p38 Mitogen-Activated Protein Kinase Controls NF-κB Transcriptional Activation and Tumor Necrosis Factor Alpha Production through RelA Phosphorylation Mediated by Mitogen- and Stress-Activated Protein Kinase 1 in Response to Borrelia burgdorferi Antigens
The interaction of Borrelia burgdorferi, the causative agent of Lyme borreliosis, with phagocytic cells induces the activation of NF-κB and the expression of proinflammatory cytokines including tumor necrosis factor alpha (TNF-α). B. burgdorferi-induced TNF-α production is also dependent on the acti...
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description | The interaction of Borrelia burgdorferi, the causative agent of Lyme borreliosis, with phagocytic cells induces the activation of NF-κB and the expression of proinflammatory cytokines including tumor necrosis factor alpha (TNF-α). B. burgdorferi-induced TNF-α production is also dependent on the activation of p38 mitogen-activated protein (MAP) kinase. The specific contribution of these signaling pathways to the response of phagocytic cells to the spirochete and the molecular mechanisms underlying this response remain unresolved. We now show that p38 MAP kinase activity regulates the transcriptional activation of NF-κB in response to spirochetal lysate stimulation of phagocytic cells. The regulation occurs at the nuclear level and is independent of the translocation of the transcription factor to the nucleus or its capacity to bind to specific DNA target sequences. In RAW264.7 cells, p38α MAP kinase regulates the phosphorylation of NF-κB RelA. p38 MAP kinase phosphorylates the nuclear kinase mitogen- and stress-activated protein kinase 1 (MSK1). MSK1 in turn phosphorylates the transcriptionally active subunit of NF-κB, RelA. The repression of MSK1 expression with small interfering RNA results in reduced RelA phosphorylation and a significant decrease in the production of TNF-α in response to B. burgdorferi lysates. Overall, these results clarify the contribution of the signaling pathways that are activated in response to the interaction of spirochetes with phagocytic cells to TNF-α production. Our results situate p38 MAP kinase activity as a central regulator of the phagocytic proinflammatory response through MSK1-mediated transcriptional activation of the transcription factor NF-κB. |
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B. burgdorferi-induced TNF-α production is also dependent on the activation of p38 mitogen-activated protein (MAP) kinase. The specific contribution of these signaling pathways to the response of phagocytic cells to the spirochete and the molecular mechanisms underlying this response remain unresolved. We now show that p38 MAP kinase activity regulates the transcriptional activation of NF-κB in response to spirochetal lysate stimulation of phagocytic cells. The regulation occurs at the nuclear level and is independent of the translocation of the transcription factor to the nucleus or its capacity to bind to specific DNA target sequences. In RAW264.7 cells, p38α MAP kinase regulates the phosphorylation of NF-κB RelA. p38 MAP kinase phosphorylates the nuclear kinase mitogen- and stress-activated protein kinase 1 (MSK1). MSK1 in turn phosphorylates the transcriptionally active subunit of NF-κB, RelA. The repression of MSK1 expression with small interfering RNA results in reduced RelA phosphorylation and a significant decrease in the production of TNF-α in response to B. burgdorferi lysates. Overall, these results clarify the contribution of the signaling pathways that are activated in response to the interaction of spirochetes with phagocytic cells to TNF-α production. Our results situate p38 MAP kinase activity as a central regulator of the phagocytic proinflammatory response through MSK1-mediated transcriptional activation of the transcription factor NF-κB.</description><identifier>ISSN: 0019-9567</identifier><identifier>EISSN: 1098-5522</identifier><identifier>DOI: 10.1128/IAI.01412-06</identifier><identifier>PMID: 17074860</identifier><identifier>CODEN: INFIBR</identifier><language>eng</language><publisher>Washington, DC: American Society for Microbiology</publisher><subject>antigens ; Bacteriology ; Biological and medical sciences ; Borrelia burgdorferi ; DNA ; Fundamental and applied biological sciences. Psychology ; Host Response and Inflammation ; Lyme disease ; Microbiology ; Miscellaneous ; mitogen-activated protein kinase ; phosphorylase kinase ; phosphorylation ; signal transduction ; small interfering RNA ; transcription factors ; transcriptional activation ; tumor necrosis factor-alpha</subject><ispartof>Infection and Immunity, 2007-01, Vol.75 (1), p.270-277</ispartof><rights>2007 INIST-CNRS</rights><rights>Copyright © 2007, American Society for Microbiology 2007</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c438t-a557d0f5c7249cd08fe93400978b25ab72e0c7515dc185a7939f0ffee643d6213</citedby><cites>FETCH-LOGICAL-c438t-a557d0f5c7249cd08fe93400978b25ab72e0c7515dc185a7939f0ffee643d6213</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1828394/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1828394/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,3188,3189,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=18614922$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>Olson, Chris M</creatorcontrib><creatorcontrib>Hedrick, Michael N</creatorcontrib><creatorcontrib>Izadi, Hooman</creatorcontrib><creatorcontrib>Bates, Tonya C</creatorcontrib><creatorcontrib>Olivera, Elias R</creatorcontrib><creatorcontrib>Anguita, Juan</creatorcontrib><title>p38 Mitogen-Activated Protein Kinase Controls NF-κB Transcriptional Activation and Tumor Necrosis Factor Alpha Production through RelA Phosphorylation Mediated by Mitogen- and Stress-Activated Protein Kinase 1 in Response to Borrelia burgdorferi Antigens</title><title>Infection and Immunity</title><description>The interaction of Borrelia burgdorferi, the causative agent of Lyme borreliosis, with phagocytic cells induces the activation of NF-κB and the expression of proinflammatory cytokines including tumor necrosis factor alpha (TNF-α). B. burgdorferi-induced TNF-α production is also dependent on the activation of p38 mitogen-activated protein (MAP) kinase. The specific contribution of these signaling pathways to the response of phagocytic cells to the spirochete and the molecular mechanisms underlying this response remain unresolved. We now show that p38 MAP kinase activity regulates the transcriptional activation of NF-κB in response to spirochetal lysate stimulation of phagocytic cells. The regulation occurs at the nuclear level and is independent of the translocation of the transcription factor to the nucleus or its capacity to bind to specific DNA target sequences. In RAW264.7 cells, p38α MAP kinase regulates the phosphorylation of NF-κB RelA. p38 MAP kinase phosphorylates the nuclear kinase mitogen- and stress-activated protein kinase 1 (MSK1). MSK1 in turn phosphorylates the transcriptionally active subunit of NF-κB, RelA. The repression of MSK1 expression with small interfering RNA results in reduced RelA phosphorylation and a significant decrease in the production of TNF-α in response to B. burgdorferi lysates. Overall, these results clarify the contribution of the signaling pathways that are activated in response to the interaction of spirochetes with phagocytic cells to TNF-α production. Our results situate p38 MAP kinase activity as a central regulator of the phagocytic proinflammatory response through MSK1-mediated transcriptional activation of the transcription factor NF-κB.</description><subject>antigens</subject><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Borrelia burgdorferi</subject><subject>DNA</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Host Response and Inflammation</subject><subject>Lyme disease</subject><subject>Microbiology</subject><subject>Miscellaneous</subject><subject>mitogen-activated protein kinase</subject><subject>phosphorylase kinase</subject><subject>phosphorylation</subject><subject>signal transduction</subject><subject>small interfering RNA</subject><subject>transcription factors</subject><subject>transcriptional activation</subject><subject>tumor necrosis factor-alpha</subject><issn>0019-9567</issn><issn>1098-5522</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><recordid>eNp1ks1u1DAUhSMEokNhxx5vYEWK7cSxvUFKRwyMaEvVTteWx3ESI0-c2k7RvBoPwSuB50dFLFjZVz73u0fXJ8teI3iGEGYflvXyDKIS4RxWT7IZgpzlhGD8NJtBiHjOSUVPshchfE9lWZbseXaCKKQlq-As-z0WDFya6Do95LWK5kFG3YBr76I2A_hqBhk0mLshemcDuFrkv36eg5WXQ1DejNG4QVpwbEwFkEMDVtPGeXCllXfBBLCQKqa6tmMvd-RmUntp7L2buh7caFuD696FsXd-aw-cS92YvZX19tHfHn4bvQ7h_14RSPcbHUY3pCo6cO6819ZIsJ581zjfam9APUSTkOFl9qyVNuhXx_M0u1t8Ws2_5BffPi_n9UWuyoLFXBJCG9gSRXHJVQNZq3lRQsgpW2Mi1xRrqChBpFGIEUl5wVvYtlpXZdFUGBWn2ccDd5zWG90onRYqrRi92Ui_FU4a8e_LYHrRuQeBGGYFLxPg3RHg3f2kQxQbE5S2Vg7aTUEgTnBRFDQJ3x-Eu-0Hr9vHIQiKXWJESozYJ0bAKsnfHrkyKGnb9LPKhL89rEIlxzjpwEHXm67_YbwWMmyESb4pEUhgCpPkzUHSSidk5xPm7hanSSl4jO-28Adw5do0</recordid><startdate>20070101</startdate><enddate>20070101</enddate><creator>Olson, Chris M</creator><creator>Hedrick, Michael N</creator><creator>Izadi, Hooman</creator><creator>Bates, Tonya C</creator><creator>Olivera, Elias R</creator><creator>Anguita, Juan</creator><general>American Society for Microbiology</general><scope>FBQ</scope><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7T5</scope><scope>C1K</scope><scope>H94</scope><scope>5PM</scope></search><sort><creationdate>20070101</creationdate><title>p38 Mitogen-Activated Protein Kinase Controls NF-κB Transcriptional Activation and Tumor Necrosis Factor Alpha Production through RelA Phosphorylation Mediated by Mitogen- and Stress-Activated Protein Kinase 1 in Response to Borrelia burgdorferi Antigens</title><author>Olson, Chris M ; Hedrick, Michael N ; Izadi, Hooman ; Bates, Tonya C ; Olivera, Elias R ; Anguita, Juan</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c438t-a557d0f5c7249cd08fe93400978b25ab72e0c7515dc185a7939f0ffee643d6213</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>antigens</topic><topic>Bacteriology</topic><topic>Biological and medical sciences</topic><topic>Borrelia burgdorferi</topic><topic>DNA</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Host Response and Inflammation</topic><topic>Lyme disease</topic><topic>Microbiology</topic><topic>Miscellaneous</topic><topic>mitogen-activated protein kinase</topic><topic>phosphorylase kinase</topic><topic>phosphorylation</topic><topic>signal transduction</topic><topic>small interfering RNA</topic><topic>transcription factors</topic><topic>transcriptional activation</topic><topic>tumor necrosis factor-alpha</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Olson, Chris M</creatorcontrib><creatorcontrib>Hedrick, Michael N</creatorcontrib><creatorcontrib>Izadi, Hooman</creatorcontrib><creatorcontrib>Bates, Tonya C</creatorcontrib><creatorcontrib>Olivera, Elias R</creatorcontrib><creatorcontrib>Anguita, Juan</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Immunology Abstracts</collection><collection>Environmental Sciences and Pollution Management</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Infection and Immunity</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Olson, Chris M</au><au>Hedrick, Michael N</au><au>Izadi, Hooman</au><au>Bates, Tonya C</au><au>Olivera, Elias R</au><au>Anguita, Juan</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>p38 Mitogen-Activated Protein Kinase Controls NF-κB Transcriptional Activation and Tumor Necrosis Factor Alpha Production through RelA Phosphorylation Mediated by Mitogen- and Stress-Activated Protein Kinase 1 in Response to Borrelia burgdorferi Antigens</atitle><jtitle>Infection and Immunity</jtitle><date>2007-01-01</date><risdate>2007</risdate><volume>75</volume><issue>1</issue><spage>270</spage><epage>277</epage><pages>270-277</pages><issn>0019-9567</issn><eissn>1098-5522</eissn><coden>INFIBR</coden><abstract>The interaction of Borrelia burgdorferi, the causative agent of Lyme borreliosis, with phagocytic cells induces the activation of NF-κB and the expression of proinflammatory cytokines including tumor necrosis factor alpha (TNF-α). B. burgdorferi-induced TNF-α production is also dependent on the activation of p38 mitogen-activated protein (MAP) kinase. The specific contribution of these signaling pathways to the response of phagocytic cells to the spirochete and the molecular mechanisms underlying this response remain unresolved. We now show that p38 MAP kinase activity regulates the transcriptional activation of NF-κB in response to spirochetal lysate stimulation of phagocytic cells. The regulation occurs at the nuclear level and is independent of the translocation of the transcription factor to the nucleus or its capacity to bind to specific DNA target sequences. In RAW264.7 cells, p38α MAP kinase regulates the phosphorylation of NF-κB RelA. p38 MAP kinase phosphorylates the nuclear kinase mitogen- and stress-activated protein kinase 1 (MSK1). MSK1 in turn phosphorylates the transcriptionally active subunit of NF-κB, RelA. The repression of MSK1 expression with small interfering RNA results in reduced RelA phosphorylation and a significant decrease in the production of TNF-α in response to B. burgdorferi lysates. Overall, these results clarify the contribution of the signaling pathways that are activated in response to the interaction of spirochetes with phagocytic cells to TNF-α production. Our results situate p38 MAP kinase activity as a central regulator of the phagocytic proinflammatory response through MSK1-mediated transcriptional activation of the transcription factor NF-κB.</abstract><cop>Washington, DC</cop><pub>American Society for Microbiology</pub><pmid>17074860</pmid><doi>10.1128/IAI.01412-06</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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subjects | antigens Bacteriology Biological and medical sciences Borrelia burgdorferi DNA Fundamental and applied biological sciences. Psychology Host Response and Inflammation Lyme disease Microbiology Miscellaneous mitogen-activated protein kinase phosphorylase kinase phosphorylation signal transduction small interfering RNA transcription factors transcriptional activation tumor necrosis factor-alpha |
title | p38 Mitogen-Activated Protein Kinase Controls NF-κB Transcriptional Activation and Tumor Necrosis Factor Alpha Production through RelA Phosphorylation Mediated by Mitogen- and Stress-Activated Protein Kinase 1 in Response to Borrelia burgdorferi Antigens |
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