Roles of JNK, p38 and ERK mitogen-activated protein kinases in the growth inhibition and apoptosis induced by cadmium
Cadmium (Cd), a human carcinogen, can induce apoptosis in various cell types. Three major mitogen-activated protein kinases (MAPKs), c-JUN N-terminal kinase (JNK), p38 and extracellular signal-regulated kinase (ERK), have been shown to regulate apoptosis. In this study we explore the ability of Cd t...
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| Veröffentlicht in: | Carcinogenesis (New York) 2000-07, Vol.21 (7), p.1423-1432 |
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| description | Cadmium (Cd), a human carcinogen, can induce apoptosis in various cell types. Three major mitogen-activated protein kinases (MAPKs), c-JUN N-terminal kinase (JNK), p38 and extracellular signal-regulated kinase (ERK), have been shown to regulate apoptosis. In this study we explore the ability of Cd to activate JNK, p38 and ERK, including their effects on Cd-mediated growth inhibition and apoptosis in a human non-small cell lung carcinoma cell line, CL3. The kinase activity of JNK was induced dose-dependently by 30-160 microM CdCl(2). High cytotoxic doses of Cd (130-160 microM) markedly activated p38, but low Cd doses did not. Conversely, the activities of ERK1 and ERK2 were decreased by low cytotoxic doses of Cd ( |
| doi_str_mv | 10.1093/carcin/21.5.423 |
| format | Article |
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Three major mitogen-activated protein kinases (MAPKs), c-JUN N-terminal kinase (JNK), p38 and extracellular signal-regulated kinase (ERK), have been shown to regulate apoptosis. In this study we explore the ability of Cd to activate JNK, p38 and ERK, including their effects on Cd-mediated growth inhibition and apoptosis in a human non-small cell lung carcinoma cell line, CL3. The kinase activity of JNK was induced dose-dependently by 30-160 microM CdCl(2). High cytotoxic doses of Cd (130-160 microM) markedly activated p38, but low Cd doses did not. Conversely, the activities of ERK1 and ERK2 were decreased by low cytotoxic doses of Cd (</=80 microM) and moderately activated by high Cd doses. Low cytotoxic doses of Cd transiently activated JNK and simultaneously reduced ERK activity, whereas high cytotoxic doses of Cd persistently activated JNK and p38. PD98059, an inhibitor of ERK upstream activators MAPK kinase (MKK) 1 and MKK2, greatly enhanced cytotoxicity and apoptosis in cells treated with low Cd doses. In contrast, SB202190, an inhibitor of p38, decreased the cytotoxicity and apoptosis induced by high Cd doses. Transient expression of a dominant negative form of JNK1, but not that of JNK2, significantly increased the viability and prevented apoptosis of Cd-treated cells. However, expression of wild-type JNK1 did not affect viability and apoptosis of Cd-treated cells. Transfection of wild-type JNK2 or p38 enhanced apoptosis of cells exposed to low Cd doses but did not affect those exposed to high Cd doses. The JNK activity stimulated by low Cd doses was partially suppressed by expression of a dominant negative form of MKK7, but not a dominant negative form of MKK4, indicating that MKK7 is involved in JNK activation by Cd. Together, the results of this study suggest that JNK and p38 cooperatively participate in apoptosis induced by Cd and that the decreased ERK signal induced by low Cd doses contributes to growth inhibition or apoptosis.</description><identifier>ISSN: 0143-3334</identifier><identifier>EISSN: 1460-2180</identifier><identifier>DOI: 10.1093/carcin/21.5.423</identifier><identifier>PMID: 10874022</identifier><identifier>CODEN: CRNGDP</identifier><language>eng</language><publisher>Oxford: Oxford University Press</publisher><subject>Adenocarcinoma - enzymology ; Adenocarcinoma - pathology ; Apoptosis - drug effects ; Apoptosis - physiology ; Biological and medical sciences ; Cadmium - toxicity ; Cell Division - drug effects ; Cell Division - physiology ; Cell Survival - drug effects ; DNA, Neoplasm - metabolism ; Enzyme Activation - drug effects ; Enzyme Activators ; ERK protein ; Gene Expression Regulation, Neoplastic - drug effects ; Genes, jun ; Growth Inhibitors - toxicity ; Humans ; JNK Mitogen-Activated Protein Kinases ; JNK protein ; lung carcinoma ; Lung Neoplasms - enzymology ; Lung Neoplasms - pathology ; Male ; MAP Kinase Kinase 4 ; MAP Kinase Kinase 7 ; Medical sciences ; Middle Aged ; Mitogen-Activated Protein Kinase Kinases - genetics ; Mitogen-Activated Protein Kinase Kinases - metabolism ; Mitogen-Activated Protein Kinase Kinases - physiology ; Mitogen-Activated Protein Kinases - metabolism ; Mitogen-Activated Protein Kinases - physiology ; p38 Mitogen-Activated Protein Kinases ; p38 protein ; Pneumology ; Proto-Oncogene Proteins c-jun - biosynthesis ; Proto-Oncogene Proteins c-jun - genetics ; Transcription Factor AP-1 - metabolism ; Transfection ; Tumor Cells, Cultured ; Tumors of the respiratory system and mediastinum</subject><ispartof>Carcinogenesis (New York), 2000-07, Vol.21 (7), p.1423-1432</ispartof><rights>2000 INIST-CNRS</rights><rights>Copyright Oxford University Press(England) Jul 2000</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c295t-26455384888450cbe4f451523e726f340e2b3115467351b73c35d9742ebf7ffd3</citedby><cites>FETCH-LOGICAL-c295t-26455384888450cbe4f451523e726f340e2b3115467351b73c35d9742ebf7ffd3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,777,781,27905,27906</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=1431116$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10874022$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>CHUANG, S.-M</creatorcontrib><creatorcontrib>WANG, I.-C</creatorcontrib><creatorcontrib>YANG, J.-L</creatorcontrib><title>Roles of JNK, p38 and ERK mitogen-activated protein kinases in the growth inhibition and apoptosis induced by cadmium</title><title>Carcinogenesis (New York)</title><addtitle>Carcinogenesis</addtitle><description>Cadmium (Cd), a human carcinogen, can induce apoptosis in various cell types. Three major mitogen-activated protein kinases (MAPKs), c-JUN N-terminal kinase (JNK), p38 and extracellular signal-regulated kinase (ERK), have been shown to regulate apoptosis. In this study we explore the ability of Cd to activate JNK, p38 and ERK, including their effects on Cd-mediated growth inhibition and apoptosis in a human non-small cell lung carcinoma cell line, CL3. The kinase activity of JNK was induced dose-dependently by 30-160 microM CdCl(2). High cytotoxic doses of Cd (130-160 microM) markedly activated p38, but low Cd doses did not. Conversely, the activities of ERK1 and ERK2 were decreased by low cytotoxic doses of Cd (</=80 microM) and moderately activated by high Cd doses. Low cytotoxic doses of Cd transiently activated JNK and simultaneously reduced ERK activity, whereas high cytotoxic doses of Cd persistently activated JNK and p38. PD98059, an inhibitor of ERK upstream activators MAPK kinase (MKK) 1 and MKK2, greatly enhanced cytotoxicity and apoptosis in cells treated with low Cd doses. In contrast, SB202190, an inhibitor of p38, decreased the cytotoxicity and apoptosis induced by high Cd doses. Transient expression of a dominant negative form of JNK1, but not that of JNK2, significantly increased the viability and prevented apoptosis of Cd-treated cells. However, expression of wild-type JNK1 did not affect viability and apoptosis of Cd-treated cells. Transfection of wild-type JNK2 or p38 enhanced apoptosis of cells exposed to low Cd doses but did not affect those exposed to high Cd doses. The JNK activity stimulated by low Cd doses was partially suppressed by expression of a dominant negative form of MKK7, but not a dominant negative form of MKK4, indicating that MKK7 is involved in JNK activation by Cd. Together, the results of this study suggest that JNK and p38 cooperatively participate in apoptosis induced by Cd and that the decreased ERK signal induced by low Cd doses contributes to growth inhibition or apoptosis.</description><subject>Adenocarcinoma - enzymology</subject><subject>Adenocarcinoma - pathology</subject><subject>Apoptosis - drug effects</subject><subject>Apoptosis - physiology</subject><subject>Biological and medical sciences</subject><subject>Cadmium - toxicity</subject><subject>Cell Division - drug effects</subject><subject>Cell Division - physiology</subject><subject>Cell Survival - drug effects</subject><subject>DNA, Neoplasm - metabolism</subject><subject>Enzyme Activation - drug effects</subject><subject>Enzyme Activators</subject><subject>ERK protein</subject><subject>Gene Expression Regulation, Neoplastic - drug effects</subject><subject>Genes, jun</subject><subject>Growth Inhibitors - toxicity</subject><subject>Humans</subject><subject>JNK Mitogen-Activated Protein Kinases</subject><subject>JNK protein</subject><subject>lung carcinoma</subject><subject>Lung Neoplasms - enzymology</subject><subject>Lung Neoplasms - pathology</subject><subject>Male</subject><subject>MAP Kinase Kinase 4</subject><subject>MAP Kinase Kinase 7</subject><subject>Medical sciences</subject><subject>Middle Aged</subject><subject>Mitogen-Activated Protein Kinase Kinases - genetics</subject><subject>Mitogen-Activated Protein Kinase Kinases - metabolism</subject><subject>Mitogen-Activated Protein Kinase Kinases - physiology</subject><subject>Mitogen-Activated Protein Kinases - metabolism</subject><subject>Mitogen-Activated Protein Kinases - physiology</subject><subject>p38 Mitogen-Activated Protein Kinases</subject><subject>p38 protein</subject><subject>Pneumology</subject><subject>Proto-Oncogene Proteins c-jun - biosynthesis</subject><subject>Proto-Oncogene Proteins c-jun - genetics</subject><subject>Transcription Factor AP-1 - metabolism</subject><subject>Transfection</subject><subject>Tumor Cells, Cultured</subject><subject>Tumors of the respiratory system and mediastinum</subject><issn>0143-3334</issn><issn>1460-2180</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkd1rFTEQxYNU7G312TcJRfrUvTfJJPvxWEo_tEWh6HPIZpPe1N1km2SV_vem3guKTzMDv3OYmYPQe0rWlHSw0Spq5zeMrsWaM3iFVpTXpGK0JQdoRSiHCgD4ITpK6ZEQWoPo3qBDStqGE8ZWaLkPo0k4WPz5y-0ZnqHFyg_48v4WTy6HB-MrpbP7qbIZ8BxDNs7jH86rVFSlzVuDH2L4lbdl2rreZRf8Hws1hzmH5F6wYdFF3j9jrYbJLdNb9NqqMZl3-3qMvl9dfru4qe6-Xn-6OL-rNOtErljNhYCWt23LBdG94ZYLKhiYhtUWODGsB0oFrxsQtG9Agxi6hjPT28baAY7R6c63bP60mJTl5JI246i8CUuStBGipV1TwJP_wMewRF92k4x2UN5VkwJtdpCOIaVorJyjm1R8lpTIlzjkLo4ikUKWOIriw9526Scz_MPv_l-Aj3tAJa1GG5XXLv3leDmvhPYbShaSAA</recordid><startdate>200007</startdate><enddate>200007</enddate><creator>CHUANG, S.-M</creator><creator>WANG, I.-C</creator><creator>YANG, J.-L</creator><general>Oxford University Press</general><general>Oxford Publishing Limited (England)</general><scope>IQODW</scope><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>7T5</scope><scope>7TM</scope><scope>7TO</scope><scope>7U7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>P64</scope><scope>RC3</scope></search><sort><creationdate>200007</creationdate><title>Roles of JNK, p38 and ERK mitogen-activated protein kinases in the growth inhibition and apoptosis induced by cadmium</title><author>CHUANG, S.-M ; WANG, I.-C ; YANG, J.-L</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c295t-26455384888450cbe4f451523e726f340e2b3115467351b73c35d9742ebf7ffd3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Adenocarcinoma - enzymology</topic><topic>Adenocarcinoma - pathology</topic><topic>Apoptosis - drug effects</topic><topic>Apoptosis - physiology</topic><topic>Biological and medical sciences</topic><topic>Cadmium - toxicity</topic><topic>Cell Division - drug effects</topic><topic>Cell Division - physiology</topic><topic>Cell Survival - drug effects</topic><topic>DNA, Neoplasm - metabolism</topic><topic>Enzyme Activation - drug effects</topic><topic>Enzyme Activators</topic><topic>ERK protein</topic><topic>Gene Expression Regulation, Neoplastic - drug effects</topic><topic>Genes, jun</topic><topic>Growth Inhibitors - toxicity</topic><topic>Humans</topic><topic>JNK Mitogen-Activated Protein Kinases</topic><topic>JNK protein</topic><topic>lung carcinoma</topic><topic>Lung Neoplasms - enzymology</topic><topic>Lung Neoplasms - pathology</topic><topic>Male</topic><topic>MAP Kinase Kinase 4</topic><topic>MAP Kinase Kinase 7</topic><topic>Medical sciences</topic><topic>Middle Aged</topic><topic>Mitogen-Activated Protein Kinase Kinases - genetics</topic><topic>Mitogen-Activated Protein Kinase Kinases - metabolism</topic><topic>Mitogen-Activated Protein Kinase Kinases - physiology</topic><topic>Mitogen-Activated Protein Kinases - metabolism</topic><topic>Mitogen-Activated Protein Kinases - physiology</topic><topic>p38 Mitogen-Activated Protein Kinases</topic><topic>p38 protein</topic><topic>Pneumology</topic><topic>Proto-Oncogene Proteins c-jun - biosynthesis</topic><topic>Proto-Oncogene Proteins c-jun - genetics</topic><topic>Transcription Factor AP-1 - metabolism</topic><topic>Transfection</topic><topic>Tumor Cells, Cultured</topic><topic>Tumors of the respiratory system and mediastinum</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>CHUANG, S.-M</creatorcontrib><creatorcontrib>WANG, I.-C</creatorcontrib><creatorcontrib>YANG, J.-L</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Immunology Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Toxicology Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><jtitle>Carcinogenesis (New York)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>CHUANG, S.-M</au><au>WANG, I.-C</au><au>YANG, J.-L</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Roles of JNK, p38 and ERK mitogen-activated protein kinases in the growth inhibition and apoptosis induced by cadmium</atitle><jtitle>Carcinogenesis (New York)</jtitle><addtitle>Carcinogenesis</addtitle><date>2000-07</date><risdate>2000</risdate><volume>21</volume><issue>7</issue><spage>1423</spage><epage>1432</epage><pages>1423-1432</pages><issn>0143-3334</issn><eissn>1460-2180</eissn><coden>CRNGDP</coden><abstract>Cadmium (Cd), a human carcinogen, can induce apoptosis in various cell types. Three major mitogen-activated protein kinases (MAPKs), c-JUN N-terminal kinase (JNK), p38 and extracellular signal-regulated kinase (ERK), have been shown to regulate apoptosis. In this study we explore the ability of Cd to activate JNK, p38 and ERK, including their effects on Cd-mediated growth inhibition and apoptosis in a human non-small cell lung carcinoma cell line, CL3. The kinase activity of JNK was induced dose-dependently by 30-160 microM CdCl(2). High cytotoxic doses of Cd (130-160 microM) markedly activated p38, but low Cd doses did not. Conversely, the activities of ERK1 and ERK2 were decreased by low cytotoxic doses of Cd (</=80 microM) and moderately activated by high Cd doses. Low cytotoxic doses of Cd transiently activated JNK and simultaneously reduced ERK activity, whereas high cytotoxic doses of Cd persistently activated JNK and p38. PD98059, an inhibitor of ERK upstream activators MAPK kinase (MKK) 1 and MKK2, greatly enhanced cytotoxicity and apoptosis in cells treated with low Cd doses. In contrast, SB202190, an inhibitor of p38, decreased the cytotoxicity and apoptosis induced by high Cd doses. Transient expression of a dominant negative form of JNK1, but not that of JNK2, significantly increased the viability and prevented apoptosis of Cd-treated cells. However, expression of wild-type JNK1 did not affect viability and apoptosis of Cd-treated cells. Transfection of wild-type JNK2 or p38 enhanced apoptosis of cells exposed to low Cd doses but did not affect those exposed to high Cd doses. The JNK activity stimulated by low Cd doses was partially suppressed by expression of a dominant negative form of MKK7, but not a dominant negative form of MKK4, indicating that MKK7 is involved in JNK activation by Cd. Together, the results of this study suggest that JNK and p38 cooperatively participate in apoptosis induced by Cd and that the decreased ERK signal induced by low Cd doses contributes to growth inhibition or apoptosis.</abstract><cop>Oxford</cop><pub>Oxford University Press</pub><pmid>10874022</pmid><doi>10.1093/carcin/21.5.423</doi><tpages>10</tpages></addata></record> |
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| ispartof | Carcinogenesis (New York), 2000-07, Vol.21 (7), p.1423-1432 |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Oxford University Press Journals All Titles (1996-Current); Alma/SFX Local Collection |
| subjects | Adenocarcinoma - enzymology Adenocarcinoma - pathology Apoptosis - drug effects Apoptosis - physiology Biological and medical sciences Cadmium - toxicity Cell Division - drug effects Cell Division - physiology Cell Survival - drug effects DNA, Neoplasm - metabolism Enzyme Activation - drug effects Enzyme Activators ERK protein Gene Expression Regulation, Neoplastic - drug effects Genes, jun Growth Inhibitors - toxicity Humans JNK Mitogen-Activated Protein Kinases JNK protein lung carcinoma Lung Neoplasms - enzymology Lung Neoplasms - pathology Male MAP Kinase Kinase 4 MAP Kinase Kinase 7 Medical sciences Middle Aged Mitogen-Activated Protein Kinase Kinases - genetics Mitogen-Activated Protein Kinase Kinases - metabolism Mitogen-Activated Protein Kinase Kinases - physiology Mitogen-Activated Protein Kinases - metabolism Mitogen-Activated Protein Kinases - physiology p38 Mitogen-Activated Protein Kinases p38 protein Pneumology Proto-Oncogene Proteins c-jun - biosynthesis Proto-Oncogene Proteins c-jun - genetics Transcription Factor AP-1 - metabolism Transfection Tumor Cells, Cultured Tumors of the respiratory system and mediastinum |
| title | Roles of JNK, p38 and ERK mitogen-activated protein kinases in the growth inhibition and apoptosis induced by cadmium |
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