Activation of GRP78 ATPase suppresses A549 lung cancer cell migration by promoting ITGB4 degradation
Hypochlorous acid (HOCl) is an essential signal molecule in cancer cells. Activated GRP78 ATPase by a HOCl probe named ZBM-H inhibits lung cancer cell growth. However, the role and underlying mechanism of GRP78 ATPase in lung cancer cell migration have not been established. Here, we reported that ac...
Main Authors: | , , , , , , |
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Format: | Article |
Language: | English |
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Taylor & Francis Group
2022-12-01
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Series: | Cell Adhesion & Migration |
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Online Access: | https://www.tandfonline.com/doi/10.1080/19336918.2022.2130415 |
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author | Junya Ning Xiaoling Cui Nan Li Na Li Baoxiang Zhao Junying Miao Zhaomin Lin |
author_facet | Junya Ning Xiaoling Cui Nan Li Na Li Baoxiang Zhao Junying Miao Zhaomin Lin |
author_sort | Junya Ning |
collection | DOAJ |
description | Hypochlorous acid (HOCl) is an essential signal molecule in cancer cells. Activated GRP78 ATPase by a HOCl probe named ZBM-H inhibits lung cancer cell growth. However, the role and underlying mechanism of GRP78 ATPase in lung cancer cell migration have not been established. Here, we reported that activation of GRP78 ATPase by ZBM-H suppressed A549 cell migration and inhibited EMT process. Notably, ZBM-H time-dependently decreased the protein level of integrin β4 (ITGB4) in A549 cells. Combinatorial treatment of 3BDO (an autophagy inhibitor) and ZBM-H partially rescued the protein level of ITGB4. Consistently, 3BDO partially reversed ZBM-H-inhibited cell migration. Furthermore, ZBM-H promoted the interaction between ANXA7 and Hsc70, which participated in the regulation of selective autophagy and degradation of ITGB4. |
first_indexed | 2024-04-13T19:52:51Z |
format | Article |
id | doaj.art-90f7933d011741edb4173909a20f181a |
institution | Directory Open Access Journal |
issn | 1933-6918 1933-6926 |
language | English |
last_indexed | 2024-04-13T19:52:51Z |
publishDate | 2022-12-01 |
publisher | Taylor & Francis Group |
record_format | Article |
series | Cell Adhesion & Migration |
spelling | doaj.art-90f7933d011741edb4173909a20f181a2022-12-22T02:32:26ZengTaylor & Francis GroupCell Adhesion & Migration1933-69181933-69262022-12-0116110711410.1080/19336918.2022.2130415Activation of GRP78 ATPase suppresses A549 lung cancer cell migration by promoting ITGB4 degradationJunya Ning0Xiaoling Cui1Nan Li2Na Li3Baoxiang Zhao4Junying Miao5Zhaomin Lin6Shandong Provincial Key Laboratory of Animal Cells and Developmental Biology, School of Life Science, Shandong University, Qingdao, P.R. ChinaShandong Provincial Key Laboratory of Animal Cells and Developmental Biology, School of Life Science, Shandong University, Qingdao, P.R. ChinaShandong Provincial Key Laboratory of Animal Cells and Developmental Biology, School of Life Science, Shandong University, Qingdao, P.R. ChinaShandong Provincial Key Laboratory of Animal Cells and Developmental Biology, School of Life Science, Shandong University, Qingdao, P.R. ChinaInstitute of Organic Chemistry, School of Chemistry and Chemical Engineering, Shandong University, Jinan, P.R. ChinaShandong Provincial Key Laboratory of Animal Cells and Developmental Biology, School of Life Science, Shandong University, Qingdao, P.R. ChinaCentral Research Laboratory, the Second Hospital, Shandong University, Jinan, P.R. ChinaHypochlorous acid (HOCl) is an essential signal molecule in cancer cells. Activated GRP78 ATPase by a HOCl probe named ZBM-H inhibits lung cancer cell growth. However, the role and underlying mechanism of GRP78 ATPase in lung cancer cell migration have not been established. Here, we reported that activation of GRP78 ATPase by ZBM-H suppressed A549 cell migration and inhibited EMT process. Notably, ZBM-H time-dependently decreased the protein level of integrin β4 (ITGB4) in A549 cells. Combinatorial treatment of 3BDO (an autophagy inhibitor) and ZBM-H partially rescued the protein level of ITGB4. Consistently, 3BDO partially reversed ZBM-H-inhibited cell migration. Furthermore, ZBM-H promoted the interaction between ANXA7 and Hsc70, which participated in the regulation of selective autophagy and degradation of ITGB4.https://www.tandfonline.com/doi/10.1080/19336918.2022.2130415Integrin β4cell migrationglucose-regulated protein 78hypochlorous acid probelung cancer cells |
spellingShingle | Junya Ning Xiaoling Cui Nan Li Na Li Baoxiang Zhao Junying Miao Zhaomin Lin Activation of GRP78 ATPase suppresses A549 lung cancer cell migration by promoting ITGB4 degradation Cell Adhesion & Migration Integrin β4 cell migration glucose-regulated protein 78 hypochlorous acid probe lung cancer cells |
title | Activation of GRP78 ATPase suppresses A549 lung cancer cell migration by promoting ITGB4 degradation |
title_full | Activation of GRP78 ATPase suppresses A549 lung cancer cell migration by promoting ITGB4 degradation |
title_fullStr | Activation of GRP78 ATPase suppresses A549 lung cancer cell migration by promoting ITGB4 degradation |
title_full_unstemmed | Activation of GRP78 ATPase suppresses A549 lung cancer cell migration by promoting ITGB4 degradation |
title_short | Activation of GRP78 ATPase suppresses A549 lung cancer cell migration by promoting ITGB4 degradation |
title_sort | activation of grp78 atpase suppresses a549 lung cancer cell migration by promoting itgb4 degradation |
topic | Integrin β4 cell migration glucose-regulated protein 78 hypochlorous acid probe lung cancer cells |
url | https://www.tandfonline.com/doi/10.1080/19336918.2022.2130415 |
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