SHP-1 inhibits LPS-mediated TNF and iNOS production in murine macrophages
Several lines of evidence have suggested that protein tyrosine phosphatases, including CD45 and SHP-1, regulate macrophage activation. Macrophages from mice lacking SHP-1 (motheaten mice) are hyper-responsive to many stimuli, suggesting that SHP-1 may negatively regulate macrophage activation. Herei...
Gespeichert in:
| Veröffentlicht in: | Biochemical and biophysical research communications 2006-04, Vol.342 (2), p.547-555 |
|---|---|
| Hauptverfasser: | , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 555 |
|---|---|
| container_issue | 2 |
| container_start_page | 547 |
| container_title | Biochemical and biophysical research communications |
| container_volume | 342 |
| creator | Hardin, Amy O. Meals, Elizabeth A. Yi, Taolin Knapp, Katherine M. English, B. Keith |
| description | Several lines of evidence have suggested that protein tyrosine phosphatases, including CD45 and SHP-1, regulate macrophage activation. Macrophages from mice lacking SHP-1 (motheaten mice) are hyper-responsive to many stimuli, suggesting that SHP-1 may negatively regulate macrophage activation. Herein we report that the repressible/inducible over-expression of wild-type SHP-1 in a subclone of RAW 264.7 macrophages (RAW-TT10 cells) inhibited both TNF secretion and iNOS protein accumulation in response to stimulation with lipopolysaccharide (LPS) and recombinant murine interferon-gamma and led to diminished LPS-mediated tyrosine phosphorylation of
vav1. In contrast, expression of a truncated SHP-1 construct previously shown to interfere with endogenous SHP-1 function modestly augmented LPS-mediated TNF and iNOS production and did not inhibit
vav1 tyrosine phosphorylation. Taken together, these data provide the first direct evidence that SHP-1 inhibits macrophage activation by LPS and suggest that this effect may be mediated in part by dephosphorylation of
vav1. |
| doi_str_mv | 10.1016/j.bbrc.2006.02.005 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_67694618</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0006291X06002889</els_id><sourcerecordid>17106289</sourcerecordid><originalsourceid>FETCH-LOGICAL-c385t-9ff90e5a6423d02499b4a84b49c690feb78d51c00ea9cd781142e1a33211bfad3</originalsourceid><addsrcrecordid>eNqFkMFqGzEQhkVpqN0kL9BD2VNvu5nRytoV9FJM0hhMEnACuQmtNFvLeHddabfQt6-MDb0lpznM9__MfIx9QSgQUN7siqYJtuAAsgBeACw-sDmCgpwjiI9sDmmTc4WvM_Y5xh0AopDqE5uhFHWlSj5nq839U46Z77e-8WPM1k-bvCPnzUgue364y0zvMv_wuMkOYXCTHf3QJzrrpuB7yjpjw3DYml8Ur9hFa_aRrs_zkr3c3T4v7_P148_V8sc6t2W9GHPVtgpoYaTgpQMulGqEqUUjlJUKWmqq2i3QApBR1lV1OpkTmrLkiE1rXHnJvp1600G_J4qj7ny0tN-bnoYpallJJSTW74JYIUheqwTyE5h-iTFQqw_Bdyb81Qj6aFrv9NG0PprWwHUynUJfz-1Tk4T9j5zVJuD7CaAk44-noKP11NskN5AdtRv8W_3_AP_wjT4</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>17106289</pqid></control><display><type>article</type><title>SHP-1 inhibits LPS-mediated TNF and iNOS production in murine macrophages</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals</source><creator>Hardin, Amy O. ; Meals, Elizabeth A. ; Yi, Taolin ; Knapp, Katherine M. ; English, B. Keith</creator><creatorcontrib>Hardin, Amy O. ; Meals, Elizabeth A. ; Yi, Taolin ; Knapp, Katherine M. ; English, B. Keith</creatorcontrib><description>Several lines of evidence have suggested that protein tyrosine phosphatases, including CD45 and SHP-1, regulate macrophage activation. Macrophages from mice lacking SHP-1 (motheaten mice) are hyper-responsive to many stimuli, suggesting that SHP-1 may negatively regulate macrophage activation. Herein we report that the repressible/inducible over-expression of wild-type SHP-1 in a subclone of RAW 264.7 macrophages (RAW-TT10 cells) inhibited both TNF secretion and iNOS protein accumulation in response to stimulation with lipopolysaccharide (LPS) and recombinant murine interferon-gamma and led to diminished LPS-mediated tyrosine phosphorylation of
vav1. In contrast, expression of a truncated SHP-1 construct previously shown to interfere with endogenous SHP-1 function modestly augmented LPS-mediated TNF and iNOS production and did not inhibit
vav1 tyrosine phosphorylation. Taken together, these data provide the first direct evidence that SHP-1 inhibits macrophage activation by LPS and suggest that this effect may be mediated in part by dephosphorylation of
vav1.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/j.bbrc.2006.02.005</identifier><identifier>PMID: 16487932</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Cell Line ; Cells, Cultured ; Clone Cells ; Cytokine ; Enzyme Inhibitors - pharmacology ; iNOS ; Interferon-gamma - pharmacology ; Intracellular Signaling Peptides and Proteins - physiology ; Kinase ; Lipopolysaccharides - pharmacology ; Macrophage ; Macrophage Activation - immunology ; Macrophages - enzymology ; Macrophages - immunology ; Mice ; Nitric Oxide Synthase Type II - antagonists & inhibitors ; Nitric Oxide Synthase Type II - biosynthesis ; Phosphatase ; Phosphorylation ; Protein Tyrosine Phosphatase, Non-Receptor Type 6 ; Protein Tyrosine Phosphatases - physiology ; Proto-Oncogene Proteins c-vav - antagonists & inhibitors ; Proto-Oncogene Proteins c-vav - metabolism ; Recombinant Proteins ; SHP-1 ; Signal transduction ; Tetracycline - pharmacology ; TNF ; Transfection ; Tumor Necrosis Factor-alpha - antagonists & inhibitors ; Tumor Necrosis Factor-alpha - biosynthesis ; Tyrosine</subject><ispartof>Biochemical and biophysical research communications, 2006-04, Vol.342 (2), p.547-555</ispartof><rights>2006 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c385t-9ff90e5a6423d02499b4a84b49c690feb78d51c00ea9cd781142e1a33211bfad3</citedby><cites>FETCH-LOGICAL-c385t-9ff90e5a6423d02499b4a84b49c690feb78d51c00ea9cd781142e1a33211bfad3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.bbrc.2006.02.005$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,778,782,3539,27907,27908,45978</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16487932$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hardin, Amy O.</creatorcontrib><creatorcontrib>Meals, Elizabeth A.</creatorcontrib><creatorcontrib>Yi, Taolin</creatorcontrib><creatorcontrib>Knapp, Katherine M.</creatorcontrib><creatorcontrib>English, B. Keith</creatorcontrib><title>SHP-1 inhibits LPS-mediated TNF and iNOS production in murine macrophages</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Several lines of evidence have suggested that protein tyrosine phosphatases, including CD45 and SHP-1, regulate macrophage activation. Macrophages from mice lacking SHP-1 (motheaten mice) are hyper-responsive to many stimuli, suggesting that SHP-1 may negatively regulate macrophage activation. Herein we report that the repressible/inducible over-expression of wild-type SHP-1 in a subclone of RAW 264.7 macrophages (RAW-TT10 cells) inhibited both TNF secretion and iNOS protein accumulation in response to stimulation with lipopolysaccharide (LPS) and recombinant murine interferon-gamma and led to diminished LPS-mediated tyrosine phosphorylation of
vav1. In contrast, expression of a truncated SHP-1 construct previously shown to interfere with endogenous SHP-1 function modestly augmented LPS-mediated TNF and iNOS production and did not inhibit
vav1 tyrosine phosphorylation. Taken together, these data provide the first direct evidence that SHP-1 inhibits macrophage activation by LPS and suggest that this effect may be mediated in part by dephosphorylation of
vav1.</description><subject>Animals</subject><subject>Cell Line</subject><subject>Cells, Cultured</subject><subject>Clone Cells</subject><subject>Cytokine</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>iNOS</subject><subject>Interferon-gamma - pharmacology</subject><subject>Intracellular Signaling Peptides and Proteins - physiology</subject><subject>Kinase</subject><subject>Lipopolysaccharides - pharmacology</subject><subject>Macrophage</subject><subject>Macrophage Activation - immunology</subject><subject>Macrophages - enzymology</subject><subject>Macrophages - immunology</subject><subject>Mice</subject><subject>Nitric Oxide Synthase Type II - antagonists & inhibitors</subject><subject>Nitric Oxide Synthase Type II - biosynthesis</subject><subject>Phosphatase</subject><subject>Phosphorylation</subject><subject>Protein Tyrosine Phosphatase, Non-Receptor Type 6</subject><subject>Protein Tyrosine Phosphatases - physiology</subject><subject>Proto-Oncogene Proteins c-vav - antagonists & inhibitors</subject><subject>Proto-Oncogene Proteins c-vav - metabolism</subject><subject>Recombinant Proteins</subject><subject>SHP-1</subject><subject>Signal transduction</subject><subject>Tetracycline - pharmacology</subject><subject>TNF</subject><subject>Transfection</subject><subject>Tumor Necrosis Factor-alpha - antagonists & inhibitors</subject><subject>Tumor Necrosis Factor-alpha - biosynthesis</subject><subject>Tyrosine</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkMFqGzEQhkVpqN0kL9BD2VNvu5nRytoV9FJM0hhMEnACuQmtNFvLeHddabfQt6-MDb0lpznM9__MfIx9QSgQUN7siqYJtuAAsgBeACw-sDmCgpwjiI9sDmmTc4WvM_Y5xh0AopDqE5uhFHWlSj5nq839U46Z77e-8WPM1k-bvCPnzUgue364y0zvMv_wuMkOYXCTHf3QJzrrpuB7yjpjw3DYml8Ur9hFa_aRrs_zkr3c3T4v7_P148_V8sc6t2W9GHPVtgpoYaTgpQMulGqEqUUjlJUKWmqq2i3QApBR1lV1OpkTmrLkiE1rXHnJvp1600G_J4qj7ny0tN-bnoYpallJJSTW74JYIUheqwTyE5h-iTFQqw_Bdyb81Qj6aFrv9NG0PprWwHUynUJfz-1Tk4T9j5zVJuD7CaAk44-noKP11NskN5AdtRv8W_3_AP_wjT4</recordid><startdate>20060407</startdate><enddate>20060407</enddate><creator>Hardin, Amy O.</creator><creator>Meals, Elizabeth A.</creator><creator>Yi, Taolin</creator><creator>Knapp, Katherine M.</creator><creator>English, B. Keith</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>7T5</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>20060407</creationdate><title>SHP-1 inhibits LPS-mediated TNF and iNOS production in murine macrophages</title><author>Hardin, Amy O. ; Meals, Elizabeth A. ; Yi, Taolin ; Knapp, Katherine M. ; English, B. Keith</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c385t-9ff90e5a6423d02499b4a84b49c690feb78d51c00ea9cd781142e1a33211bfad3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Animals</topic><topic>Cell Line</topic><topic>Cells, Cultured</topic><topic>Clone Cells</topic><topic>Cytokine</topic><topic>Enzyme Inhibitors - pharmacology</topic><topic>iNOS</topic><topic>Interferon-gamma - pharmacology</topic><topic>Intracellular Signaling Peptides and Proteins - physiology</topic><topic>Kinase</topic><topic>Lipopolysaccharides - pharmacology</topic><topic>Macrophage</topic><topic>Macrophage Activation - immunology</topic><topic>Macrophages - enzymology</topic><topic>Macrophages - immunology</topic><topic>Mice</topic><topic>Nitric Oxide Synthase Type II - antagonists & inhibitors</topic><topic>Nitric Oxide Synthase Type II - biosynthesis</topic><topic>Phosphatase</topic><topic>Phosphorylation</topic><topic>Protein Tyrosine Phosphatase, Non-Receptor Type 6</topic><topic>Protein Tyrosine Phosphatases - physiology</topic><topic>Proto-Oncogene Proteins c-vav - antagonists & inhibitors</topic><topic>Proto-Oncogene Proteins c-vav - metabolism</topic><topic>Recombinant Proteins</topic><topic>SHP-1</topic><topic>Signal transduction</topic><topic>Tetracycline - pharmacology</topic><topic>TNF</topic><topic>Transfection</topic><topic>Tumor Necrosis Factor-alpha - antagonists & inhibitors</topic><topic>Tumor Necrosis Factor-alpha - biosynthesis</topic><topic>Tyrosine</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hardin, Amy O.</creatorcontrib><creatorcontrib>Meals, Elizabeth A.</creatorcontrib><creatorcontrib>Yi, Taolin</creatorcontrib><creatorcontrib>Knapp, Katherine M.</creatorcontrib><creatorcontrib>English, B. Keith</creatorcontrib><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>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hardin, Amy O.</au><au>Meals, Elizabeth A.</au><au>Yi, Taolin</au><au>Knapp, Katherine M.</au><au>English, B. Keith</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>SHP-1 inhibits LPS-mediated TNF and iNOS production in murine macrophages</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2006-04-07</date><risdate>2006</risdate><volume>342</volume><issue>2</issue><spage>547</spage><epage>555</epage><pages>547-555</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Several lines of evidence have suggested that protein tyrosine phosphatases, including CD45 and SHP-1, regulate macrophage activation. Macrophages from mice lacking SHP-1 (motheaten mice) are hyper-responsive to many stimuli, suggesting that SHP-1 may negatively regulate macrophage activation. Herein we report that the repressible/inducible over-expression of wild-type SHP-1 in a subclone of RAW 264.7 macrophages (RAW-TT10 cells) inhibited both TNF secretion and iNOS protein accumulation in response to stimulation with lipopolysaccharide (LPS) and recombinant murine interferon-gamma and led to diminished LPS-mediated tyrosine phosphorylation of
vav1. In contrast, expression of a truncated SHP-1 construct previously shown to interfere with endogenous SHP-1 function modestly augmented LPS-mediated TNF and iNOS production and did not inhibit
vav1 tyrosine phosphorylation. Taken together, these data provide the first direct evidence that SHP-1 inhibits macrophage activation by LPS and suggest that this effect may be mediated in part by dephosphorylation of
vav1.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>16487932</pmid><doi>10.1016/j.bbrc.2006.02.005</doi><tpages>9</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0006-291X |
| ispartof | Biochemical and biophysical research communications, 2006-04, Vol.342 (2), p.547-555 |
| issn | 0006-291X 1090-2104 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_67694618 |
| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Animals Cell Line Cells, Cultured Clone Cells Cytokine Enzyme Inhibitors - pharmacology iNOS Interferon-gamma - pharmacology Intracellular Signaling Peptides and Proteins - physiology Kinase Lipopolysaccharides - pharmacology Macrophage Macrophage Activation - immunology Macrophages - enzymology Macrophages - immunology Mice Nitric Oxide Synthase Type II - antagonists & inhibitors Nitric Oxide Synthase Type II - biosynthesis Phosphatase Phosphorylation Protein Tyrosine Phosphatase, Non-Receptor Type 6 Protein Tyrosine Phosphatases - physiology Proto-Oncogene Proteins c-vav - antagonists & inhibitors Proto-Oncogene Proteins c-vav - metabolism Recombinant Proteins SHP-1 Signal transduction Tetracycline - pharmacology TNF Transfection Tumor Necrosis Factor-alpha - antagonists & inhibitors Tumor Necrosis Factor-alpha - biosynthesis Tyrosine |
| title | SHP-1 inhibits LPS-mediated TNF and iNOS production in murine macrophages |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-17T07%3A59%3A03IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=SHP-1%20inhibits%20LPS-mediated%20TNF%20and%20iNOS%20production%20in%20murine%20macrophages&rft.jtitle=Biochemical%20and%20biophysical%20research%20communications&rft.au=Hardin,%20Amy%20O.&rft.date=2006-04-07&rft.volume=342&rft.issue=2&rft.spage=547&rft.epage=555&rft.pages=547-555&rft.issn=0006-291X&rft.eissn=1090-2104&rft_id=info:doi/10.1016/j.bbrc.2006.02.005&rft_dat=%3Cproquest_cross%3E17106289%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=17106289&rft_id=info:pmid/16487932&rft_els_id=S0006291X06002889&rfr_iscdi=true |