Atractylenolide III Attenuates Apoptosis in H9c2 Cells by Inhibiting Endoplasmic Reticulum Stress through the GRP78/PERK/CHOP Signaling Pathway
The objective of this study was to determine the effect of atractylenolide III (ATL-III) on endoplasmic reticulum stress (ERS) injury, H9c2 cardiomyocyte apoptosis induced by tunicamycin (TM), and the GRP78/PERK/CHOP signaling pathway. Molecular docking was applied to predict the binding affinity of...
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| Veröffentlicht in: | Evidence-based complementary and alternative medicine 2022-09, Vol.2022, p.1-12 |
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| creator | Zuo, Meng-yu Tang, Tong-juan Wang, Xiang Gu, Jin-fan Wang, Liang Chen, Jian Yao, Juan Li, Xiang-yang Zhou, Peng Huang, Jin-ling |
| description | The objective of this study was to determine the effect of atractylenolide III (ATL-III) on endoplasmic reticulum stress (ERS) injury, H9c2 cardiomyocyte apoptosis induced by tunicamycin (TM), and the GRP78/PERK/CHOP signaling pathway. Molecular docking was applied to predict the binding affinity of ATL-III to the key proteins GRP78, PERK, IREα, and ATF6 in ERS. Then, in vitro experiments were used to verify the molecular docking results. ERS injury model of H9c2 cells was established by TM. Cell viability was detected by MTT assay, and apoptosis was detected by Hoechst/PI double staining and flow cytometry. Protein expression levels of GRP78, PERK, eIF2α, ATF4, CHOP, Bax, Bcl-2, and Caspase-3 were detected by Western blot. And mRNA levels of GRP78, CHOP, PERK, eIF2α, and ATF4 were detected by RT-qPCR. Moreover, the mechanism was further studied by using GRP78 inhibitor (4-phenylbutyric acid, 4-PBA), and PERK inhibitor (GSK2656157). The results showed that ATL-III had a good binding affinity with GRP78, and the best binding affinity was with PERK. ATL-III increased the viability of H9c2 cells, decreased the apoptosis rate, downregulated Bax and Caspase-3, and increased Bcl-2 compared with the model group. Moreover, ATL-III downregulated the protein and mRNA levels of GRP78, CHOP, PERK, eIF2α, and ATF4, consistent with the inhibition of 4-PBA. ATL-III also decreased the expression levels of PERK, eIF2α, ATF4, CHOP, Bax, and Caspase-3, while increasing the expression of Bcl-2, which is consistent with GSK2656157. Taken together, ATL-III could inhibit TM-induced ERS injury and H9c2 cardiomyocyte apoptosis by regulating the GRP78/PERK/CHOP signaling pathway and has myocardial protection. |
| doi_str_mv | 10.1155/2022/1149231 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_9492373</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2718639069</sourcerecordid><originalsourceid>FETCH-LOGICAL-c425t-e00e05db03c85d8077c2e9ab4ebd20c1fa6e8afb1f833163c11bcbd08c67be383</originalsourceid><addsrcrecordid>eNp9kVFr2zAUhc3YYF23t_0AwV4GaxpJtiz5ZRBC1pgWGtIV-iYk-TpWsSXPklfyK_aX5zSh0D3s6Vy4H4d7z0mSzwRfEsLYnGJK54RkBU3Jm-SM8IzMMirE25eZP7xPPoTwiDEtOOdnyZ9FHJSJ-xacb20FqCxLtIgR3KgiBLTofR99sAFZh9aFoWgJbRuQ3qPSNVbbaN0OrVzl-1aFzhq0hWjN2I4duosDhIBiM_hx10wK6Gq74WK-WW2v58v17Qbd2Z1T7cFio2LzpPYfk3e1agN8Oul5cv9j9XO5nt3cXpXLxc3MZJTFGWAMmFUap0awSmDODYVC6Qx0RbEhtcpBqFqTWqQpyVNDiDa6wsLkXEMq0vPk-9G3H3UHlQE35dDKfrCdGvbSKytfb5xt5M7_lsUhXZ5OBl9PBoP_NUKIsrPBTNkoB34MknIi8rTAeTGhX_5BH_04TH8_U5yRnDE2URdHygw-hAHql2MIlod65aFeeap3wr8d8ca6Sj3Z_9N_AUQDpl8</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2717516555</pqid></control><display><type>article</type><title>Atractylenolide III Attenuates Apoptosis in H9c2 Cells by Inhibiting Endoplasmic Reticulum Stress through the GRP78/PERK/CHOP Signaling Pathway</title><source>Wiley Online Library Open Access</source><source>EZB-FREE-00999 freely available EZB journals</source><source>PubMed Central</source><source>Alma/SFX Local Collection</source><source>PubMed Central Open Access</source><creator>Zuo, Meng-yu ; Tang, Tong-juan ; Wang, Xiang ; Gu, Jin-fan ; Wang, Liang ; Chen, Jian ; Yao, Juan ; Li, Xiang-yang ; Zhou, Peng ; Huang, Jin-ling</creator><contributor>Cohen, Guy</contributor><creatorcontrib>Zuo, Meng-yu ; Tang, Tong-juan ; Wang, Xiang ; Gu, Jin-fan ; Wang, Liang ; Chen, Jian ; Yao, Juan ; Li, Xiang-yang ; Zhou, Peng ; Huang, Jin-ling ; Cohen, Guy</creatorcontrib><description>The objective of this study was to determine the effect of atractylenolide III (ATL-III) on endoplasmic reticulum stress (ERS) injury, H9c2 cardiomyocyte apoptosis induced by tunicamycin (TM), and the GRP78/PERK/CHOP signaling pathway. Molecular docking was applied to predict the binding affinity of ATL-III to the key proteins GRP78, PERK, IREα, and ATF6 in ERS. Then, in vitro experiments were used to verify the molecular docking results. ERS injury model of H9c2 cells was established by TM. Cell viability was detected by MTT assay, and apoptosis was detected by Hoechst/PI double staining and flow cytometry. Protein expression levels of GRP78, PERK, eIF2α, ATF4, CHOP, Bax, Bcl-2, and Caspase-3 were detected by Western blot. And mRNA levels of GRP78, CHOP, PERK, eIF2α, and ATF4 were detected by RT-qPCR. Moreover, the mechanism was further studied by using GRP78 inhibitor (4-phenylbutyric acid, 4-PBA), and PERK inhibitor (GSK2656157). The results showed that ATL-III had a good binding affinity with GRP78, and the best binding affinity was with PERK. ATL-III increased the viability of H9c2 cells, decreased the apoptosis rate, downregulated Bax and Caspase-3, and increased Bcl-2 compared with the model group. Moreover, ATL-III downregulated the protein and mRNA levels of GRP78, CHOP, PERK, eIF2α, and ATF4, consistent with the inhibition of 4-PBA. ATL-III also decreased the expression levels of PERK, eIF2α, ATF4, CHOP, Bax, and Caspase-3, while increasing the expression of Bcl-2, which is consistent with GSK2656157. Taken together, ATL-III could inhibit TM-induced ERS injury and H9c2 cardiomyocyte apoptosis by regulating the GRP78/PERK/CHOP signaling pathway and has myocardial protection.</description><identifier>ISSN: 1741-427X</identifier><identifier>EISSN: 1741-4288</identifier><identifier>DOI: 10.1155/2022/1149231</identifier><language>eng</language><publisher>New York: Hindawi</publisher><subject>Affinity ; Antibodies ; Apoptosis ; BAX protein ; Bcl-2 protein ; Cardiomyocytes ; Caspase-3 ; Cell viability ; Chinese medicine ; Endoplasmic reticulum ; Experiments ; Flow cytometry ; Heart failure ; Kinases ; Medical prognosis ; mRNA ; Oxidative stress ; Pathogenesis ; Phenylbutyric acid ; Proteins ; Signal transduction ; Tunicamycin</subject><ispartof>Evidence-based complementary and alternative medicine, 2022-09, Vol.2022, p.1-12</ispartof><rights>Copyright © 2022 Meng-yu Zuo et al.</rights><rights>Copyright © 2022 Meng-yu Zuo et al. This is an open access article distributed under the Creative Commons Attribution License (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. https://creativecommons.org/licenses/by/4.0</rights><rights>Copyright © 2022 Meng-yu Zuo et al. 2022</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c425t-e00e05db03c85d8077c2e9ab4ebd20c1fa6e8afb1f833163c11bcbd08c67be383</citedby><cites>FETCH-LOGICAL-c425t-e00e05db03c85d8077c2e9ab4ebd20c1fa6e8afb1f833163c11bcbd08c67be383</cites><orcidid>0000-0002-0625-8921 ; 0000-0002-7322-692X ; 0000-0001-5881-1170 ; 0000-0002-2322-5988</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC9492373/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC9492373/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids></links><search><contributor>Cohen, Guy</contributor><creatorcontrib>Zuo, Meng-yu</creatorcontrib><creatorcontrib>Tang, Tong-juan</creatorcontrib><creatorcontrib>Wang, Xiang</creatorcontrib><creatorcontrib>Gu, Jin-fan</creatorcontrib><creatorcontrib>Wang, Liang</creatorcontrib><creatorcontrib>Chen, Jian</creatorcontrib><creatorcontrib>Yao, Juan</creatorcontrib><creatorcontrib>Li, Xiang-yang</creatorcontrib><creatorcontrib>Zhou, Peng</creatorcontrib><creatorcontrib>Huang, Jin-ling</creatorcontrib><title>Atractylenolide III Attenuates Apoptosis in H9c2 Cells by Inhibiting Endoplasmic Reticulum Stress through the GRP78/PERK/CHOP Signaling Pathway</title><title>Evidence-based complementary and alternative medicine</title><description>The objective of this study was to determine the effect of atractylenolide III (ATL-III) on endoplasmic reticulum stress (ERS) injury, H9c2 cardiomyocyte apoptosis induced by tunicamycin (TM), and the GRP78/PERK/CHOP signaling pathway. Molecular docking was applied to predict the binding affinity of ATL-III to the key proteins GRP78, PERK, IREα, and ATF6 in ERS. Then, in vitro experiments were used to verify the molecular docking results. ERS injury model of H9c2 cells was established by TM. Cell viability was detected by MTT assay, and apoptosis was detected by Hoechst/PI double staining and flow cytometry. Protein expression levels of GRP78, PERK, eIF2α, ATF4, CHOP, Bax, Bcl-2, and Caspase-3 were detected by Western blot. And mRNA levels of GRP78, CHOP, PERK, eIF2α, and ATF4 were detected by RT-qPCR. Moreover, the mechanism was further studied by using GRP78 inhibitor (4-phenylbutyric acid, 4-PBA), and PERK inhibitor (GSK2656157). The results showed that ATL-III had a good binding affinity with GRP78, and the best binding affinity was with PERK. ATL-III increased the viability of H9c2 cells, decreased the apoptosis rate, downregulated Bax and Caspase-3, and increased Bcl-2 compared with the model group. Moreover, ATL-III downregulated the protein and mRNA levels of GRP78, CHOP, PERK, eIF2α, and ATF4, consistent with the inhibition of 4-PBA. ATL-III also decreased the expression levels of PERK, eIF2α, ATF4, CHOP, Bax, and Caspase-3, while increasing the expression of Bcl-2, which is consistent with GSK2656157. Taken together, ATL-III could inhibit TM-induced ERS injury and H9c2 cardiomyocyte apoptosis by regulating the GRP78/PERK/CHOP signaling pathway and has myocardial protection.</description><subject>Affinity</subject><subject>Antibodies</subject><subject>Apoptosis</subject><subject>BAX protein</subject><subject>Bcl-2 protein</subject><subject>Cardiomyocytes</subject><subject>Caspase-3</subject><subject>Cell viability</subject><subject>Chinese medicine</subject><subject>Endoplasmic reticulum</subject><subject>Experiments</subject><subject>Flow cytometry</subject><subject>Heart failure</subject><subject>Kinases</subject><subject>Medical prognosis</subject><subject>mRNA</subject><subject>Oxidative stress</subject><subject>Pathogenesis</subject><subject>Phenylbutyric acid</subject><subject>Proteins</subject><subject>Signal 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medicine</jtitle><date>2022-09-14</date><risdate>2022</risdate><volume>2022</volume><spage>1</spage><epage>12</epage><pages>1-12</pages><issn>1741-427X</issn><eissn>1741-4288</eissn><abstract>The objective of this study was to determine the effect of atractylenolide III (ATL-III) on endoplasmic reticulum stress (ERS) injury, H9c2 cardiomyocyte apoptosis induced by tunicamycin (TM), and the GRP78/PERK/CHOP signaling pathway. Molecular docking was applied to predict the binding affinity of ATL-III to the key proteins GRP78, PERK, IREα, and ATF6 in ERS. Then, in vitro experiments were used to verify the molecular docking results. ERS injury model of H9c2 cells was established by TM. Cell viability was detected by MTT assay, and apoptosis was detected by Hoechst/PI double staining and flow cytometry. Protein expression levels of GRP78, PERK, eIF2α, ATF4, CHOP, Bax, Bcl-2, and Caspase-3 were detected by Western blot. And mRNA levels of GRP78, CHOP, PERK, eIF2α, and ATF4 were detected by RT-qPCR. Moreover, the mechanism was further studied by using GRP78 inhibitor (4-phenylbutyric acid, 4-PBA), and PERK inhibitor (GSK2656157). The results showed that ATL-III had a good binding affinity with GRP78, and the best binding affinity was with PERK. ATL-III increased the viability of H9c2 cells, decreased the apoptosis rate, downregulated Bax and Caspase-3, and increased Bcl-2 compared with the model group. Moreover, ATL-III downregulated the protein and mRNA levels of GRP78, CHOP, PERK, eIF2α, and ATF4, consistent with the inhibition of 4-PBA. ATL-III also decreased the expression levels of PERK, eIF2α, ATF4, CHOP, Bax, and Caspase-3, while increasing the expression of Bcl-2, which is consistent with GSK2656157. Taken together, ATL-III could inhibit TM-induced ERS injury and H9c2 cardiomyocyte apoptosis by regulating the GRP78/PERK/CHOP signaling pathway and has myocardial protection.</abstract><cop>New York</cop><pub>Hindawi</pub><doi>10.1155/2022/1149231</doi><tpages>12</tpages><orcidid>https://orcid.org/0000-0002-0625-8921</orcidid><orcidid>https://orcid.org/0000-0002-7322-692X</orcidid><orcidid>https://orcid.org/0000-0001-5881-1170</orcidid><orcidid>https://orcid.org/0000-0002-2322-5988</orcidid><oa>free_for_read</oa></addata></record> |
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| source | Wiley Online Library Open Access; EZB-FREE-00999 freely available EZB journals; PubMed Central; Alma/SFX Local Collection; PubMed Central Open Access |
| subjects | Affinity Antibodies Apoptosis BAX protein Bcl-2 protein Cardiomyocytes Caspase-3 Cell viability Chinese medicine Endoplasmic reticulum Experiments Flow cytometry Heart failure Kinases Medical prognosis mRNA Oxidative stress Pathogenesis Phenylbutyric acid Proteins Signal transduction Tunicamycin |
| title | Atractylenolide III Attenuates Apoptosis in H9c2 Cells by Inhibiting Endoplasmic Reticulum Stress through the GRP78/PERK/CHOP Signaling Pathway |
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