The immunosuppressive drugs cyclosporin A and tacrolimus inhibit membrane depolarization‐induced CREB transcriptional activity at the coactivator level
1 Cyclosporin A and tacrolimus are clinically important immunosuppressive drugs directly targeting the transcription factor nuclear factor of activated T cells (NFAT). Through inhibition of calcineurin phosphatase activity they block the dephosphorylation and thus activation of NFAT. Cyclosporin A a...
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| Veröffentlicht in: | British journal of pharmacology 2005-04, Vol.144 (7), p.982-993 |
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| creator | Oetjen, Elke Thoms, Kai‐Martin Laufer, Yvonne Pape, Daniela Blume, Roland Li, Pingfeng Knepel, Willhart |
| description | 1
Cyclosporin A and tacrolimus are clinically important immunosuppressive drugs directly targeting the transcription factor nuclear factor of activated T cells (NFAT). Through inhibition of calcineurin phosphatase activity they block the dephosphorylation and thus activation of NFAT. Cyclosporin A and tacrolimus also inhibit other calcineurin‐dependent transcription factors including the ubiquitously expressed cAMP response element‐binding protein (CREB). Membrane depolarization by phosphorylating CREB on Ser119 leads to the recruitment of its coactivator CREB‐binding protein (CBP) that stimulates initiation of transcription.
2
It was unknown at what step in CREB‐mediated transcription cyclosporin A and tacrolimus interfere.
3
In transient transfection experiments, using GAL4‐CREB fusion proteins and a pancreatic islet β‐cell line, cyclosporin A inhibited depolarization‐induced activation of CREB proteins which carried various deletions or mutations throughout their sequence providing no evidence for the existence of a distinct CREB domain conferring cyclosporin A sensitivity. In a mammalian two‐hybrid assay, cyclosporin A did not inhibit Ser119‐dependent interaction of CREB with its coactivator CBP.
4
Using GAL4‐CBP fusion proteins, cyclosporin A inhibited depolarization‐induced CBP activity, with cyclosporin A‐sensitive domains mapped to both the N‐ (aa 1–451) and C‐terminal (aa 2040–2305) ends of CBP. The depolarization‐induced transcriptional activity of the CBP C‐terminus was enhanced by overexpression of calcineurin and was inhibited by cyclosporin A and tacrolimus in a concentration‐dependent manner with IC50 values (10 and 1 nM, respectively) consistent with their known IC50 values for inhibition of calcineurin.
5
These data suggest that, in contrast to NFAT, cyclosporin A and tacrolimus inhibit CREB transcriptional activity at the coactivator level.
British Journal of Pharmacology (2005) 144, 982–993. doi:10.1038/sj.bjp.0706127 |
| doi_str_mv | 10.1038/sj.bjp.0706127 |
| format | Article |
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Cyclosporin A and tacrolimus are clinically important immunosuppressive drugs directly targeting the transcription factor nuclear factor of activated T cells (NFAT). Through inhibition of calcineurin phosphatase activity they block the dephosphorylation and thus activation of NFAT. Cyclosporin A and tacrolimus also inhibit other calcineurin‐dependent transcription factors including the ubiquitously expressed cAMP response element‐binding protein (CREB). Membrane depolarization by phosphorylating CREB on Ser119 leads to the recruitment of its coactivator CREB‐binding protein (CBP) that stimulates initiation of transcription.
2
It was unknown at what step in CREB‐mediated transcription cyclosporin A and tacrolimus interfere.
3
In transient transfection experiments, using GAL4‐CREB fusion proteins and a pancreatic islet β‐cell line, cyclosporin A inhibited depolarization‐induced activation of CREB proteins which carried various deletions or mutations throughout their sequence providing no evidence for the existence of a distinct CREB domain conferring cyclosporin A sensitivity. In a mammalian two‐hybrid assay, cyclosporin A did not inhibit Ser119‐dependent interaction of CREB with its coactivator CBP.
4
Using GAL4‐CBP fusion proteins, cyclosporin A inhibited depolarization‐induced CBP activity, with cyclosporin A‐sensitive domains mapped to both the N‐ (aa 1–451) and C‐terminal (aa 2040–2305) ends of CBP. The depolarization‐induced transcriptional activity of the CBP C‐terminus was enhanced by overexpression of calcineurin and was inhibited by cyclosporin A and tacrolimus in a concentration‐dependent manner with IC50 values (10 and 1 nM, respectively) consistent with their known IC50 values for inhibition of calcineurin.
5
These data suggest that, in contrast to NFAT, cyclosporin A and tacrolimus inhibit CREB transcriptional activity at the coactivator level.
British Journal of Pharmacology (2005) 144, 982–993. doi:10.1038/sj.bjp.0706127</description><identifier>ISSN: 0007-1188</identifier><identifier>EISSN: 1476-5381</identifier><identifier>DOI: 10.1038/sj.bjp.0706127</identifier><identifier>PMID: 15711594</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Animals ; calcineurin ; cAMP response element‐binding protein (CREB) ; CREB-Binding Protein ; CREB‐binding protein (CBP) ; Cricetinae ; Cyclic AMP Response Element-Binding Protein - biosynthesis ; Cyclic AMP Response Element-Binding Protein - genetics ; Cyclosporin A ; Cyclosporine - pharmacology ; Immunosuppressive Agents - pharmacology ; Islets of Langerhans - drug effects ; Islets of Langerhans - metabolism ; Membrane Potentials - drug effects ; Membrane Potentials - physiology ; Nuclear Proteins - biosynthesis ; Nuclear Proteins - genetics ; pancreatic β cell ; Tacrolimus - pharmacology ; Trans-Activators - biosynthesis ; Trans-Activators - genetics ; Transcription, Genetic - drug effects ; Transcription, Genetic - physiology</subject><ispartof>British journal of pharmacology, 2005-04, Vol.144 (7), p.982-993</ispartof><rights>2005 British Pharmacological Society</rights><rights>Copyright Nature Publishing Group Apr 2005</rights><rights>Copyright 2005, Nature Publishing Group 2005 Nature Publishing Group</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4597-652bf8517a77ab0bb1a565202994970d6d7e041302dca07f4767c591e019bb603</citedby><cites>FETCH-LOGICAL-c4597-652bf8517a77ab0bb1a565202994970d6d7e041302dca07f4767c591e019bb603</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/PMC1576078/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1576078/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,1416,1432,27923,27924,45573,45574,46408,46832,53790,53792</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15711594$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Oetjen, Elke</creatorcontrib><creatorcontrib>Thoms, Kai‐Martin</creatorcontrib><creatorcontrib>Laufer, Yvonne</creatorcontrib><creatorcontrib>Pape, Daniela</creatorcontrib><creatorcontrib>Blume, Roland</creatorcontrib><creatorcontrib>Li, Pingfeng</creatorcontrib><creatorcontrib>Knepel, Willhart</creatorcontrib><title>The immunosuppressive drugs cyclosporin A and tacrolimus inhibit membrane depolarization‐induced CREB transcriptional activity at the coactivator level</title><title>British journal of pharmacology</title><addtitle>Br J Pharmacol</addtitle><description>1
Cyclosporin A and tacrolimus are clinically important immunosuppressive drugs directly targeting the transcription factor nuclear factor of activated T cells (NFAT). Through inhibition of calcineurin phosphatase activity they block the dephosphorylation and thus activation of NFAT. Cyclosporin A and tacrolimus also inhibit other calcineurin‐dependent transcription factors including the ubiquitously expressed cAMP response element‐binding protein (CREB). Membrane depolarization by phosphorylating CREB on Ser119 leads to the recruitment of its coactivator CREB‐binding protein (CBP) that stimulates initiation of transcription.
2
It was unknown at what step in CREB‐mediated transcription cyclosporin A and tacrolimus interfere.
3
In transient transfection experiments, using GAL4‐CREB fusion proteins and a pancreatic islet β‐cell line, cyclosporin A inhibited depolarization‐induced activation of CREB proteins which carried various deletions or mutations throughout their sequence providing no evidence for the existence of a distinct CREB domain conferring cyclosporin A sensitivity. In a mammalian two‐hybrid assay, cyclosporin A did not inhibit Ser119‐dependent interaction of CREB with its coactivator CBP.
4
Using GAL4‐CBP fusion proteins, cyclosporin A inhibited depolarization‐induced CBP activity, with cyclosporin A‐sensitive domains mapped to both the N‐ (aa 1–451) and C‐terminal (aa 2040–2305) ends of CBP. The depolarization‐induced transcriptional activity of the CBP C‐terminus was enhanced by overexpression of calcineurin and was inhibited by cyclosporin A and tacrolimus in a concentration‐dependent manner with IC50 values (10 and 1 nM, respectively) consistent with their known IC50 values for inhibition of calcineurin.
5
These data suggest that, in contrast to NFAT, cyclosporin A and tacrolimus inhibit CREB transcriptional activity at the coactivator level.
British Journal of Pharmacology (2005) 144, 982–993. doi:10.1038/sj.bjp.0706127</description><subject>Animals</subject><subject>calcineurin</subject><subject>cAMP response element‐binding protein (CREB)</subject><subject>CREB-Binding Protein</subject><subject>CREB‐binding protein (CBP)</subject><subject>Cricetinae</subject><subject>Cyclic AMP Response Element-Binding Protein - biosynthesis</subject><subject>Cyclic AMP Response Element-Binding Protein - genetics</subject><subject>Cyclosporin A</subject><subject>Cyclosporine - pharmacology</subject><subject>Immunosuppressive Agents - pharmacology</subject><subject>Islets of Langerhans - drug effects</subject><subject>Islets of Langerhans - metabolism</subject><subject>Membrane Potentials - drug effects</subject><subject>Membrane Potentials - physiology</subject><subject>Nuclear Proteins - biosynthesis</subject><subject>Nuclear Proteins - genetics</subject><subject>pancreatic β cell</subject><subject>Tacrolimus - pharmacology</subject><subject>Trans-Activators - biosynthesis</subject><subject>Trans-Activators - genetics</subject><subject>Transcription, Genetic - drug effects</subject><subject>Transcription, Genetic - physiology</subject><issn>0007-1188</issn><issn>1476-5381</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqFkc1u1DAUhS0EotPCliWyWLDL4JvEcbJBakctRaoEQmVt2Y6n48ixg-1MNax4BLa8Hk-Chxnxt2F1pXu_e3R0DkLPgCyBVO2rOCzlMC0JIw2U7AFaQM2aglYtPEQLQggrANr2BJ3GOBCSj4w-RidAGQDt6gX6drvR2Izj7HycpynoGM1W4z7MdxGrnbI-Tj4Yh8-xcD1OQgVvzThHbNzGSJPwqEcZhMs_evJWBPNZJOPd9y9fjetnpXu8-nB5gVNmogpm2h-FxUIlszVph0XCKXtQ_udGJB-w1Vttn6BHa2GjfnqcZ-jj1eXt6rq4effm7er8plA17VjR0FKuWwpMMCYkkRIEzTtSdl3dMdI3PdOkhoqUvRKErXM8TNEONIFOyoZUZ-j1QXea5ah7pV22avkUzCjCjnth-N8XZzb8zm95DrEhrM0CL48CwX-adUx8NFFpa3Mofo68YU1HG6gy-OIfcPBzyGFEXgKDlrawt7M8QDnoGINe_3IChO8r53HguXJ-rDw_PP_T_2_82HEGqgNwb6ze_UeOX7y_LlnHqh9YI73j</recordid><startdate>200504</startdate><enddate>200504</enddate><creator>Oetjen, Elke</creator><creator>Thoms, Kai‐Martin</creator><creator>Laufer, Yvonne</creator><creator>Pape, Daniela</creator><creator>Blume, Roland</creator><creator>Li, Pingfeng</creator><creator>Knepel, Willhart</creator><general>Blackwell Publishing Ltd</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>3V.</scope><scope>7QP</scope><scope>7RV</scope><scope>7TK</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>NAPCQ</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>200504</creationdate><title>The immunosuppressive drugs cyclosporin A and tacrolimus inhibit membrane depolarization‐induced CREB transcriptional activity at the coactivator level</title><author>Oetjen, Elke ; Thoms, Kai‐Martin ; Laufer, Yvonne ; Pape, Daniela ; Blume, Roland ; Li, Pingfeng ; Knepel, Willhart</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4597-652bf8517a77ab0bb1a565202994970d6d7e041302dca07f4767c591e019bb603</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Animals</topic><topic>calcineurin</topic><topic>cAMP response element‐binding protein (CREB)</topic><topic>CREB-Binding Protein</topic><topic>CREB‐binding protein (CBP)</topic><topic>Cricetinae</topic><topic>Cyclic AMP Response Element-Binding Protein - biosynthesis</topic><topic>Cyclic AMP Response Element-Binding Protein - genetics</topic><topic>Cyclosporin A</topic><topic>Cyclosporine - pharmacology</topic><topic>Immunosuppressive Agents - pharmacology</topic><topic>Islets of Langerhans - drug effects</topic><topic>Islets of Langerhans - metabolism</topic><topic>Membrane Potentials - drug effects</topic><topic>Membrane Potentials - physiology</topic><topic>Nuclear Proteins - biosynthesis</topic><topic>Nuclear Proteins - genetics</topic><topic>pancreatic β cell</topic><topic>Tacrolimus - pharmacology</topic><topic>Trans-Activators - biosynthesis</topic><topic>Trans-Activators - genetics</topic><topic>Transcription, Genetic - drug effects</topic><topic>Transcription, Genetic - physiology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Oetjen, Elke</creatorcontrib><creatorcontrib>Thoms, Kai‐Martin</creatorcontrib><creatorcontrib>Laufer, Yvonne</creatorcontrib><creatorcontrib>Pape, Daniela</creatorcontrib><creatorcontrib>Blume, Roland</creatorcontrib><creatorcontrib>Li, Pingfeng</creatorcontrib><creatorcontrib>Knepel, Willhart</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Nursing & Allied Health Database</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>ProQuest Pharma Collection</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>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>Biological Science Database</collection><collection>Nursing & Allied Health Premium</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>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>British journal of pharmacology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Oetjen, Elke</au><au>Thoms, Kai‐Martin</au><au>Laufer, Yvonne</au><au>Pape, Daniela</au><au>Blume, Roland</au><au>Li, Pingfeng</au><au>Knepel, Willhart</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The immunosuppressive drugs cyclosporin A and tacrolimus inhibit membrane depolarization‐induced CREB transcriptional activity at the coactivator level</atitle><jtitle>British journal of pharmacology</jtitle><addtitle>Br J Pharmacol</addtitle><date>2005-04</date><risdate>2005</risdate><volume>144</volume><issue>7</issue><spage>982</spage><epage>993</epage><pages>982-993</pages><issn>0007-1188</issn><eissn>1476-5381</eissn><abstract>1
Cyclosporin A and tacrolimus are clinically important immunosuppressive drugs directly targeting the transcription factor nuclear factor of activated T cells (NFAT). Through inhibition of calcineurin phosphatase activity they block the dephosphorylation and thus activation of NFAT. Cyclosporin A and tacrolimus also inhibit other calcineurin‐dependent transcription factors including the ubiquitously expressed cAMP response element‐binding protein (CREB). Membrane depolarization by phosphorylating CREB on Ser119 leads to the recruitment of its coactivator CREB‐binding protein (CBP) that stimulates initiation of transcription.
2
It was unknown at what step in CREB‐mediated transcription cyclosporin A and tacrolimus interfere.
3
In transient transfection experiments, using GAL4‐CREB fusion proteins and a pancreatic islet β‐cell line, cyclosporin A inhibited depolarization‐induced activation of CREB proteins which carried various deletions or mutations throughout their sequence providing no evidence for the existence of a distinct CREB domain conferring cyclosporin A sensitivity. In a mammalian two‐hybrid assay, cyclosporin A did not inhibit Ser119‐dependent interaction of CREB with its coactivator CBP.
4
Using GAL4‐CBP fusion proteins, cyclosporin A inhibited depolarization‐induced CBP activity, with cyclosporin A‐sensitive domains mapped to both the N‐ (aa 1–451) and C‐terminal (aa 2040–2305) ends of CBP. The depolarization‐induced transcriptional activity of the CBP C‐terminus was enhanced by overexpression of calcineurin and was inhibited by cyclosporin A and tacrolimus in a concentration‐dependent manner with IC50 values (10 and 1 nM, respectively) consistent with their known IC50 values for inhibition of calcineurin.
5
These data suggest that, in contrast to NFAT, cyclosporin A and tacrolimus inhibit CREB transcriptional activity at the coactivator level.
British Journal of Pharmacology (2005) 144, 982–993. doi:10.1038/sj.bjp.0706127</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>15711594</pmid><doi>10.1038/sj.bjp.0706127</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Wiley Free Content; EZB-FREE-00999 freely available EZB journals; Wiley Online Library All Journals; PubMed Central; Alma/SFX Local Collection |
| subjects | Animals calcineurin cAMP response element‐binding protein (CREB) CREB-Binding Protein CREB‐binding protein (CBP) Cricetinae Cyclic AMP Response Element-Binding Protein - biosynthesis Cyclic AMP Response Element-Binding Protein - genetics Cyclosporin A Cyclosporine - pharmacology Immunosuppressive Agents - pharmacology Islets of Langerhans - drug effects Islets of Langerhans - metabolism Membrane Potentials - drug effects Membrane Potentials - physiology Nuclear Proteins - biosynthesis Nuclear Proteins - genetics pancreatic β cell Tacrolimus - pharmacology Trans-Activators - biosynthesis Trans-Activators - genetics Transcription, Genetic - drug effects Transcription, Genetic - physiology |
| title | The immunosuppressive drugs cyclosporin A and tacrolimus inhibit membrane depolarization‐induced CREB transcriptional activity at the coactivator level |
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