
Polyamine_LCMSMS_20250411_20260409_page1.csv
3.06 KB
-
Polyamine_LCMSMS_20250411_20260409_page2.csv
807 B
-
Polyamine_LCMSMS_20250411_20260409_page3.csv
808 B
-
Polyamine_LCMSMS_20250411_20260409_page4.csv
808 B
-
Polyamine_LCMSMS_20250411_20260409_page5.csv
4.79 KB
-
README.md
3.01 KB
-
README.txt
2.69 KB
-
TissueDistributionUncroppedimage.TIF
243.78 KB
Abstract
Polyamines are present in all living cells and are implicated in various crucial cellular processes such as proliferation, apoptosis, and autophagy, while excess amounts of polyamines can be toxic to cells. ATP13A2 was recently identified as a mammalian polyamine transporter in neuronal cells, and in this study, we attempted to characterize the function of ATP13A2 in cultured human lung epithelial cells. The data demonstrate that ATP13A2 is endogenously expressed in the mouse lung, and in cultured lung epithelial cells, the expression level of ATP13A2 drastically changes over culture time and peaks at logarithmic phase during the proliferation curve. ATPase activity in ATP13A2-enriched microsomes from lung cells showed polyamine-dependence, as previously reported in other cell types and species. Overexpression of ATP13A2 caused a moderate increase in total cellular polyamine content, while genetic ablation of ATP13A2 resulted in a decrease in cellular polyamine levels. These findings provide novel information regarding the cellular function of ATP13A2 in the lung and contribute to the understanding of the cellular polyamine transport system.
Dataset DOI: 10.5061/dryad.7m0cfxq72
ATP13A2 constitutes intracellular polyamine transport system in the lung epithelial cells
Yuta Hatori et al.
Description of the data and file structure
TissueDistributionUncroppedimage.TIF
Uncropped image of the data shown in Fig. 1A (tissue distribution of ATP13A2 expression in mouse organs).
EndogenousATP13A2inH441Uncroppedimage.TIF
Uncropped image of the data shown in Fig. 1B (western blotting analysis of time-dependence of ATP13A2 expression in H441 cells).
EndogenousATP13A1and2matrixUncroppedimage.TIF
Uncropped image of the data shown in Fig. 1C and D (western blotting analysis of time- and cell density-dependence of ATP13A2 expression in H441 cells).
ATP13A2overexpressionMOItitrationUncroppedimage.TIF
Uncropped image of the data shown in Fig. 2B (western blotting analysis of MOI-dependence of ATP13A2 overexpression).
Mo-blue_OD660_20240217_223008_ATPaseactTimecourse_page1.csv
Mo-blue_OD660_20240217_223008_ATPaseactTimecourse_page2.csv
Raw data used for Fig.3A (Time course of spermidine-dependent ATP hydrolysis by ATP13A2).
ATPase activity was measured by quantifying inorganic phosphate (Pi) using Fiske-Subburow method. Pi standards were taken; 0, 0.2, 0.4, 0.6, 0.8, 1 mM. LacZ basal; control mock microsome. LacZ SPMDN; control mock microsome in the presence of 2 mM spermidine. 13A2 basal; ATP13A2-overexpressing microsome. 13A2 SPMDN; ATP13A2-overexpressing microsome in the presence of 2 mM spermidine.
Mo-blue_OD660_20240314_175736_Mock_page1.csv
Mo-blue_OD660_20240314_175736_Mock_page2.csv
Mo-blue_OD660_20240313_145945_ATP13A2_page1.csv
Mo-blue_OD660_20240313_145945_ATP13A2_page2.csv
Mo-blue_OD660_20240313_145945_ATP13A2_page3.csv
Mock_vs_13A2.prism
Raw data used for Fig.3B (Spermidine-dependence of ATP hydrolysis by ATP13A2).
ATPase activity was measured by quantifying inorganic phosphate (Pi) using Fiske-Subburow method. Pi standards were taken; 0, 0.2, 0.4, 0.6, 0.8, 1 mM. Ccontrol mock microsome and ATP13A2-overexpressing microsome were analyzed. The activity was measured in the presence of 0-10 mM spermidine. Plots were made using PRISM software and fitted to Michaelis-Menten equation. The enzyme parameters were listed in page 3.
Polyamine_LCMSMS_20250411_20260409_page1.csv
Polyamine_LCMSMS_20250411_20260409_page2.csv
Polyamine_LCMSMS_20250411_20260409_page3.csv
Polyamine_LCMSMS_20250411_20260409_page4.csv
Polyamine_LCMSMS_20250411_20260409_page5.csv
Raw data used for Fig.4 (Spermidine and putrescin quantification).
LC-MS/MS peak areas are listed in the tables. PUT, SPD, SPM standards were measured and used for converting peak area values to weight (ng). Sample 1, 3, 5, 7; control cells. Sample 2, 4, 6, 8; ATP13A1-overexpressing cells.
README.txt
Copy of this README.