Ferritinophagic Flux Activation in CT26 Cells Contributed to EMT Inhibition Induced by a Novel Iron Chelator, DpdtpA
Identifieur interne : 000818 ( Ncbi/Merge ); précédent : 000817; suivant : 000819Ferritinophagic Flux Activation in CT26 Cells Contributed to EMT Inhibition Induced by a Novel Iron Chelator, DpdtpA
Auteurs : Yanjie Sun [République populaire de Chine] ; Cuiping Li [République populaire de Chine] ; Jiankang Feng [République populaire de Chine] ; Yongli Li [République populaire de Chine] ; Xinbo Zhai [République populaire de Chine] ; Lei Zhang [République populaire de Chine] ; Changzheng Li [République populaire de Chine]Source :
- Oxidative Medicine and Cellular Longevity [ 1942-0900 ] ; 2019.
Abstract
Epithelial-mesenchymal transition (EMT) contributes to metastasis and drug resistance; inhibition of EMT may attenuate metastasis and drug resistance. It has been demonstrated that ferritinophagy involves the process of many diseases; however, the relationship between EMT and ferritinophagy was not fully established. Some iron chelators show the ability to inhibit EMT, but whether ferritinophagy plays a role in EMT is largely unknown. To this end, we investigated the effect of a novel iron chelator, DpdtpA (2,2 ′-di-pyridylketone dithiocarbamate propionic acid), on EMT in the CT26 cell line. The DpdtpA displayed excellent antitumor (IC50 = 1.5 ± 0.2
Url:
DOI: 10.1155/2019/8753413
PubMed: 31320987
PubMed Central: 6610730
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Biology and Biochemistry, Xinxiang Medical University, Xinxiang, Henan 453003, China</nlm:aff><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Department of Molecular Biology and Biochemistry, Xinxiang Medical University, Xinxiang, Henan 453003</wicri:regionArea><wicri:noRegion>Henan 453003</wicri:noRegion></affiliation></author><author><name sortKey="Li, Yongli" sort="Li, Yongli" uniqKey="Li Y" first="Yongli" last="Li">Yongli Li</name><affiliation wicri:level="1"><nlm:aff id="I3">Department of Histology and Embryology, Sanquan College of Xinxiang Medical University, Xinxiang, Henan 453003, China</nlm:aff><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Department of Histology and Embryology, Sanquan College of Xinxiang Medical University, Xinxiang, Henan 453003</wicri:regionArea><wicri:noRegion>Henan 453003</wicri:noRegion></affiliation></author><author><name sortKey="Zhai, Xinbo" sort="Zhai, Xinbo" uniqKey="Zhai X" first="Xinbo" last="Zhai">Xinbo Zhai</name><affiliation wicri:level="1"><nlm:aff id="I2">Experimental Teaching Center of Biology and Basic Medical Sciences, Sanquan College of Xinxiang Medical University, Xinxiang, Henan 453003, China</nlm:aff><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Experimental Teaching Center of Biology and Basic Medical Sciences, Sanquan College of Xinxiang Medical University, Xinxiang, Henan 453003</wicri:regionArea><wicri:noRegion>Henan 453003</wicri:noRegion></affiliation></author><author><name sortKey="Zhang, Lei" sort="Zhang, Lei" uniqKey="Zhang L" first="Lei" last="Zhang">Lei Zhang</name><affiliation wicri:level="1"><nlm:aff id="I2">Experimental Teaching Center of Biology and Basic Medical Sciences, Sanquan College of Xinxiang Medical University, Xinxiang, Henan 453003, China</nlm:aff><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Experimental Teaching Center of Biology and Basic Medical 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de Chine</country><wicri:regionArea>Department of Molecular Biology and Biochemistry, Xinxiang Medical University, Xinxiang, Henan 453003</wicri:regionArea><wicri:noRegion>Henan 453003</wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:aff id="I2">Experimental Teaching Center of Biology and Basic Medical Sciences, Sanquan College of Xinxiang Medical University, Xinxiang, Henan 453003, China</nlm:aff><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Experimental Teaching Center of Biology and Basic Medical Sciences, Sanquan College of Xinxiang Medical University, Xinxiang, Henan 453003</wicri:regionArea><wicri:noRegion>Henan 453003</wicri:noRegion></affiliation></author><author><name sortKey="Li, Cuiping" sort="Li, Cuiping" uniqKey="Li C" first="Cuiping" last="Li">Cuiping Li</name><affiliation wicri:level="1"><nlm:aff id="I1">Department of Molecular Biology and Biochemistry, Xinxiang Medical University, Xinxiang, Henan 453003, China</nlm:aff><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Department of Molecular Biology and Biochemistry, Xinxiang Medical University, Xinxiang, Henan 453003</wicri:regionArea><wicri:noRegion>Henan 453003</wicri:noRegion></affiliation></author><author><name sortKey="Feng, Jiankang" sort="Feng, Jiankang" uniqKey="Feng J" first="Jiankang" last="Feng">Jiankang Feng</name><affiliation wicri:level="1"><nlm:aff id="I1">Department of Molecular Biology and Biochemistry, Xinxiang Medical University, Xinxiang, Henan 453003, China</nlm:aff><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Department of Molecular Biology and Biochemistry, Xinxiang Medical University, Xinxiang, Henan 453003</wicri:regionArea><wicri:noRegion>Henan 453003</wicri:noRegion></affiliation></author><author><name sortKey="Li, Yongli" sort="Li, Yongli" uniqKey="Li Y" first="Yongli" last="Li">Yongli Li</name><affiliation wicri:level="1"><nlm:aff id="I3">Department of Histology and Embryology, Sanquan College of Xinxiang Medical University, Xinxiang, Henan 453003, China</nlm:aff><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Department of Histology and Embryology, Sanquan College of Xinxiang Medical University, Xinxiang, Henan 453003</wicri:regionArea><wicri:noRegion>Henan 453003</wicri:noRegion></affiliation></author><author><name sortKey="Zhai, Xinbo" sort="Zhai, Xinbo" uniqKey="Zhai X" first="Xinbo" last="Zhai">Xinbo Zhai</name><affiliation wicri:level="1"><nlm:aff id="I2">Experimental Teaching Center of Biology and Basic Medical Sciences, Sanquan College of Xinxiang Medical University, Xinxiang, Henan 453003, China</nlm:aff><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Experimental Teaching Center of Biology and Basic Medical Sciences, Sanquan College of Xinxiang Medical University, Xinxiang, Henan 453003</wicri:regionArea><wicri:noRegion>Henan 453003</wicri:noRegion></affiliation></author><author><name sortKey="Zhang, Lei" sort="Zhang, Lei" uniqKey="Zhang L" first="Lei" last="Zhang">Lei Zhang</name><affiliation wicri:level="1"><nlm:aff id="I2">Experimental Teaching Center of Biology and Basic Medical Sciences, Sanquan College of Xinxiang Medical University, Xinxiang, Henan 453003, China</nlm:aff><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Experimental Teaching Center of Biology and Basic Medical Sciences, Sanquan College of Xinxiang Medical University, Xinxiang, Henan 453003</wicri:regionArea><wicri:noRegion>Henan 453003</wicri:noRegion></affiliation></author><author><name sortKey="Li, Changzheng" sort="Li, Changzheng" uniqKey="Li C" first="Changzheng" last="Li">Changzheng Li</name><affiliation wicri:level="1"><nlm:aff id="I1">Department of Molecular Biology and Biochemistry, Xinxiang Medical University, Xinxiang, Henan 453003, China</nlm:aff><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Department of Molecular Biology and Biochemistry, Xinxiang Medical University, Xinxiang, Henan 453003</wicri:regionArea><wicri:noRegion>Henan 453003</wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:aff id="I2">Experimental Teaching Center of Biology and Basic Medical Sciences, Sanquan College of Xinxiang Medical University, Xinxiang, Henan 453003, China</nlm:aff><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Experimental Teaching Center of Biology and Basic Medical Sciences, Sanquan College of Xinxiang Medical University, Xinxiang, Henan 453003</wicri:regionArea><wicri:noRegion>Henan 453003</wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:aff id="I4">Laboratory of Molecular Medicine, Xinxiang Medical University, Xinxiang, Henan 453003, China</nlm:aff><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Laboratory of Molecular Medicine, Xinxiang Medical University, Xinxiang, Henan 453003</wicri:regionArea><wicri:noRegion>Henan 453003</wicri:noRegion></affiliation></author></analytic><series><title level="j">Oxidative Medicine and Cellular Longevity</title><idno type="ISSN">1942-0900</idno><idno type="eISSN">1942-0994</idno><imprint><date when="2019">2019</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Epithelial-mesenchymal transition (EMT) contributes to metastasis and drug resistance; inhibition of EMT may attenuate metastasis and drug resistance. It has been demonstrated that ferritinophagy involves the process of many diseases; however, the relationship between EMT and ferritinophagy was not fully established. Some iron chelators show the ability to inhibit EMT, but whether ferritinophagy plays a role in EMT is largely unknown. To this end, we investigated the effect of a novel iron chelator, DpdtpA (2,2 ′-di-pyridylketone dithiocarbamate propionic acid), on EMT in the CT26 cell line. The DpdtpA displayed excellent antitumor (IC<sub>50</sub> = 1.5 ± 0.2 <italic>μ</italic>M), leading to ROS production and apoptosis occurrence. Moreover, the ROS production correlated with ferritin degradation. The upregulation of LC3-II and NCOA4 from immunofluorescence and Western blotting analysis revealed that the occurrence of ferritinophagy contributed to ROS production. Furthermore, DpdtpA could induce an alteration both in morphology and in epithelial-mesenchymal markers, displaying significant EMT inhibition. The correlation analysis revealed that DpdtpA-induced ferritinophagy contributed to the EMT inhibition, implying that NCOA4 involved EMT process, which was firstly reported. To reinforce this concept, the ferritinophagic flux (NCOA4/ferritin) in either treated by TGF-<italic>β</italic>1 or combined with DpdtpA was determined. The results indicated that activating ferritinophagic flux would enhance ROS production which accordingly suppressed EMT or implementing the EMT suppression seemed to be through “fighting fire with fire” strategy. Taken together, our data demonstrated that ferritinophagic flux was a dominating driving force in EMT proceeding, and the new finding definitely will enrich our knowledge of ferritinophagy in EMT process.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Savagner, P" uniqKey="Savagner P">P. 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<front><journal-meta><journal-id journal-id-type="nlm-ta">Oxid Med Cell Longev</journal-id><journal-id journal-id-type="iso-abbrev">Oxid Med Cell Longev</journal-id><journal-id journal-id-type="publisher-id">OMCL</journal-id><journal-title-group><journal-title>Oxidative Medicine and Cellular Longevity</journal-title></journal-title-group><issn pub-type="ppub">1942-0900</issn><issn pub-type="epub">1942-0994</issn><publisher><publisher-name>Hindawi</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">31320987</article-id><article-id pub-id-type="pmc">6610730</article-id><article-id pub-id-type="doi">10.1155/2019/8753413</article-id><article-categories><subj-group subj-group-type="heading"><subject>Research Article</subject></subj-group></article-categories><title-group><article-title>Ferritinophagic Flux Activation in CT26 Cells Contributed to EMT Inhibition Induced by a Novel Iron Chelator, DpdtpA</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Sun</surname><given-names>Yanjie</given-names></name><xref ref-type="aff" rid="I1"><sup>1</sup></xref><xref ref-type="aff" rid="I2"><sup>2</sup></xref></contrib><contrib contrib-type="author"><name><surname>Li</surname><given-names>Cuiping</given-names></name><xref ref-type="aff" rid="I1"><sup>1</sup></xref></contrib><contrib contrib-type="author"><name><surname>Feng</surname><given-names>Jiankang</given-names></name><xref ref-type="aff" rid="I1"><sup>1</sup></xref></contrib><contrib contrib-type="author"><name><surname>Li</surname><given-names>Yongli</given-names></name><xref ref-type="aff" rid="I3"><sup>3</sup></xref></contrib><contrib contrib-type="author"><name><surname>Zhai</surname><given-names>Xinbo</given-names></name><xref ref-type="aff" rid="I2"><sup>2</sup></xref></contrib><contrib contrib-type="author"><name><surname>Zhang</surname><given-names>Lei</given-names></name><xref ref-type="aff" rid="I2"><sup>2</sup></xref></contrib><contrib contrib-type="author" corresp="yes"><contrib-id contrib-id-type="orcid" authenticated="false">https://orcid.org/0000-0002-6226-5843</contrib-id><name><surname>Li</surname><given-names>Changzheng</given-names></name><email>changzhenl@yahoo.com</email><xref ref-type="aff" rid="I1"><sup>1</sup></xref><xref ref-type="aff" rid="I2"><sup>2</sup></xref><xref ref-type="aff" rid="I4"><sup>4</sup></xref></contrib></contrib-group><aff id="I1"><sup>1</sup>Department of Molecular Biology and Biochemistry, Xinxiang Medical University, Xinxiang, Henan 453003, China</aff><aff id="I2"><sup>2</sup>Experimental Teaching Center of Biology and Basic Medical Sciences, Sanquan College of Xinxiang Medical University, Xinxiang, Henan 453003, China</aff><aff id="I3"><sup>3</sup>Department of Histology and Embryology, Sanquan College of Xinxiang Medical University, Xinxiang, Henan 453003, China</aff><aff id="I4"><sup>4</sup>Laboratory of Molecular Medicine, Xinxiang Medical University, Xinxiang, Henan 453003, China</aff><author-notes><fn fn-type="other"><p>Guest Editor: Marco Cordani</p></fn></author-notes><pub-date pub-type="collection"><year>2019</year></pub-date><pub-date pub-type="epub"><day>20</day><month>6</month><year>2019</year></pub-date><volume>2019</volume><elocation-id>8753413</elocation-id><history><date date-type="received"><day>24</day><month>1</month><year>2019</year></date><date date-type="rev-recd"><day>7</day><month>4</month><year>2019</year></date><date date-type="accepted"><day>8</day><month>5</month><year>2019</year></date></history><permissions><copyright-statement>Copyright © 2019 Yanjie Sun et al.</copyright-statement><copyright-year>2019</copyright-year><license xlink:href="http://creativecommons.org/licenses/by/4.0/"><license-p>This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.</license-p></license></permissions><abstract><p>Epithelial-mesenchymal transition (EMT) contributes to metastasis and drug resistance; inhibition of EMT may attenuate metastasis and drug resistance. It has been demonstrated that ferritinophagy involves the process of many diseases; however, the relationship between EMT and ferritinophagy was not fully established. Some iron chelators show the ability to inhibit EMT, but whether ferritinophagy plays a role in EMT is largely unknown. To this end, we investigated the effect of a novel iron chelator, DpdtpA (2,2 ′-di-pyridylketone dithiocarbamate propionic acid), on EMT in the CT26 cell line. The DpdtpA displayed excellent antitumor (IC<sub>50</sub> = 1.5 ± 0.2 <italic>μ</italic>M), leading to ROS production and apoptosis occurrence. Moreover, the ROS production correlated with ferritin degradation. The upregulation of LC3-II and NCOA4 from immunofluorescence and Western blotting analysis revealed that the occurrence of ferritinophagy contributed to ROS production. Furthermore, DpdtpA could induce an alteration both in morphology and in epithelial-mesenchymal markers, displaying significant EMT inhibition. The correlation analysis revealed that DpdtpA-induced ferritinophagy contributed to the EMT inhibition, implying that NCOA4 involved EMT process, which was firstly reported. To reinforce this concept, the ferritinophagic flux (NCOA4/ferritin) in either treated by TGF-<italic>β</italic>1 or combined with DpdtpA was determined. The results indicated that activating ferritinophagic flux would enhance ROS production which accordingly suppressed EMT or implementing the EMT suppression seemed to be through “fighting fire with fire” strategy. Taken together, our data demonstrated that ferritinophagic flux was a dominating driving force in EMT proceeding, and the new finding definitely will enrich our knowledge of ferritinophagy in EMT process.</p></abstract><funding-group><award-group><funding-source>Xinxiang Medical University</funding-source><award-id>SQTD201802</award-id><award-id>SQTD201703</award-id></award-group><award-group><funding-source>Key Research Project Funding Program of Higher Educational Institutions of Henan Province</funding-source><award-id>19A310021</award-id></award-group><award-group><funding-source>Henan Provincial Department of Science and Technology</funding-source><award-id>152300410118</award-id></award-group><award-group><funding-source>National Natural Science Foundation of China</funding-source><award-id>21571153</award-id></award-group></funding-group></article-meta></front><floats-group><fig id="fig1" orientation="portrait" position="float"><label>Figure 1</label><caption><p>DpdtpA-induced growth inhibition involved ROS generation. (a) Structure of DpdtpA; (b) antiproliferative effect of DpdtpA on the CT26 cells; (c) DpdtpA induced ROS production: C1, 0.7% DMSO; C2, 0.78 <italic>μ</italic>M DpdtpA; C3, 0.78 <italic>μ</italic>M DpdtpA+NAC (1.5 mM). The data from MTT were from five measurements, and ROS assays were conducted twice.</p></caption><graphic xlink:href="OMCL2019-8753413.001"></graphic></fig><fig id="fig2" orientation="portrait" position="float"><label>Figure 2</label><caption><p>A DpdtpA induced apoptosis in the CT26 cell after 24 h posttreatment as detected by flow cytometry and EtBr/AO staining assay. Flow cytometry analysis: (A1) DMSO; (A2) 0.78 <italic>μ</italic>M DpdtpA; (A3) 1.56 <italic>μ</italic>M DpdtpA; (A4) 1.56 <italic>μ</italic>M DpdtpA+NAC (1.5 mM). (b) Quantification analysis of apoptosis and necrosis induced by DpdtpA. The data were from two measurements. Microscopical analysis by EtBr/AO stains: (c) DMSO; (d) 0.78 <italic>μ</italic>M DpdtpA; (e) 1.56 <italic>μ</italic>M DpdtpA. Green, orange, and red fluorescence indicates live, apoptotic, and dead cells, respectively. Images were captured by fluorescence microscope (Nikon ECLIPSE TiE) at ×10 magnification. AO: acridine orange; EtBr: ethidium bromide. The measurements were performed thrice from different field of view (AO/EtBr stains); the quantification analysis of apoptosis by flow cytometry was from two measurements.</p></caption><graphic xlink:href="OMCL2019-8753413.002"></graphic></fig><fig id="fig3" orientation="portrait" position="float"><label>Figure 3</label><caption><p>DpdtpA induced ferritin degradation. The nuclei stained by DAPI in blue, ferritin labeled in red. (a-c) Control group (DMSO): (a) nuclei in blue; (b) ferritin in red; (c) merge of nuclei and ferritin. (d-f) DpdtpA-treated CT26 cells: (d) nuclei in blue; (e) ferritin in red; (f) merge of nuclei and ferritin. The measurements were performed thrice. (g) Western blotting analysis. Scale bar: 100 <italic>μ</italic>m.</p></caption><graphic xlink:href="OMCL2019-8753413.003"></graphic></fig><fig id="fig4" orientation="portrait" position="float"><label>Figure 4</label><caption><p>DpdtpA induced ferritin autophagy (ferritinophagy). The nuclei stained by DAPI in blue, ferritin labeled in red; LC3 labeled in green. (a-d) Control group: (a) nuclei in blue; (b) ferritin in red; (c) LC3 in green; (d) merge of ferritin with LC3. (e-h) DpdtpA-treated group: (e) nuclei in blue; (f) ferritin in red; (g) LC3 in green; (h) merge of ferritin with LC3. (i-l) DpdtpA combined with 3-MA group: (i) nuclei in blue; (j) ferritin in red; (k) LC3 in green; (l) merge of ferritin with LC3. The experiments were performed thrice. Scale bar: 100 <italic>μ</italic>m.</p></caption><graphic xlink:href="OMCL2019-8753413.004"></graphic></fig><fig id="fig5" orientation="portrait" position="float"><label>Figure 5</label><caption><p>DpdtpA exposure resulted in alterations of ferritinophagy and autophagy proteins. (a) Western blotting analysis of autophagic and ferritinophagic proteins; (b) the quantitative comparisons of the proteins from (a). The quantification analysis of NCOA4 and ferritin was from two experiments. The condition was as indicated in the figure (<sup>∗∗</sup><italic>p</italic> < 0.05; <sup>∗∗∗,###</sup><italic>p</italic> < 0.01).</p></caption><graphic xlink:href="OMCL2019-8753413.005"></graphic></fig><fig id="fig6" orientation="portrait" position="float"><label>Figure 6</label><caption><p>DpdtpA induced alteration in morphology correlated with EMT modulation. (a-c) Alteration in morphology treated by DpdtpA for 48 h at indicated concentration; the blue arrow: spindle-shaped cells, black arrow: retracted and rounded cells; (a) 0.7% DMSO; (b) 0.26 <italic>μ</italic>M DpdtpA; (c) 0.52 <italic>μ</italic>M DpdtpA; objective size: 20 × 10, scale bar: 200 <italic>μ</italic>m. (d) Western blotting analysis. (e-l) Immunofluorescence analysis of epithelial-mesenchymal markers. (e-h) (0.7% DMSO): (e) nuclei in blue; (f) E-cadherin in green; (g) vimentin in red; (h) merge of nuclei, E-cadherin, and vimentin in the DMSO group. (i-l) DpdtpA-treated group: (i) nuclei in blue; (j) E-cadherin in green; (k) vimentin in red; (l) merge of nuclei, E-cadherin and vimentin in the DpdtpA-treated group. The measurements were performed thrice from different field of view. Objective size: 40 × 10 (fluorescence), scale bar: 100 <italic>μ</italic>m.</p></caption><graphic xlink:href="OMCL2019-8753413.006"></graphic></fig><fig id="fig7" orientation="portrait" position="float"><label>Figure 7</label><caption><p>DpdtpA resisted TGF-<italic>β</italic>1-induced EMT. (a-d) (TGF-<italic>β</italic>1-treated group): (a) nuclei stained by DAPI in blue (DMSO); (b) E-cadherin in green; (c) vimentin in red; (d) merge of nuclei, E-cadherin, and vimentin. (e-h) (TGF-<italic>β</italic>1 treatment plus DpdtpA): (e) nuclei in blue; (f) E-cadherin in green; (g) vimentin in red; (h) merge of nuclei, E-cadherin, and vimentin. The measurements were performed thrice from different field of view. Objective size: 40 × 10, scale bar: 100 <italic>μ</italic>m.</p></caption><graphic xlink:href="OMCL2019-8753413.007"></graphic></fig><fig id="fig8" orientation="portrait" position="float"><label>Figure 8</label><caption><p>DpdtpA induced ferritinophagy in the presence of TGF-<italic>β</italic>1. The nuclei stained by DAPI in blue, NCOA4 in green, and ferritin in red. (a-d) (0.7% DMSO, TGF-<italic>β</italic>1 treatment only): (a) nuclei in blue; (b) NCOA4 in green; (c) ferritin in red; (d) merge of nuclei, ferritin, and NCOA4. (e)-(h) TGF-<italic>β</italic>1 combined with DpdtpA: (e) nuclei in blue; (f) NCOA4 in green; (g) ferritin in red; (h) merge of nuclei, ferritin, and NCOA4. Objective size: 40 × 10, scale bar: 100 <italic>μ</italic>m. The measurements were performed thrice from different field of view.</p></caption><graphic xlink:href="OMCL2019-8753413.008"></graphic></fig><fig id="fig9" orientation="portrait" position="float"><label>Figure 9</label><caption><p>Ferritinophagic flux played an important role in EMT process. (a) The alterations in ferritinophagy and EMT-related proteins when either TGF-<italic>β</italic>1 or combined with DpdtpA treatment; (b) quantitative analysis of the ferritinophagic flux in the investigated condition. The quantification analysis of ferritinophagic flux was from three experiments (<sup>∗∗</sup><sup>, $$</sup><italic>p</italic> < 0.05; one-way ANOVA).</p></caption><graphic xlink:href="OMCL2019-8753413.009"></graphic></fig><fig id="fig10" orientation="portrait" position="float"><label>Figure 10</label><caption><p>DpdtpA induced alteration in lysosomal membrane permeability and release of cathepsin D. (a) DMSO; (b) 0.78 <italic>μ</italic>M DpdtpA; (c) 1.56 <italic>μ</italic>M DpdtpA; (d) 0.78 <italic>μ</italic>M DpdtpA+3-MA (5 mM); (e) 1.56 <italic>μ</italic>M DpdtpA+3-MA (5 mM); (f) 3-MA (5 mM); (g) quantitative analysis of alteration in fluorescence after treated by either DpdtpA or combined with 3-MA; (h) DpdtpA induced cathepsin D release. The quantification analysis of intensity of red fluorescence was from three measurements. The Western blots were performed twice (<sup>∗∗∗</sup><sup>, ###, $$$</sup><italic>p</italic> < 0.01).</p></caption><graphic xlink:href="OMCL2019-8753413.010"></graphic></fig></floats-group></pmc><affiliations><list><country><li>République populaire de Chine</li></country></list><tree><country name="République populaire de Chine"><noRegion><name sortKey="Sun, Yanjie" sort="Sun, Yanjie" uniqKey="Sun Y" first="Yanjie" last="Sun">Yanjie Sun</name></noRegion><name sortKey="Feng, Jiankang" sort="Feng, Jiankang" uniqKey="Feng J" first="Jiankang" last="Feng">Jiankang Feng</name><name sortKey="Li, Changzheng" sort="Li, Changzheng" uniqKey="Li C" first="Changzheng" last="Li">Changzheng Li</name><name sortKey="Li, Changzheng" sort="Li, Changzheng" uniqKey="Li C" first="Changzheng" last="Li">Changzheng Li</name><name sortKey="Li, Changzheng" sort="Li, Changzheng" uniqKey="Li C" first="Changzheng" last="Li">Changzheng Li</name><name sortKey="Li, Cuiping" sort="Li, Cuiping" uniqKey="Li C" first="Cuiping" last="Li">Cuiping Li</name><name sortKey="Li, Yongli" sort="Li, Yongli" uniqKey="Li Y" first="Yongli" last="Li">Yongli Li</name><name sortKey="Sun, Yanjie" sort="Sun, Yanjie" uniqKey="Sun Y" first="Yanjie" last="Sun">Yanjie Sun</name><name sortKey="Zhai, Xinbo" sort="Zhai, Xinbo" uniqKey="Zhai X" first="Xinbo" last="Zhai">Xinbo Zhai</name><name sortKey="Zhang, Lei" sort="Zhang, Lei" uniqKey="Zhang L" first="Lei" last="Zhang">Lei Zhang</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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| HfdSelect -Kh $EXPLOR_AREA/Data/Ncbi/Merge/biblio.hfd \
| NlmPubMed2Wicri -a ChloroquineV1
| This area was generated with Dilib version V0.6.33. |  |