| SHPS-1 and a synthetic peptide representing its ITIM inhibit the MyD88, but not TRIF, pathway of TLR signaling through activation of SHP and PI3K in THP-1 cells. | |
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MedLine Citation:
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PMID: 23314616 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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BACKGROUND: Src homology 2 domain-containing protein tyrosine phosphatase substrate (SHPS)-1 is known to have regulatory effects on myeloid cells. However, its role in macrophage activation is not clearly understood. METHODS AND RESULTS: In order to investigate the role of SHPS-1 in Toll-like receptor (TLR)-mediated activation, human monocytic cell lines were treated with anti-SHPS-1 monoclonal antibody. The triggering of SHPS-1 blocked the expression of IL-8 and TNF-α in cells treated with a TLR4 ligand that induces a signaling pathway involving myeloid differentiation factor 88 (MyD88) and Toll-interleukin-1 receptor (TIR)-domain-containing adapter-inducing interferon-β (TRIF). Interestingly, SHPS-1 inhibited TLR9/MyD88-mediated, but not TLR3/TRIF-mediated, expression of IL-8. Accordingly, a synthetic peptide representing the immunoreceptor tyrosine-based inhibition motif (ITIM) of SHPS-1 suppressed only the MyD88 pathway. Utilization of specific inhibitors and Western blot analysis indicated that the inhibitory effects were mediated by Src homology 2 domain-containing phosphatases (SHPs) and phosphoinositide 3-kinase (PI3K). CONCLUSION: SHPS-1 negatively regulates the MyD88-dependent TLR signaling pathway through the inhibition of NF-κB activation. |
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Authors:
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Eun-Ju Kim; Kyoungho Suk; Won-Ha Lee |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2013-1-12 |
Journal Detail:
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Title: Inflammation research : official journal of the European Histamine Research Society ... [et al.] Volume: - ISSN: 1420-908X ISO Abbreviation: Inflamm. Res. Publication Date: 2013 Jan |
Date Detail:
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Created Date: 2013-1-14 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 9508160 Medline TA: Inflamm Res Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Affiliation:
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School of Life Sciences and Biotechnology, Kyungpook National University, Daegu, 702-701, Korea. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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