Sulfur dioxide alleviates programmed cell death in barley aleurone by acting as an antioxidant
Sulfur dioxide (SO2), a gaseous signaling molecule in animal cells, has recently been found to play a physiological role in plants. Here we studied the role of SO2 in gibberellic acid (GA3)-induced programmed cell death (PCD) in barley (Hordeum vulgare L.) aleurone layers. The application of the SO2...
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| description | Sulfur dioxide (SO2), a gaseous signaling molecule in animal cells, has recently been found to play a physiological role in plants. Here we studied the role of SO2 in gibberellic acid (GA3)-induced programmed cell death (PCD) in barley (Hordeum vulgare L.) aleurone layers. The application of the SO2 donor (NaHSO3/Na2SO3, 1:3 M/M) effectively alleviated PCD in barley aleurone layers in a dose-dependent manner with an optimal concentration of 50 μM. Further investigations showed that SO2 reduced the accumulation of hydrogen peroxide (H2O2), superoxide anion (⋅O2-) and malondialdehyde (MDA) in aleurone layers. Moreover, the activities of antioxidant enzymes such as superoxide dismutase (SOD), catalase (CAT), ascorbate peroxidase (APX), glutathione reductase (GR) and guaiacol peroxidase (POD) were enhanced by SO2 donor treatment. Meanwhile, lipoxygenase (LOX) activity was attenuated by SO2 donor treatment. Furthermore, an induction of endogenous H2S and NO were also observed in SO2-treated aleurone layers, suggesting interactions of SO2 with other well-known signaling molecules. Taken together, we show that SO2 negatively regulated PCD by acting as an antioxidant to scavenge excessive reactive oxygen species (ROS) generated during PCD. |
| doi_str_mv | 10.1371/journal.pone.0188289 |
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Here we studied the role of SO2 in gibberellic acid (GA3)-induced programmed cell death (PCD) in barley (Hordeum vulgare L.) aleurone layers. The application of the SO2 donor (NaHSO3/Na2SO3, 1:3 M/M) effectively alleviated PCD in barley aleurone layers in a dose-dependent manner with an optimal concentration of 50 μM. Further investigations showed that SO2 reduced the accumulation of hydrogen peroxide (H2O2), superoxide anion (⋅O2-) and malondialdehyde (MDA) in aleurone layers. Moreover, the activities of antioxidant enzymes such as superoxide dismutase (SOD), catalase (CAT), ascorbate peroxidase (APX), glutathione reductase (GR) and guaiacol peroxidase (POD) were enhanced by SO2 donor treatment. Meanwhile, lipoxygenase (LOX) activity was attenuated by SO2 donor treatment. Furthermore, an induction of endogenous H2S and NO were also observed in SO2-treated aleurone layers, suggesting interactions of SO2 with other well-known signaling molecules. Taken together, we show that SO2 negatively regulated PCD by acting as an antioxidant to scavenge excessive reactive oxygen species (ROS) generated during PCD.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0188289</identifier><identifier>PMID: 29155872</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Aluminum ; Antioxidants ; Antioxidants - metabolism ; Antioxidants - pharmacology ; Apoptosis ; Apoptosis - drug effects ; Ascorbate Peroxidases - metabolism ; Ascorbic acid ; Barley ; Biology and Life Sciences ; Catalase ; Catalase - metabolism ; Cell death ; Engineering ; Enzymes ; Food science ; Gibberellic acid ; Gibberellins - antagonists & inhibitors ; Gibberellins - pharmacology ; Glutathione ; Glutathione reductase ; Glutathione Reductase - metabolism ; Guaiacol ; Hordeum - drug effects ; Hordeum - metabolism ; Hydrogen ; Hydrogen peroxide ; Hydrogen sulfide ; L-Ascorbate peroxidase ; Lipoxygenase ; Lipoxygenase - metabolism ; Liquid oxygen ; Malondialdehyde ; Malondialdehyde - metabolism ; Metabolism ; Methods ; Oxidative stress ; Oxygen ; Peroxidase ; Peroxidase - metabolism ; Physical Sciences ; Physiological aspects ; Physiology ; Plant proteins ; Plant Proteins - metabolism ; Reactive oxygen species ; Research and Analysis Methods ; Seeds ; Signal Transduction ; Signaling ; Sulfates - chemistry ; Sulfur ; Sulfur dioxide ; Sulfur Dioxide - metabolism ; Sulfur Dioxide - pharmacology ; Superoxide dismutase ; Superoxide Dismutase - metabolism ; Superoxides - metabolism</subject><ispartof>PloS one, 2017-11, Vol.12 (11), p.e0188289</ispartof><rights>COPYRIGHT 2017 Public Library of Science</rights><rights>2017 Wang et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2017 Wang et al 2017 Wang et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c692t-a863b2d2c568764efa33ae413e6b0edeb7b259fd3d087886efb3fe026012552d3</citedby><cites>FETCH-LOGICAL-c692t-a863b2d2c568764efa33ae413e6b0edeb7b259fd3d087886efb3fe026012552d3</cites><orcidid>0000-0002-8406-8373</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/PMC5695815/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5695815/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,2096,2915,23845,27901,27902,53766,53768,79342,79343</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29155872$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wang, Sha-Sha</creatorcontrib><creatorcontrib>Zhang, Ying-Xin</creatorcontrib><creatorcontrib>Yang, Feng</creatorcontrib><creatorcontrib>Huang, Zhong-Qin</creatorcontrib><creatorcontrib>Tang, Jun</creatorcontrib><creatorcontrib>Hu, Kang-Di</creatorcontrib><creatorcontrib>Zhang, Hua</creatorcontrib><title>Sulfur dioxide alleviates programmed cell death in barley aleurone by acting as an antioxidant</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>Sulfur dioxide (SO2), a gaseous signaling molecule in animal cells, has recently been found to play a physiological role in plants. Here we studied the role of SO2 in gibberellic acid (GA3)-induced programmed cell death (PCD) in barley (Hordeum vulgare L.) aleurone layers. The application of the SO2 donor (NaHSO3/Na2SO3, 1:3 M/M) effectively alleviated PCD in barley aleurone layers in a dose-dependent manner with an optimal concentration of 50 μM. Further investigations showed that SO2 reduced the accumulation of hydrogen peroxide (H2O2), superoxide anion (⋅O2-) and malondialdehyde (MDA) in aleurone layers. Moreover, the activities of antioxidant enzymes such as superoxide dismutase (SOD), catalase (CAT), ascorbate peroxidase (APX), glutathione reductase (GR) and guaiacol peroxidase (POD) were enhanced by SO2 donor treatment. Meanwhile, lipoxygenase (LOX) activity was attenuated by SO2 donor treatment. Furthermore, an induction of endogenous H2S and NO were also observed in SO2-treated aleurone layers, suggesting interactions of SO2 with other well-known signaling molecules. Taken together, we show that SO2 negatively regulated PCD by acting as an antioxidant to scavenge excessive reactive oxygen species (ROS) generated during PCD.</description><subject>Aluminum</subject><subject>Antioxidants</subject><subject>Antioxidants - metabolism</subject><subject>Antioxidants - pharmacology</subject><subject>Apoptosis</subject><subject>Apoptosis - drug effects</subject><subject>Ascorbate Peroxidases - metabolism</subject><subject>Ascorbic acid</subject><subject>Barley</subject><subject>Biology and Life Sciences</subject><subject>Catalase</subject><subject>Catalase - metabolism</subject><subject>Cell death</subject><subject>Engineering</subject><subject>Enzymes</subject><subject>Food science</subject><subject>Gibberellic acid</subject><subject>Gibberellins - antagonists & inhibitors</subject><subject>Gibberellins - pharmacology</subject><subject>Glutathione</subject><subject>Glutathione reductase</subject><subject>Glutathione Reductase - metabolism</subject><subject>Guaiacol</subject><subject>Hordeum - drug effects</subject><subject>Hordeum - metabolism</subject><subject>Hydrogen</subject><subject>Hydrogen peroxide</subject><subject>Hydrogen sulfide</subject><subject>L-Ascorbate peroxidase</subject><subject>Lipoxygenase</subject><subject>Lipoxygenase - metabolism</subject><subject>Liquid oxygen</subject><subject>Malondialdehyde</subject><subject>Malondialdehyde - metabolism</subject><subject>Metabolism</subject><subject>Methods</subject><subject>Oxidative stress</subject><subject>Oxygen</subject><subject>Peroxidase</subject><subject>Peroxidase - metabolism</subject><subject>Physical Sciences</subject><subject>Physiological aspects</subject><subject>Physiology</subject><subject>Plant proteins</subject><subject>Plant Proteins - metabolism</subject><subject>Reactive oxygen species</subject><subject>Research and Analysis Methods</subject><subject>Seeds</subject><subject>Signal Transduction</subject><subject>Signaling</subject><subject>Sulfates - chemistry</subject><subject>Sulfur</subject><subject>Sulfur dioxide</subject><subject>Sulfur Dioxide - metabolism</subject><subject>Sulfur Dioxide - pharmacology</subject><subject>Superoxide dismutase</subject><subject>Superoxide Dismutase - metabolism</subject><subject>Superoxides - metabolism</subject><issn>1932-6203</issn><issn>1932-6203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><sourceid>DOA</sourceid><recordid>eNqNku9r1DAcxosobk7_A9GCIPjizvxo0vSNMIY_DgYDp740pMm3vYxcc0vSsf335nbduIKCtJCQfp7nG54-RfEaoyWmNf545ccwKLfc-gGWCAtBRPOkOMYNJQtOEH16sD8qXsR4hRCjgvPnxRFpMGOiJsfF78vRdWMojfW31kCpnIMbqxLEcht8H9RmA6bU4FxpQKV1aYeyVcHBXUZhDHl42ea9TnboSxVLNeQ33bvl9WXxrFMuwqtpPSl-fvn84-zb4vzi6-rs9HyheUPSQglOW2KIZlzUvIJOUaqgwhR4i8BAW7eENZ2hBolaCA5dSztAhCNMGCOGnhRv975b56OcookSN5xXpKoJy8RqTxivruQ22I0Kd9IrK-8PfOilCslqB1LwmrVKkQZlbcegFbTK47UiRCPMd9M-TdPGNsejYUhBuZnp_Mtg17L3N5Lxhgm8u8y7ySD46xFi-seVJ6rPUUs7dD6b6Y2NWp4yzBCvCRaZWv6Fyo-BjdX5_3Q2n88EH2aCzCS4Tb0aY5Sry-__z178mrPvD9g1KJfW0bsxl2GIc7Dagzr4GAN0j8lhJHfdfkhD7rotp25n2ZvD1B9FD2WmfwBo5_R0</recordid><startdate>20171120</startdate><enddate>20171120</enddate><creator>Wang, Sha-Sha</creator><creator>Zhang, Ying-Xin</creator><creator>Yang, Feng</creator><creator>Huang, Zhong-Qin</creator><creator>Tang, Jun</creator><creator>Hu, Kang-Di</creator><creator>Zhang, Hua</creator><general>Public Library of Science</general><general>Public Library of Science (PLoS)</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>IOV</scope><scope>ISR</scope><scope>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QO</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TG</scope><scope>7TM</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PDBOC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>RC3</scope><scope>5PM</scope><scope>DOA</scope><orcidid>https://orcid.org/0000-0002-8406-8373</orcidid></search><sort><creationdate>20171120</creationdate><title>Sulfur dioxide alleviates programmed cell death in barley aleurone by acting as an antioxidant</title><author>Wang, Sha-Sha ; Zhang, Ying-Xin ; Yang, Feng ; Huang, Zhong-Qin ; Tang, Jun ; Hu, Kang-Di ; Zhang, Hua</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c692t-a863b2d2c568764efa33ae413e6b0edeb7b259fd3d087886efb3fe026012552d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Aluminum</topic><topic>Antioxidants</topic><topic>Antioxidants - metabolism</topic><topic>Antioxidants - pharmacology</topic><topic>Apoptosis</topic><topic>Apoptosis - drug effects</topic><topic>Ascorbate Peroxidases - metabolism</topic><topic>Ascorbic acid</topic><topic>Barley</topic><topic>Biology and Life Sciences</topic><topic>Catalase</topic><topic>Catalase - metabolism</topic><topic>Cell death</topic><topic>Engineering</topic><topic>Enzymes</topic><topic>Food science</topic><topic>Gibberellic acid</topic><topic>Gibberellins - antagonists & inhibitors</topic><topic>Gibberellins - pharmacology</topic><topic>Glutathione</topic><topic>Glutathione reductase</topic><topic>Glutathione Reductase - metabolism</topic><topic>Guaiacol</topic><topic>Hordeum - drug effects</topic><topic>Hordeum - metabolism</topic><topic>Hydrogen</topic><topic>Hydrogen peroxide</topic><topic>Hydrogen sulfide</topic><topic>L-Ascorbate peroxidase</topic><topic>Lipoxygenase</topic><topic>Lipoxygenase - metabolism</topic><topic>Liquid oxygen</topic><topic>Malondialdehyde</topic><topic>Malondialdehyde - 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Here we studied the role of SO2 in gibberellic acid (GA3)-induced programmed cell death (PCD) in barley (Hordeum vulgare L.) aleurone layers. The application of the SO2 donor (NaHSO3/Na2SO3, 1:3 M/M) effectively alleviated PCD in barley aleurone layers in a dose-dependent manner with an optimal concentration of 50 μM. Further investigations showed that SO2 reduced the accumulation of hydrogen peroxide (H2O2), superoxide anion (⋅O2-) and malondialdehyde (MDA) in aleurone layers. Moreover, the activities of antioxidant enzymes such as superoxide dismutase (SOD), catalase (CAT), ascorbate peroxidase (APX), glutathione reductase (GR) and guaiacol peroxidase (POD) were enhanced by SO2 donor treatment. Meanwhile, lipoxygenase (LOX) activity was attenuated by SO2 donor treatment. Furthermore, an induction of endogenous H2S and NO were also observed in SO2-treated aleurone layers, suggesting interactions of SO2 with other well-known signaling molecules. Taken together, we show that SO2 negatively regulated PCD by acting as an antioxidant to scavenge excessive reactive oxygen species (ROS) generated during PCD.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>29155872</pmid><doi>10.1371/journal.pone.0188289</doi><tpages>e0188289</tpages><orcidid>https://orcid.org/0000-0002-8406-8373</orcidid><oa>free_for_read</oa></addata></record> |
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| issn | 1932-6203 1932-6203 |
| language | eng |
| recordid | cdi_plos_journals_1966424725 |
| source | MEDLINE; DOAJ Directory of Open Access Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central; Free Full-Text Journals in Chemistry; Public Library of Science (PLoS) |
| subjects | Aluminum Antioxidants Antioxidants - metabolism Antioxidants - pharmacology Apoptosis Apoptosis - drug effects Ascorbate Peroxidases - metabolism Ascorbic acid Barley Biology and Life Sciences Catalase Catalase - metabolism Cell death Engineering Enzymes Food science Gibberellic acid Gibberellins - antagonists & inhibitors Gibberellins - pharmacology Glutathione Glutathione reductase Glutathione Reductase - metabolism Guaiacol Hordeum - drug effects Hordeum - metabolism Hydrogen Hydrogen peroxide Hydrogen sulfide L-Ascorbate peroxidase Lipoxygenase Lipoxygenase - metabolism Liquid oxygen Malondialdehyde Malondialdehyde - metabolism Metabolism Methods Oxidative stress Oxygen Peroxidase Peroxidase - metabolism Physical Sciences Physiological aspects Physiology Plant proteins Plant Proteins - metabolism Reactive oxygen species Research and Analysis Methods Seeds Signal Transduction Signaling Sulfates - chemistry Sulfur Sulfur dioxide Sulfur Dioxide - metabolism Sulfur Dioxide - pharmacology Superoxide dismutase Superoxide Dismutase - metabolism Superoxides - metabolism |
| title | Sulfur dioxide alleviates programmed cell death in barley aleurone by acting as an antioxidant |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-09T22%3A27%3A08IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_plos_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Sulfur%20dioxide%20alleviates%20programmed%20cell%20death%20in%20barley%20aleurone%20by%20acting%20as%20an%20antioxidant&rft.jtitle=PloS%20one&rft.au=Wang,%20Sha-Sha&rft.date=2017-11-20&rft.volume=12&rft.issue=11&rft.spage=e0188289&rft.pages=e0188289-&rft.issn=1932-6203&rft.eissn=1932-6203&rft_id=info:doi/10.1371/journal.pone.0188289&rft_dat=%3Cgale_plos_%3EA515067218%3C/gale_plos_%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1966424725&rft_id=info:pmid/29155872&rft_galeid=A515067218&rft_doaj_id=oai_doaj_org_article_8675baa290424f5eb834259ca22c016d&rfr_iscdi=true |