H2S‐induced pancreatic acinar cell apoptosis is mediated via JNK and p38 MAP kinase
Treatment of pancreatic acinar cells by hydrogen sulphide has been shown to induce apoptosis. However, a potential role of mitogen‐activated protein kinases (MAPKs) in this apoptotic pathway remains unknown. The present study examined the role of MAPKs in H2S‐induced apoptosis in mouse pancreatic ac...
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| description | Treatment of pancreatic acinar cells by hydrogen sulphide has been shown to induce apoptosis. However, a potential role of mitogen‐activated protein kinases (MAPKs) in this apoptotic pathway remains unknown. The present study examined the role of MAPKs in H2S‐induced apoptosis in mouse pancreatic acinar cells. Pancreatic acinar cells were treated with 10 μM NaHS (a donor of H2S) for 3 hrs. For the evaluation of the role of MAPKs, PD98059, SP600125 and SB203580 were used as MAPKs inhibitors for ERK1/2, JNK1/2 and p38 MAPK, respectively. We observed activation of ERK1/2, JNK1/2 and p38 when pancreatic acini were exposed to H2S. Moreover, H2S‐induced ERK1/2, JNK1/2 and p38 activation were blocked by pre‐treatment with their corresponding inhibitor in a dose‐dependent manner. H2S‐induced apoptosis led to an increase in caspase 3 activity and this activity was attenuated when caspase 3 inhibitor were used. Also, the cleavage of caspase 3 correlated with that of poly‐(ADP‐ribose)‐polymerase (PARP) cleavage. H2S treatment induced the release of cytochrome c, smac from mitochondria into the cytoplasm, translocation of Bax into mitochondria and decreased the protein level of Bcl‐2. Inhibition of ERK1/2 using PD98059 caused further enhancement of apoptosis as evidenced by annexin V staining, while SP600125 and SB203580 abrogated H2S‐induced apoptosis. Taken together, the data suggest that activation of ERKs promotes cell survival, whereas activation of JNKs and p38 MAP kinase leads to H2S‐induced apoptosis. |
| doi_str_mv | 10.1111/j.1582-4934.2008.00318.x |
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However, a potential role of mitogen‐activated protein kinases (MAPKs) in this apoptotic pathway remains unknown. The present study examined the role of MAPKs in H2S‐induced apoptosis in mouse pancreatic acinar cells. Pancreatic acinar cells were treated with 10 μM NaHS (a donor of H2S) for 3 hrs. For the evaluation of the role of MAPKs, PD98059, SP600125 and SB203580 were used as MAPKs inhibitors for ERK1/2, JNK1/2 and p38 MAPK, respectively. We observed activation of ERK1/2, JNK1/2 and p38 when pancreatic acini were exposed to H2S. Moreover, H2S‐induced ERK1/2, JNK1/2 and p38 activation were blocked by pre‐treatment with their corresponding inhibitor in a dose‐dependent manner. H2S‐induced apoptosis led to an increase in caspase 3 activity and this activity was attenuated when caspase 3 inhibitor were used. Also, the cleavage of caspase 3 correlated with that of poly‐(ADP‐ribose)‐polymerase (PARP) cleavage. H2S treatment induced the release of cytochrome c, smac from mitochondria into the cytoplasm, translocation of Bax into mitochondria and decreased the protein level of Bcl‐2. Inhibition of ERK1/2 using PD98059 caused further enhancement of apoptosis as evidenced by annexin V staining, while SP600125 and SB203580 abrogated H2S‐induced apoptosis. Taken together, the data suggest that activation of ERKs promotes cell survival, whereas activation of JNKs and p38 MAP kinase leads to H2S‐induced apoptosis.</description><identifier>ISSN: 1582-1838</identifier><identifier>EISSN: 1582-4934</identifier><identifier>DOI: 10.1111/j.1582-4934.2008.00318.x</identifier><identifier>PMID: 18373739</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Acinar cells ; Animals ; Annexin V ; Antibodies ; Apoptosis ; Apoptosis - drug effects ; BAX protein ; Bcl-2 protein ; bcl-2-Associated X Protein - metabolism ; Biotechnology ; Carrier Proteins - metabolism ; Caspase 3 - metabolism ; Caspase-3 ; Cell activation ; Cell cycle ; Cell survival ; Cytochrome ; Cytochrome c ; Cytochromes c - metabolism ; Cytoplasm ; DIABLO protein ; Enzyme Activation - drug effects ; ERK ; Experiments ; Extracellular signal-regulated kinase ; Extracellular Signal-Regulated MAP Kinases - metabolism ; Fluorides ; H2S ; Hydrogen sulfide ; JNK ; JNK Mitogen-Activated Protein Kinases - metabolism ; Kinases ; Laboratory animals ; Male ; MAP kinase ; Metabolism ; Mice ; Mitochondria ; Mitochondrial Proteins - metabolism ; Models, Biological ; p38 ; p38 Mitogen-Activated Protein Kinases - metabolism ; Pancreas ; Pancreas, Exocrine - cytology ; Pancreas, Exocrine - enzymology ; Phosphoproteins - metabolism ; Phosphorylation ; Phosphorylation - drug effects ; Poly(ADP-ribose) Polymerases - metabolism ; Protein transport ; Protein Transport - drug effects ; Proteins ; Sulfides - pharmacology</subject><ispartof>Journal of cellular and molecular medicine, 2008-08, Vol.12 (4), p.1374-1383</ispartof><rights>2008 The Authors Journal compilation © 2008 Foundation for Cellular and Molecular Medicine/Blackwell Publishing Ltd</rights><rights>2008. This work is published under https://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2008 The Authors Journal compilation © 2008 Foundation for Cellular and Molecular Medicine/Blackwell Publishing Ltd 2008</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3865679/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3865679/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,1417,11562,27924,27925,45574,45575,46052,46476,53791,53793</link.rule.ids><linktorsrc>$$Uhttps://onlinelibrary.wiley.com/doi/abs/10.1111%2Fj.1582-4934.2008.00318.x$$EView_record_in_Wiley-Blackwell$$FView_record_in_$$GWiley-Blackwell</linktorsrc><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18373739$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Adhikari, Sharmila</creatorcontrib><creatorcontrib>Bhatia, Madhav</creatorcontrib><title>H2S‐induced pancreatic acinar cell apoptosis is mediated via JNK and p38 MAP kinase</title><title>Journal of cellular and molecular medicine</title><addtitle>J Cell Mol Med</addtitle><description>Treatment of pancreatic acinar cells by hydrogen sulphide has been shown to induce apoptosis. However, a potential role of mitogen‐activated protein kinases (MAPKs) in this apoptotic pathway remains unknown. The present study examined the role of MAPKs in H2S‐induced apoptosis in mouse pancreatic acinar cells. Pancreatic acinar cells were treated with 10 μM NaHS (a donor of H2S) for 3 hrs. For the evaluation of the role of MAPKs, PD98059, SP600125 and SB203580 were used as MAPKs inhibitors for ERK1/2, JNK1/2 and p38 MAPK, respectively. We observed activation of ERK1/2, JNK1/2 and p38 when pancreatic acini were exposed to H2S. Moreover, H2S‐induced ERK1/2, JNK1/2 and p38 activation were blocked by pre‐treatment with their corresponding inhibitor in a dose‐dependent manner. H2S‐induced apoptosis led to an increase in caspase 3 activity and this activity was attenuated when caspase 3 inhibitor were used. Also, the cleavage of caspase 3 correlated with that of poly‐(ADP‐ribose)‐polymerase (PARP) cleavage. H2S treatment induced the release of cytochrome c, smac from mitochondria into the cytoplasm, translocation of Bax into mitochondria and decreased the protein level of Bcl‐2. Inhibition of ERK1/2 using PD98059 caused further enhancement of apoptosis as evidenced by annexin V staining, while SP600125 and SB203580 abrogated H2S‐induced apoptosis. Taken together, the data suggest that activation of ERKs promotes cell survival, whereas activation of JNKs and p38 MAP kinase leads to H2S‐induced apoptosis.</description><subject>Acinar cells</subject><subject>Animals</subject><subject>Annexin V</subject><subject>Antibodies</subject><subject>Apoptosis</subject><subject>Apoptosis - drug effects</subject><subject>BAX protein</subject><subject>Bcl-2 protein</subject><subject>bcl-2-Associated X Protein - metabolism</subject><subject>Biotechnology</subject><subject>Carrier Proteins - metabolism</subject><subject>Caspase 3 - metabolism</subject><subject>Caspase-3</subject><subject>Cell activation</subject><subject>Cell cycle</subject><subject>Cell survival</subject><subject>Cytochrome</subject><subject>Cytochrome c</subject><subject>Cytochromes c - metabolism</subject><subject>Cytoplasm</subject><subject>DIABLO protein</subject><subject>Enzyme Activation - drug effects</subject><subject>ERK</subject><subject>Experiments</subject><subject>Extracellular signal-regulated kinase</subject><subject>Extracellular Signal-Regulated MAP Kinases - metabolism</subject><subject>Fluorides</subject><subject>H2S</subject><subject>Hydrogen sulfide</subject><subject>JNK</subject><subject>JNK Mitogen-Activated Protein Kinases - metabolism</subject><subject>Kinases</subject><subject>Laboratory animals</subject><subject>Male</subject><subject>MAP kinase</subject><subject>Metabolism</subject><subject>Mice</subject><subject>Mitochondria</subject><subject>Mitochondrial Proteins - metabolism</subject><subject>Models, Biological</subject><subject>p38</subject><subject>p38 Mitogen-Activated Protein Kinases - metabolism</subject><subject>Pancreas</subject><subject>Pancreas, Exocrine - cytology</subject><subject>Pancreas, Exocrine - enzymology</subject><subject>Phosphoproteins - metabolism</subject><subject>Phosphorylation</subject><subject>Phosphorylation - drug effects</subject><subject>Poly(ADP-ribose) Polymerases - metabolism</subject><subject>Protein transport</subject><subject>Protein Transport - drug effects</subject><subject>Proteins</subject><subject>Sulfides - 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drug effects</topic><topic>BAX protein</topic><topic>Bcl-2 protein</topic><topic>bcl-2-Associated X Protein - metabolism</topic><topic>Biotechnology</topic><topic>Carrier Proteins - metabolism</topic><topic>Caspase 3 - metabolism</topic><topic>Caspase-3</topic><topic>Cell activation</topic><topic>Cell cycle</topic><topic>Cell survival</topic><topic>Cytochrome</topic><topic>Cytochrome c</topic><topic>Cytochromes c - metabolism</topic><topic>Cytoplasm</topic><topic>DIABLO protein</topic><topic>Enzyme Activation - drug effects</topic><topic>ERK</topic><topic>Experiments</topic><topic>Extracellular signal-regulated kinase</topic><topic>Extracellular Signal-Regulated MAP Kinases - metabolism</topic><topic>Fluorides</topic><topic>H2S</topic><topic>Hydrogen sulfide</topic><topic>JNK</topic><topic>JNK Mitogen-Activated Protein Kinases - metabolism</topic><topic>Kinases</topic><topic>Laboratory animals</topic><topic>Male</topic><topic>MAP kinase</topic><topic>Metabolism</topic><topic>Mice</topic><topic>Mitochondria</topic><topic>Mitochondrial Proteins - metabolism</topic><topic>Models, Biological</topic><topic>p38</topic><topic>p38 Mitogen-Activated Protein Kinases - metabolism</topic><topic>Pancreas</topic><topic>Pancreas, Exocrine - cytology</topic><topic>Pancreas, Exocrine - enzymology</topic><topic>Phosphoproteins - metabolism</topic><topic>Phosphorylation</topic><topic>Phosphorylation - drug effects</topic><topic>Poly(ADP-ribose) Polymerases - metabolism</topic><topic>Protein transport</topic><topic>Protein Transport - drug effects</topic><topic>Proteins</topic><topic>Sulfides - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Adhikari, Sharmila</creatorcontrib><creatorcontrib>Bhatia, Madhav</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>ProQuest Central (Corporate)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Access via ProQuest (Open Access)</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Journal of cellular and molecular medicine</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext_linktorsrc</fulltext></delivery><addata><au>Adhikari, Sharmila</au><au>Bhatia, Madhav</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>H2S‐induced pancreatic acinar cell apoptosis is mediated via JNK and p38 MAP kinase</atitle><jtitle>Journal of cellular and molecular medicine</jtitle><addtitle>J Cell Mol Med</addtitle><date>2008-08</date><risdate>2008</risdate><volume>12</volume><issue>4</issue><spage>1374</spage><epage>1383</epage><pages>1374-1383</pages><issn>1582-1838</issn><eissn>1582-4934</eissn><abstract>Treatment of pancreatic acinar cells by hydrogen sulphide has been shown to induce apoptosis. However, a potential role of mitogen‐activated protein kinases (MAPKs) in this apoptotic pathway remains unknown. The present study examined the role of MAPKs in H2S‐induced apoptosis in mouse pancreatic acinar cells. Pancreatic acinar cells were treated with 10 μM NaHS (a donor of H2S) for 3 hrs. For the evaluation of the role of MAPKs, PD98059, SP600125 and SB203580 were used as MAPKs inhibitors for ERK1/2, JNK1/2 and p38 MAPK, respectively. We observed activation of ERK1/2, JNK1/2 and p38 when pancreatic acini were exposed to H2S. Moreover, H2S‐induced ERK1/2, JNK1/2 and p38 activation were blocked by pre‐treatment with their corresponding inhibitor in a dose‐dependent manner. H2S‐induced apoptosis led to an increase in caspase 3 activity and this activity was attenuated when caspase 3 inhibitor were used. Also, the cleavage of caspase 3 correlated with that of poly‐(ADP‐ribose)‐polymerase (PARP) cleavage. H2S treatment induced the release of cytochrome c, smac from mitochondria into the cytoplasm, translocation of Bax into mitochondria and decreased the protein level of Bcl‐2. Inhibition of ERK1/2 using PD98059 caused further enhancement of apoptosis as evidenced by annexin V staining, while SP600125 and SB203580 abrogated H2S‐induced apoptosis. Taken together, the data suggest that activation of ERKs promotes cell survival, whereas activation of JNKs and p38 MAP kinase leads to H2S‐induced apoptosis.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>18373739</pmid><doi>10.1111/j.1582-4934.2008.00318.x</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Acinar cells Animals Annexin V Antibodies Apoptosis Apoptosis - drug effects BAX protein Bcl-2 protein bcl-2-Associated X Protein - metabolism Biotechnology Carrier Proteins - metabolism Caspase 3 - metabolism Caspase-3 Cell activation Cell cycle Cell survival Cytochrome Cytochrome c Cytochromes c - metabolism Cytoplasm DIABLO protein Enzyme Activation - drug effects ERK Experiments Extracellular signal-regulated kinase Extracellular Signal-Regulated MAP Kinases - metabolism Fluorides H2S Hydrogen sulfide JNK JNK Mitogen-Activated Protein Kinases - metabolism Kinases Laboratory animals Male MAP kinase Metabolism Mice Mitochondria Mitochondrial Proteins - metabolism Models, Biological p38 p38 Mitogen-Activated Protein Kinases - metabolism Pancreas Pancreas, Exocrine - cytology Pancreas, Exocrine - enzymology Phosphoproteins - metabolism Phosphorylation Phosphorylation - drug effects Poly(ADP-ribose) Polymerases - metabolism Protein transport Protein Transport - drug effects Proteins Sulfides - pharmacology |
| title | H2S‐induced pancreatic acinar cell apoptosis is mediated via JNK and p38 MAP kinase |
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