| Resistance of B16 melanoma cells to CD47-induced negative regulation of motility as a result of aberrant N-glycosylation of SHPS-1. | |
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MedLine Citation:
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PMID: 14739297 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The adhesion receptor SHPS-1 activates the protein-tyrosine-phosphatase SHP-2 and thereby promotes integrin-mediated reorganization of the cytoskeleton. SHPS-1 also contributes to cell-cell communication through association with CD47. Although functional alteration of SHPS-1 is implicated in cellular transformation, the role of the CD47-SHPS-1 interaction in carcinogenesis has been unclear. A soluble SHPS-1 ligand (CD47-Fc) has now been shown to bind to Melan-a non-tumorigenic melanocytes but not to syngeneic B16F10 melanoma cells. Treatment of B16F10 cells with 1-deoxymannojirimycin, which prevents N-glycan processing, restored the ability of SHPS-1 derived from these cells to bind CD47-Fc in vitro, indicating that aberrant N-glycosylation of SHPS-1 impairs CD47 binding in B16F10 cells. CD47-Fc inhibited the migration of Melan-a cells but not that of B16F10 cells. However, a monoclonal antibody that reacts with SHPS-1 on both Melan-a and B16F10 cells inhibited the migration of both cell types similarly. CD47 binding induced proteasome-mediated degradation of SHPS-1 in a tyrosine phosphorylation-independent manner. Furthermore, overexpression of SHPS-1 reduced the level of tyrosine phosphorylation of focal adhesion kinase, and this effect was reversed by CD47 binding. These results suggest that CD47 binds to and thereby down-regulates SHPS-1 on adjacent cells, resulting in inhibition of cell motility. Resistance to this inhibitory mechanism may contribute to the highly metastatic potential of B16 melanoma. |
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Authors:
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Takeshi Ogura; Tetsuya Noguchi; Reiko Murai-Takebe; Tetsuya Hosooka; Nakayuki Honma; Masato Kasuga |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2004-01-21 |
Journal Detail:
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Title: The Journal of biological chemistry Volume: 279 ISSN: 0021-9258 ISO Abbreviation: J. Biol. Chem. Publication Date: 2004 Apr |
Date Detail:
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Created Date: 2004-03-29 Completed Date: 2004-05-11 Revised Date: 2009-11-19 |
Medline Journal Info:
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Nlm Unique ID: 2985121R Medline TA: J Biol Chem Country: United States |
Other Details:
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Languages: eng Pagination: 13711-20 Citation Subset: IM |
Affiliation:
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Department of Clinical Molecular Medicine, Kobe University Graduate School of Medicine, 7-5-1 Kusunoki-cho, Chuo-ku, Kobe 650-0017, Japan. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Animals Antigens, CD / genetics, metabolism* Antigens, CD47 Antigens, Differentiation* Carrier Proteins / genetics, metabolism* Cell Communication / physiology Cell Line, Tumor Cell Movement / physiology* Cysteine Endopeptidases / metabolism Down-Regulation / physiology Focal Adhesion Kinase 1 Focal Adhesion Protein-Tyrosine Kinases Glycosylation Ligands Macrophages / cytology, metabolism Melanocytes / cytology, metabolism Melanoma, Experimental* Membrane Glycoproteins / metabolism* Mice Multienzyme Complexes / metabolism Neural Cell Adhesion Molecule L1 / metabolism* Phosphorylation Proteasome Endopeptidase Complex Protein-Tyrosine Kinases / metabolism Receptors, Immunologic / metabolism* Skin Neoplasms* Solubility Tyrosine / metabolism |
| Chemical | |
Reg. No./Substance:
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0/Antigens, CD; 0/Antigens, CD47; 0/Antigens, Differentiation; 0/Carrier Proteins; 0/Cd47 protein, mouse; 0/Ligands; 0/Membrane Glycoproteins; 0/Multienzyme Complexes; 0/Neural Cell Adhesion Molecule L1; 0/Ptpns1 protein, mouse; 0/Receptors, Immunologic; 55520-40-6/Tyrosine; EC 2.7.1.112/Ptk2 protein, mouse; EC 2.7.10.1/Focal Adhesion Kinase 1; EC 2.7.10.1/Protein-Tyrosine Kinases; EC 2.7.10.2/Focal Adhesion Protein-Tyrosine Kinases; EC 3.4.22.-/Cysteine Endopeptidases; EC 3.4.25.1/Proteasome Endopeptidase Complex |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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