The Mitogen-Activated Protein Kinase p38-2 Is Necessary for the Inhibition of N-Type Calcium Current by Bradykinin
Calcium influx via voltage-dependent calcium channels (ICa,V) links depolarization of excitable cells to critical cellular processes, such as secretion, contraction, and gene transcription. Fast regulation of ICa,V (
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Veröffentlicht in: | The Journal of neuroscience 1998-01, Vol.18 (1), p.112-118 |
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creator | Wilk-Blaszczak, Malgorzata A Stein, Bernd Xu, Shuichan Barbosa, Miguel S Cobb, Melanie H Belardetti, Francesco |
description | Calcium influx via voltage-dependent calcium channels (ICa,V) links depolarization of excitable cells to critical cellular processes, such as secretion, contraction, and gene transcription. Fast regulation of ICa,V ( |
doi_str_mv | 10.1523/jneurosci.18-01-00112.1998 |
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Fast regulation of ICa,V (<1 sec) by G-protein-coupled receptors is a relatively well-defined mechanism, whereas slow (30-60 sec) actions of transmitters and hormones on the same current remain poorly understood. In NG108-15 cells, the kinetically slow inhibition of N-type ICa,V by bradykinin (BK) requires the sequential activation of two G-proteins, heterotrimeric G13 and monomeric Rac1/Cdc42. We have now defined a role in this pathway for the relatively fast-acting p38 mitogen-activated protein kinase (MAPK). The slow inhibition of ICa,V by BK was suppressed specifically by SB203580, a compound that inhibits the p38 family of MAPKs. BK potently and selectively activated a newly discovered p38 family member, p38-2. These data provide the first evidence that a MAPK is involved in the regulation of ICa,V by a receptor-mediated process.</description><identifier>ISSN: 0270-6474</identifier><identifier>EISSN: 1529-2401</identifier><identifier>DOI: 10.1523/jneurosci.18-01-00112.1998</identifier><identifier>PMID: 9412491</identifier><language>eng</language><publisher>United States: Soc Neuroscience</publisher><subject>Animals ; Arachidonic Acid - metabolism ; Bradykinin - pharmacology ; Calcium - metabolism ; Calcium Channels - physiology ; Calcium-Calmodulin-Dependent Protein Kinases - metabolism ; Enzyme Inhibitors - pharmacology ; Extracellular Space - enzymology ; Glioma ; GTP-Binding Proteins - physiology ; Hybrid Cells - chemistry ; Hybrid Cells - drug effects ; Hybrid Cells - enzymology ; Imidazoles - pharmacology ; Mice ; Mitogen-Activated Protein Kinases - metabolism ; Nerve Tissue Proteins - metabolism ; Neuroblastoma ; p38 Mitogen-Activated Protein Kinases ; Pyridines - pharmacology ; Rats ; Signal Transduction - drug effects ; Signal Transduction - physiology</subject><ispartof>The Journal of neuroscience, 1998-01, Vol.18 (1), p.112-118</ispartof><rights>Copyright © 1998 Society for Neuroscience 1998</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c548t-57ae7b4eaa6989ae6a8c1f5e23d580ebdf274ec7bb12ec47e25156f63b0b51453</citedby><cites>FETCH-LOGICAL-c548t-57ae7b4eaa6989ae6a8c1f5e23d580ebdf274ec7bb12ec47e25156f63b0b51453</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/PMC6793377/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC6793377/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9412491$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wilk-Blaszczak, Malgorzata A</creatorcontrib><creatorcontrib>Stein, Bernd</creatorcontrib><creatorcontrib>Xu, Shuichan</creatorcontrib><creatorcontrib>Barbosa, Miguel S</creatorcontrib><creatorcontrib>Cobb, Melanie H</creatorcontrib><creatorcontrib>Belardetti, Francesco</creatorcontrib><title>The Mitogen-Activated Protein Kinase p38-2 Is Necessary for the Inhibition of N-Type Calcium Current by Bradykinin</title><title>The Journal of neuroscience</title><addtitle>J Neurosci</addtitle><description>Calcium influx via voltage-dependent calcium channels (ICa,V) links depolarization of excitable cells to critical cellular processes, such as secretion, contraction, and gene transcription. Fast regulation of ICa,V (<1 sec) by G-protein-coupled receptors is a relatively well-defined mechanism, whereas slow (30-60 sec) actions of transmitters and hormones on the same current remain poorly understood. In NG108-15 cells, the kinetically slow inhibition of N-type ICa,V by bradykinin (BK) requires the sequential activation of two G-proteins, heterotrimeric G13 and monomeric Rac1/Cdc42. We have now defined a role in this pathway for the relatively fast-acting p38 mitogen-activated protein kinase (MAPK). The slow inhibition of ICa,V by BK was suppressed specifically by SB203580, a compound that inhibits the p38 family of MAPKs. BK potently and selectively activated a newly discovered p38 family member, p38-2. These data provide the first evidence that a MAPK is involved in the regulation of ICa,V by a receptor-mediated process.</description><subject>Animals</subject><subject>Arachidonic Acid - metabolism</subject><subject>Bradykinin - pharmacology</subject><subject>Calcium - metabolism</subject><subject>Calcium Channels - physiology</subject><subject>Calcium-Calmodulin-Dependent Protein Kinases - metabolism</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>Extracellular Space - enzymology</subject><subject>Glioma</subject><subject>GTP-Binding Proteins - physiology</subject><subject>Hybrid Cells - chemistry</subject><subject>Hybrid Cells - drug effects</subject><subject>Hybrid Cells - enzymology</subject><subject>Imidazoles - pharmacology</subject><subject>Mice</subject><subject>Mitogen-Activated Protein Kinases - metabolism</subject><subject>Nerve Tissue Proteins - metabolism</subject><subject>Neuroblastoma</subject><subject>p38 Mitogen-Activated Protein Kinases</subject><subject>Pyridines - pharmacology</subject><subject>Rats</subject><subject>Signal Transduction - drug effects</subject><subject>Signal Transduction - physiology</subject><issn>0270-6474</issn><issn>1529-2401</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkVFv0zAUhSMEGmXwE5AsJHhz8XWcOOEBaYvGVhgdgu7ZctybxiNxip2s6r_Ho9UETzzdh_Odo3N1kuQNsDlkPH1_53DyQzB2DgVlQBkD4HMoy-JJMotESblg8DSZMS4ZzYUUz5MXIdwxxiQDeZKclAK4KGGW-FWL5Ksdhw06emZGe69HXJNvfhjROvLFOh2QbNOCcrIIZIkGQ9B-T5rBkzF6F661tR3t4MjQkCVd7bdIKt0ZO_WkmrxHN5J6T869Xu9_Wmfdy-RZo7uAr473NLn9dLGqruj1zeWiOrumJhPFSDOpUdYCtc7LotSY68JAkyFP11nBsF43XAo0sq6BoxESeQZZ3uRpzeoMRJaeJh8Pudup7nFtYhGvO7X1to8PqEFb9a_ibKs2w73KZZmmUsaAd8cAP_yaMIyqt8Fg12mHwxSULPOUZQD_BSGPVUEUEfxwAE2cL3hsHtsAUw_Tqs_Li9vvNz-qhYJCMVB_plUP00bz67__ebQet4z624Pe2k27sx5V6HXXRRrUbreLeaBiWPobOO-waw</recordid><startdate>19980101</startdate><enddate>19980101</enddate><creator>Wilk-Blaszczak, Malgorzata A</creator><creator>Stein, Bernd</creator><creator>Xu, Shuichan</creator><creator>Barbosa, Miguel S</creator><creator>Cobb, Melanie H</creator><creator>Belardetti, Francesco</creator><general>Soc Neuroscience</general><general>Society for Neuroscience</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>7QP</scope><scope>7TK</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19980101</creationdate><title>The Mitogen-Activated Protein Kinase p38-2 Is Necessary for the Inhibition of N-Type Calcium Current by Bradykinin</title><author>Wilk-Blaszczak, Malgorzata A ; Stein, Bernd ; Xu, Shuichan ; Barbosa, Miguel S ; Cobb, Melanie H ; Belardetti, Francesco</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c548t-57ae7b4eaa6989ae6a8c1f5e23d580ebdf274ec7bb12ec47e25156f63b0b51453</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Animals</topic><topic>Arachidonic Acid - metabolism</topic><topic>Bradykinin - pharmacology</topic><topic>Calcium - metabolism</topic><topic>Calcium Channels - physiology</topic><topic>Calcium-Calmodulin-Dependent Protein Kinases - metabolism</topic><topic>Enzyme Inhibitors - pharmacology</topic><topic>Extracellular Space - enzymology</topic><topic>Glioma</topic><topic>GTP-Binding Proteins - physiology</topic><topic>Hybrid Cells - chemistry</topic><topic>Hybrid Cells - drug effects</topic><topic>Hybrid Cells - enzymology</topic><topic>Imidazoles - pharmacology</topic><topic>Mice</topic><topic>Mitogen-Activated Protein Kinases - metabolism</topic><topic>Nerve Tissue Proteins - metabolism</topic><topic>Neuroblastoma</topic><topic>p38 Mitogen-Activated Protein Kinases</topic><topic>Pyridines - pharmacology</topic><topic>Rats</topic><topic>Signal Transduction - drug effects</topic><topic>Signal Transduction - physiology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wilk-Blaszczak, Malgorzata A</creatorcontrib><creatorcontrib>Stein, Bernd</creatorcontrib><creatorcontrib>Xu, Shuichan</creatorcontrib><creatorcontrib>Barbosa, Miguel S</creatorcontrib><creatorcontrib>Cobb, Melanie H</creatorcontrib><creatorcontrib>Belardetti, Francesco</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The Journal of neuroscience</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wilk-Blaszczak, Malgorzata A</au><au>Stein, Bernd</au><au>Xu, Shuichan</au><au>Barbosa, Miguel S</au><au>Cobb, Melanie H</au><au>Belardetti, Francesco</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Mitogen-Activated Protein Kinase p38-2 Is Necessary for the Inhibition of N-Type Calcium Current by Bradykinin</atitle><jtitle>The Journal of neuroscience</jtitle><addtitle>J Neurosci</addtitle><date>1998-01-01</date><risdate>1998</risdate><volume>18</volume><issue>1</issue><spage>112</spage><epage>118</epage><pages>112-118</pages><issn>0270-6474</issn><eissn>1529-2401</eissn><abstract>Calcium influx via voltage-dependent calcium channels (ICa,V) links depolarization of excitable cells to critical cellular processes, such as secretion, contraction, and gene transcription. Fast regulation of ICa,V (<1 sec) by G-protein-coupled receptors is a relatively well-defined mechanism, whereas slow (30-60 sec) actions of transmitters and hormones on the same current remain poorly understood. In NG108-15 cells, the kinetically slow inhibition of N-type ICa,V by bradykinin (BK) requires the sequential activation of two G-proteins, heterotrimeric G13 and monomeric Rac1/Cdc42. We have now defined a role in this pathway for the relatively fast-acting p38 mitogen-activated protein kinase (MAPK). The slow inhibition of ICa,V by BK was suppressed specifically by SB203580, a compound that inhibits the p38 family of MAPKs. BK potently and selectively activated a newly discovered p38 family member, p38-2. These data provide the first evidence that a MAPK is involved in the regulation of ICa,V by a receptor-mediated process.</abstract><cop>United States</cop><pub>Soc Neuroscience</pub><pmid>9412491</pmid><doi>10.1523/jneurosci.18-01-00112.1998</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Animals Arachidonic Acid - metabolism Bradykinin - pharmacology Calcium - metabolism Calcium Channels - physiology Calcium-Calmodulin-Dependent Protein Kinases - metabolism Enzyme Inhibitors - pharmacology Extracellular Space - enzymology Glioma GTP-Binding Proteins - physiology Hybrid Cells - chemistry Hybrid Cells - drug effects Hybrid Cells - enzymology Imidazoles - pharmacology Mice Mitogen-Activated Protein Kinases - metabolism Nerve Tissue Proteins - metabolism Neuroblastoma p38 Mitogen-Activated Protein Kinases Pyridines - pharmacology Rats Signal Transduction - drug effects Signal Transduction - physiology |
title | The Mitogen-Activated Protein Kinase p38-2 Is Necessary for the Inhibition of N-Type Calcium Current by Bradykinin |
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