|Functional modulation of human macrophages through CD46 (measles virus receptor): production of IL-12 p40 and nitric oxide in association with recruitment of protein-tyrosine phosphatase SHP-1 to CD46.|
|PMID: 11046046 Owner: NLM Status: MEDLINE|
|Human CD46, formerly membrane cofactor protein, binds and inactivates complement C3b and serves as a receptor for measles virus (MV), thereby protecting cells from homologous complement and sustaining systemic measles infection. Suppression of cell-mediated immunity, including down-regulation of IL-12 production, has been reported on macrophages (Mphi) by cross-linking their CD46. The intracellular events responsible for these immune responses, however, remain unknown. In this study, we found that 6- to 8-day GM-CSF-treated peripheral blood monocytes acquired the capacity to recruit protein-tyrosine phosphatase SHP-1 to their CD46 and concomitantly were able to produce IL-12 p40 and NO. These responses were induced by stimulation with mAbs F(ab')(2) against CD46 that block MV binding or by a wild-type MV strain Kohno MV strain (KO; UV treated or untreated) that was reported to induce early phase CD46 down-regulation. Direct ligation of CD46 by these reagents, but not intracellular MV replication, was required for these cellular responses. Interestingly, the KO strain failed to replicate in the 6- to 8-day GM-CSF-cultured Mphi, while other MV strains replicated to form syncytia under the same conditions. When stimulated with the KO strain, rapid and transient dissociation of SHP-1 from CD46 was observed. These and previous results provide strong evidence that CD46 serves as a signal modulatory molecule and that the properties of ligands determine suppression or activation of an innate immune system at a specific maturation stage of human Mphi.|
|M Kurita-Taniguchi; A Fukui; K Hazeki; A Hirano; S Tsuji; M Matsumoto; M Watanabe; S Ueda; T Seya|
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|Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't|
|Title: Journal of immunology (Baltimore, Md. : 1950) Volume: 165 ISSN: 0022-1767 ISO Abbreviation: J. Immunol. Publication Date: 2000 Nov|
|Created Date: 2000-11-03 Completed Date: 2000-11-30 Revised Date: 2007-11-15|
Medline Journal Info:
|Nlm Unique ID: 2985117R Medline TA: J Immunol Country: UNITED STATES|
|Languages: eng Pagination: 5143-52 Citation Subset: AIM; IM|
|Department of Immunology, Osaka Medical Center for Cancer and Cardiovascular Diseases, Higashinari-ku, Osaka, Japan.|
|APA/MLA Format Download EndNote Download BibTex|
Antibodies, Monoclonal / metabolism
Antigens, CD / immunology, metabolism, physiology*
Binding Sites, Antibody
Giant Cells / immunology, virology
Hemagglutinins, Viral / genetics, immunology
Interleukin-12 / biosynthesis*
Intracellular Signaling Peptides and Proteins
Macrophages / enzymology, immunology*, metabolism*, virology
Measles virus / immunology*, physiology
Membrane Glycoproteins / immunology, metabolism, physiology*
Nitric Oxide / biosynthesis*
Protein Tyrosine Phosphatase, Non-Receptor Type 11
Protein Tyrosine Phosphatase, Non-Receptor Type 6
Protein Tyrosine Phosphatases / metabolism*
Receptors, Virus / immunology*
SH2 Domain-Containing Protein Tyrosine Phosphatases
Virus Replication / immunology
src Homology Domains / immunology
|0/Antibodies, Monoclonal; 0/Antigens, CD; 0/Antigens, CD46; 0/Binding Sites, Antibody; 0/CD46 protein, human; 0/Hemagglutinins, Viral; 0/Intracellular Signaling Peptides and Proteins; 0/Mcp protein, mouse; 0/Membrane Glycoproteins; 0/Receptors, Virus; 0/hemagglutinin protein G, measles virus; 10102-43-9/Nitric Oxide; 187348-17-0/Interleukin-12; EC 18.104.22.168/PTPN11 protein, human; EC 22.214.171.124/PTPN6 protein, human; EC 126.96.36.199/Protein Tyrosine Phosphatase, Non-Receptor Type 11; EC 188.8.131.52/Protein Tyrosine Phosphatase, Non-Receptor Type 6; EC 184.108.40.206/Protein Tyrosine Phosphatases; EC 220.127.116.11/Ptpn11 protein, mouse; EC 18.104.22.168/Ptpn6 protein, mouse; EC 22.214.171.124/SH2 Domain-Containing Protein Tyrosine Phosphatases|
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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