Title: The gp200-MR6 molecule which is functionally associated with the IL-4 receptor modulates B cell phenotype and is a novel member of the human macrophage mannose receptor family
Abstract: European Journal of ImmunologyVolume 28, Issue 12 p. 4071-4083 ArticleFree Access The gp200-MR6 molecule which is functionally associated with the IL-4 receptor modulates B cell phenotype and is a novel member of the human macrophage mannose receptor family Paul F. McKay, Paul F. McKay Department of Immunology Imperial College School of Medicine, Hammersmith Hospital, London, GBSearch for more papers by this authorNesrina Imami, Nesrina Imami Department of Immunology Imperial College School of Medicine, Hammersmith Hospital, London, GBSearch for more papers by this authorMichael Johns, Michael Johns Department of Immunology Imperial College School of Medicine, Hammersmith Hospital, London, GBSearch for more papers by this authorDavid A. Taylor-Fishwick, David A. Taylor-Fishwick Kennedy Institute of Rheumatology, London, GBSearch for more papers by this authorLucas M. Sedibane, Lucas M. Sedibane Department of Immunology Imperial College School of Medicine, Hammersmith Hospital, London, GBSearch for more papers by this authorNicholas F. Totty, Nicholas F. Totty Ludwig Institute for Cancer Research, London, GBSearch for more papers by this authorJ. Justin Hsuan, J. Justin Hsuan Ludwig Institute for Cancer Research, London, GB Department of Biochemistry, University College London, London, GBSearch for more papers by this authorDonald B. Palmer, Donald B. Palmer Department of Immunology Imperial College School of Medicine, Hammersmith Hospital, London, GBSearch for more papers by this authorAndrew J. T. George, Andrew J. T. George Department of Immunology Imperial College School of Medicine, Hammersmith Hospital, London, GBSearch for more papers by this authorBrian M. J. Foxwell, Brian M. J. Foxwell Kennedy Institute of Rheumatology, London, GBSearch for more papers by this authorMary A. Ritter, Mary A. Ritter Department of Immunology Imperial College School of Medicine, Hammersmith Hospital, London, GBSearch for more papers by this author Paul F. McKay, Paul F. McKay Department of Immunology Imperial College School of Medicine, Hammersmith Hospital, London, GBSearch for more papers by this authorNesrina Imami, Nesrina Imami Department of Immunology Imperial College School of Medicine, Hammersmith Hospital, London, GBSearch for more papers by this authorMichael Johns, Michael Johns Department of Immunology Imperial College School of Medicine, Hammersmith Hospital, London, GBSearch for more papers by this authorDavid A. Taylor-Fishwick, David A. Taylor-Fishwick Kennedy Institute of Rheumatology, London, GBSearch for more papers by this authorLucas M. Sedibane, Lucas M. Sedibane Department of Immunology Imperial College School of Medicine, Hammersmith Hospital, London, GBSearch for more papers by this authorNicholas F. Totty, Nicholas F. Totty Ludwig Institute for Cancer Research, London, GBSearch for more papers by this authorJ. Justin Hsuan, J. Justin Hsuan Ludwig Institute for Cancer Research, London, GB Department of Biochemistry, University College London, London, GBSearch for more papers by this authorDonald B. Palmer, Donald B. Palmer Department of Immunology Imperial College School of Medicine, Hammersmith Hospital, London, GBSearch for more papers by this authorAndrew J. T. George, Andrew J. T. George Department of Immunology Imperial College School of Medicine, Hammersmith Hospital, London, GBSearch for more papers by this authorBrian M. J. Foxwell, Brian M. J. Foxwell Kennedy Institute of Rheumatology, London, GBSearch for more papers by this authorMary A. Ritter, Mary A. Ritter Department of Immunology Imperial College School of Medicine, Hammersmith Hospital, London, GBSearch for more papers by this author First published: 14 December 1998 https://doi.org/10.1002/(SICI)1521-4141(199812)28:12<4071::AID-IMMU4071>3.0.CO;2-OCitations: 26AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinked InRedditWechat Abstract The human gp200-MR6 molecule has previously been shown to have either an antagonistic or agonistic effect on IL-4 function, demonstrated by inhibition of IL-4-induced proliferation of T cells or mimicking of IL-4-induced maturation of epithelium, respectively. We now show that gp200-MR6 ligation can also mimic IL-4 and have an anti-proliferative pro-maturational influence within the immune system, causing up-regulation of co-stimulatory molecules on B lymphocytes. Biochemical analysis and cDNA cloning reveal that gp200-MR6 belongs to the human macrophage mannose receptor family of multidomain molecules. It comprises 1722 amino acids in toto (mature protein, 1695 amino acids; signal sequence, 27 amino acids) organized into 12 external domains (an N-terminal cysteine-rich domain, a fibronectin type II domain and 10 C-type carbohydrate recognition domains), a transmembrane region and a small cytoplasmic C terminus (31 amino acids) containing a single tyrosine residue (Y1679), but no obvious kinase domain. Strong amino acid sequence identity (77 %) suggests that gp200-MR6 is the human homologue of the murine DEC-205, indicating that this molecule has much wider functional activity than its classical endocytic role. We also show that the gp200-MR6 molecule is closely associated with tyrosine kinase activity; the link between gp200-MR6 and the IL-4 receptor may therefore be via intracellular signaling pathways, with multifunctionality residing in its extracellular multidomain structure. Citing Literature Volume28, Issue12December 1998Pages 4071-4083 ReferencesRelatedInformation
Publication Year: 1998
Publication Date: 1998-12-01
Language: en
Type: article
Indexed In: ['crossref', 'pubmed']
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Cited By Count: 33
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