MAPK-activated protein kinase-2 participates in p38 MAPK-dependent and ERK-dependent functions in human neutrophils
Many neutrophil responses, including chemotaxis, exocytosis, respiratory burst activity and chemokine synthesis, are mediated by p38 MAPK. MAPK-activated protein kinase-2 (MK2) is activated by p38 MAPK in human neutrophils. The present study tested the hypothesis that MK2 mediates multiple p38 MAPK-...
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| Veröffentlicht in: | Cellular signalling 2003-11, Vol.15 (11), p.993-1001 |
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| creator | Coxon, PatriciaY Rane, MadhaviJ Uriarte, Silvia Powell, DavidW Singh, Saurabh Butt, Waseem Chen, Qingdan McLeish, KennethR |
| description | Many neutrophil responses, including chemotaxis, exocytosis, respiratory burst activity and chemokine synthesis, are mediated by p38 MAPK. MAPK-activated protein kinase-2 (MK2) is activated by p38 MAPK in human neutrophils. The present study tested the hypothesis that MK2 mediates multiple p38 MAPK-dependent responses in human neutrophils by comparing the effect of the p38 MAPK inhibitor, SB203580, with an MK2 inhibitory peptide. Both SB203580 and MK2 inhibitory peptide attenuated respiratory burst activity, exocytosis, and chemotaxis. Lipopolysaccharide (LPS)-induced IL-8 production was inhibited by SB203580, but not by the MK2 inhibitory peptide. Inhibition of chemotaxis and respiratory burst activity by SB203580 was less than that of MK2 inhibitory peptide. Inhibition of extracellular signal-regulated kinase (ERK) activity by PD98059 attenuated superoxide release and chemotaxis, and simultaneous treatment with SB203580 and PD98059 demonstrated additive inhibition. ERK phosphorylated MK2 in vitro and activated MK2 in
f-methionyl-leucyl-phenylalanine (FMLP)-stimulated neutrophils. These data suggest that MK2 mediates both ERK- and p38 MAPK-dependent neutrophil responses. |
| doi_str_mv | 10.1016/S0898-6568(03)00074-3 |
| format | Article |
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f-methionyl-leucyl-phenylalanine (FMLP)-stimulated neutrophils. These data suggest that MK2 mediates both ERK- and p38 MAPK-dependent neutrophil responses.</description><identifier>ISSN: 0898-6568</identifier><identifier>EISSN: 1873-3913</identifier><identifier>DOI: 10.1016/S0898-6568(03)00074-3</identifier><identifier>PMID: 14499342</identifier><language>eng</language><publisher>England: Elsevier Inc</publisher><subject>Cellular activation ; Chemotaxis, Leukocyte - physiology ; Enzyme Activation - physiology ; Enzyme Inhibitors - pharmacology ; Exocytosis - physiology ; Flavonoids - pharmacology ; Human ; Humans ; Imidazoles - pharmacology ; Interleukin-8 - metabolism ; Intracellular Signaling Peptides and Proteins ; Lipopolysaccharides - metabolism ; MAP Kinase Signaling System - physiology ; Mitogen-Activated Protein Kinases - metabolism ; N-Formylmethionine Leucyl-Phenylalanine - metabolism ; Neutrophil Activation - physiology ; Neutrophils ; Neutrophils - enzymology ; p38 Mitogen-Activated Protein Kinases ; Phosphorylation ; Protein Kinases ; Protein kinases/phosphatases ; Protein-Serine-Threonine Kinases ; Pyridines - pharmacology ; Respiratory Burst - physiology ; Signal transduction ; Signal Transduction - physiology ; Superoxides - metabolism</subject><ispartof>Cellular signalling, 2003-11, Vol.15 (11), p.993-1001</ispartof><rights>2003</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c392t-d4ec557468327baacf9ecab249fe0dc0956ebc90648a5abad53e124ac18e75103</citedby><cites>FETCH-LOGICAL-c392t-d4ec557468327baacf9ecab249fe0dc0956ebc90648a5abad53e124ac18e75103</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0898-6568(03)00074-3$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/14499342$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Coxon, PatriciaY</creatorcontrib><creatorcontrib>Rane, MadhaviJ</creatorcontrib><creatorcontrib>Uriarte, Silvia</creatorcontrib><creatorcontrib>Powell, DavidW</creatorcontrib><creatorcontrib>Singh, Saurabh</creatorcontrib><creatorcontrib>Butt, Waseem</creatorcontrib><creatorcontrib>Chen, Qingdan</creatorcontrib><creatorcontrib>McLeish, KennethR</creatorcontrib><title>MAPK-activated protein kinase-2 participates in p38 MAPK-dependent and ERK-dependent functions in human neutrophils</title><title>Cellular signalling</title><addtitle>Cell Signal</addtitle><description>Many neutrophil responses, including chemotaxis, exocytosis, respiratory burst activity and chemokine synthesis, are mediated by p38 MAPK. MAPK-activated protein kinase-2 (MK2) is activated by p38 MAPK in human neutrophils. The present study tested the hypothesis that MK2 mediates multiple p38 MAPK-dependent responses in human neutrophils by comparing the effect of the p38 MAPK inhibitor, SB203580, with an MK2 inhibitory peptide. Both SB203580 and MK2 inhibitory peptide attenuated respiratory burst activity, exocytosis, and chemotaxis. Lipopolysaccharide (LPS)-induced IL-8 production was inhibited by SB203580, but not by the MK2 inhibitory peptide. Inhibition of chemotaxis and respiratory burst activity by SB203580 was less than that of MK2 inhibitory peptide. Inhibition of extracellular signal-regulated kinase (ERK) activity by PD98059 attenuated superoxide release and chemotaxis, and simultaneous treatment with SB203580 and PD98059 demonstrated additive inhibition. ERK phosphorylated MK2 in vitro and activated MK2 in
f-methionyl-leucyl-phenylalanine (FMLP)-stimulated neutrophils. These data suggest that MK2 mediates both ERK- and p38 MAPK-dependent neutrophil responses.</description><subject>Cellular activation</subject><subject>Chemotaxis, Leukocyte - physiology</subject><subject>Enzyme Activation - physiology</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>Exocytosis - physiology</subject><subject>Flavonoids - pharmacology</subject><subject>Human</subject><subject>Humans</subject><subject>Imidazoles - pharmacology</subject><subject>Interleukin-8 - metabolism</subject><subject>Intracellular Signaling Peptides and Proteins</subject><subject>Lipopolysaccharides - metabolism</subject><subject>MAP Kinase Signaling System - physiology</subject><subject>Mitogen-Activated Protein Kinases - metabolism</subject><subject>N-Formylmethionine Leucyl-Phenylalanine - metabolism</subject><subject>Neutrophil Activation - physiology</subject><subject>Neutrophils</subject><subject>Neutrophils - enzymology</subject><subject>p38 Mitogen-Activated Protein Kinases</subject><subject>Phosphorylation</subject><subject>Protein Kinases</subject><subject>Protein kinases/phosphatases</subject><subject>Protein-Serine-Threonine Kinases</subject><subject>Pyridines - pharmacology</subject><subject>Respiratory Burst - physiology</subject><subject>Signal transduction</subject><subject>Signal Transduction - physiology</subject><subject>Superoxides - metabolism</subject><issn>0898-6568</issn><issn>1873-3913</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUtP3TAQhS1UBLeUn0CVVUUXKeNn4lWFELSoIKo-1pZjT4Tbe51gO0j8e3IfatmxGmnmO3M0cwg5ofCJAlVnP6HVba2kak-BfwSARtR8jyxo2_Caa8rfkMU_5JC8zfkPAJWg2AE5pEJozQVbkHx7_v1bbV0Jj7agr8Y0FAyx-huizVizarSpBBfGeZqreTDyttpoPI4YPcZS2eiryx8vO_0U541D3Cjup5WNVcSppGG8D8v8juz3dpnxeFePyO-ry18XX-ubuy_XF-c3teOaldoLdFI2QrWcNZ21rtfobMeE7hG8Ay0Vdk6DEq2VtrNecqRMWEdbbCQFfkQ-bPfORz1MmItZhexwubQRhymbhisppOKvggxUo1gjZ1BuQZeGnBP2ZkxhZdOToWDWsZhNLGb9cwPcbGIxa4P3O4OpW6H_r9rlMAOftwDO_3gMmEx2AaNDHxK6YvwQXrF4BsZGnXY</recordid><startdate>20031101</startdate><enddate>20031101</enddate><creator>Coxon, PatriciaY</creator><creator>Rane, MadhaviJ</creator><creator>Uriarte, Silvia</creator><creator>Powell, DavidW</creator><creator>Singh, Saurabh</creator><creator>Butt, Waseem</creator><creator>Chen, Qingdan</creator><creator>McLeish, KennethR</creator><general>Elsevier Inc</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>7QR</scope><scope>7T5</scope><scope>8FD</scope><scope>FR3</scope><scope>H94</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>20031101</creationdate><title>MAPK-activated protein kinase-2 participates in p38 MAPK-dependent and ERK-dependent functions in human neutrophils</title><author>Coxon, PatriciaY ; 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MAPK-activated protein kinase-2 (MK2) is activated by p38 MAPK in human neutrophils. The present study tested the hypothesis that MK2 mediates multiple p38 MAPK-dependent responses in human neutrophils by comparing the effect of the p38 MAPK inhibitor, SB203580, with an MK2 inhibitory peptide. Both SB203580 and MK2 inhibitory peptide attenuated respiratory burst activity, exocytosis, and chemotaxis. Lipopolysaccharide (LPS)-induced IL-8 production was inhibited by SB203580, but not by the MK2 inhibitory peptide. Inhibition of chemotaxis and respiratory burst activity by SB203580 was less than that of MK2 inhibitory peptide. Inhibition of extracellular signal-regulated kinase (ERK) activity by PD98059 attenuated superoxide release and chemotaxis, and simultaneous treatment with SB203580 and PD98059 demonstrated additive inhibition. ERK phosphorylated MK2 in vitro and activated MK2 in
f-methionyl-leucyl-phenylalanine (FMLP)-stimulated neutrophils. These data suggest that MK2 mediates both ERK- and p38 MAPK-dependent neutrophil responses.</abstract><cop>England</cop><pub>Elsevier Inc</pub><pmid>14499342</pmid><doi>10.1016/S0898-6568(03)00074-3</doi><tpages>9</tpages></addata></record> |
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| subjects | Cellular activation Chemotaxis, Leukocyte - physiology Enzyme Activation - physiology Enzyme Inhibitors - pharmacology Exocytosis - physiology Flavonoids - pharmacology Human Humans Imidazoles - pharmacology Interleukin-8 - metabolism Intracellular Signaling Peptides and Proteins Lipopolysaccharides - metabolism MAP Kinase Signaling System - physiology Mitogen-Activated Protein Kinases - metabolism N-Formylmethionine Leucyl-Phenylalanine - metabolism Neutrophil Activation - physiology Neutrophils Neutrophils - enzymology p38 Mitogen-Activated Protein Kinases Phosphorylation Protein Kinases Protein kinases/phosphatases Protein-Serine-Threonine Kinases Pyridines - pharmacology Respiratory Burst - physiology Signal transduction Signal Transduction - physiology Superoxides - metabolism |
| title | MAPK-activated protein kinase-2 participates in p38 MAPK-dependent and ERK-dependent functions in human neutrophils |
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