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Molecular Cloning and Characterization of a Novel CXC Chemokine Macrophage Inflammatory Protein-2γ Chemoattractant for Human Neutrophils and Dendritic Cells
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| Zeitschriftentitel: | The Journal of Immunology |
|---|---|
| Personen und Körperschaften: | , , , , , , , , |
| In: | The Journal of Immunology, 165, 2000, 5, S. 2588-2595 |
| Medientyp: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
The American Association of Immunologists
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| Schlagwörter: |
| author_facet |
Cao, Xuetao Zhang, Weiping Wan, Tao He, Long Chen, Taoyong Yuan, Zhenglong Ma, Shihua Yu, Yizhi Chen, Guoyou Cao, Xuetao Zhang, Weiping Wan, Tao He, Long Chen, Taoyong Yuan, Zhenglong Ma, Shihua Yu, Yizhi Chen, Guoyou |
|---|---|
| author |
Cao, Xuetao Zhang, Weiping Wan, Tao He, Long Chen, Taoyong Yuan, Zhenglong Ma, Shihua Yu, Yizhi Chen, Guoyou |
| spellingShingle |
Cao, Xuetao Zhang, Weiping Wan, Tao He, Long Chen, Taoyong Yuan, Zhenglong Ma, Shihua Yu, Yizhi Chen, Guoyou The Journal of Immunology Molecular Cloning and Characterization of a Novel CXC Chemokine Macrophage Inflammatory Protein-2γ Chemoattractant for Human Neutrophils and Dendritic Cells Immunology Immunology and Allergy |
| author_sort |
cao, xuetao |
| spelling |
Cao, Xuetao Zhang, Weiping Wan, Tao He, Long Chen, Taoyong Yuan, Zhenglong Ma, Shihua Yu, Yizhi Chen, Guoyou 0022-1767 1550-6606 The American Association of Immunologists Immunology Immunology and Allergy http://dx.doi.org/10.4049/jimmunol.165.5.2588 <jats:title>Abstract</jats:title><jats:p>Chemokines play important roles in leukocyte trafficking as well as function regulation. In this study, we described the identification and characterization of a novel CXC chemokine from a human dendritic cell (DC) cDNA library, the full-length cDNA of which contains an open reading frame encoding 111 aa with a putative signal peptide of 34 aa. This CXC chemokine shares greatest homology with macrophage inflammatory protein (MIP)-2αβ, hence is designated as MIP-2γ. Mouse MIP-2γ was identified by electrocloning and is highly homologous to human MIP-2γ. Northern blotting revealed that MIP-2γ was constitutively and widely expressed in most normal tissues with the greatest expression in kidney, but undetectable in most tumor cell lines except THP-1 cells. In situ hybridization analysis demonstrated that MIP-2γ was mainly expressed by the epithelium of tubules in the kidney and hepatocytes in the liver. Although no detectable expression was observed in freshly isolated or PMA-treated monocytes, RT-PCR analysis revealed MIP-2γ expression by monocyte-derived DC. Recombinant MIP-2γ from 293 cells is about 9.5 kDa in size and specifically detectable by its polyclonal Ab developed by the immunization with its 6His-tagged fusion protein. The eukaryotically expressed MIP-2γ is a potent chemoattractant for neutrophils, and weaker for DC, but inactive to monocytes, NK cells, and T and B lymphocytes. Receptor binding assays showed that MIP-2γ does not bind to CXCR2. This implies that DC might contribute to the innate immunity through the production of neutrophil-attracting chemokines and extends the knowledge about the regulation of DC migration.</jats:p> Molecular Cloning and Characterization of a Novel CXC Chemokine Macrophage Inflammatory Protein-2γ Chemoattractant for Human Neutrophils and Dendritic Cells The Journal of Immunology |
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| title |
Molecular Cloning and Characterization of a Novel CXC Chemokine Macrophage Inflammatory Protein-2γ Chemoattractant for Human Neutrophils and Dendritic Cells |
| title_unstemmed |
Molecular Cloning and Characterization of a Novel CXC Chemokine Macrophage Inflammatory Protein-2γ Chemoattractant for Human Neutrophils and Dendritic Cells |
| title_full |
Molecular Cloning and Characterization of a Novel CXC Chemokine Macrophage Inflammatory Protein-2γ Chemoattractant for Human Neutrophils and Dendritic Cells |
| title_fullStr |
Molecular Cloning and Characterization of a Novel CXC Chemokine Macrophage Inflammatory Protein-2γ Chemoattractant for Human Neutrophils and Dendritic Cells |
| title_full_unstemmed |
Molecular Cloning and Characterization of a Novel CXC Chemokine Macrophage Inflammatory Protein-2γ Chemoattractant for Human Neutrophils and Dendritic Cells |
| title_short |
Molecular Cloning and Characterization of a Novel CXC Chemokine Macrophage Inflammatory Protein-2γ Chemoattractant for Human Neutrophils and Dendritic Cells |
| title_sort |
molecular cloning and characterization of a novel cxc chemokine macrophage inflammatory protein-2γ chemoattractant for human neutrophils and dendritic cells |
| topic |
Immunology Immunology and Allergy |
| url |
http://dx.doi.org/10.4049/jimmunol.165.5.2588 |
| publishDate |
2000 |
| physical |
2588-2595 |
| description |
<jats:title>Abstract</jats:title><jats:p>Chemokines play important roles in leukocyte trafficking as well as function regulation. In this study, we described the identification and characterization of a novel CXC chemokine from a human dendritic cell (DC) cDNA library, the full-length cDNA of which contains an open reading frame encoding 111 aa with a putative signal peptide of 34 aa. This CXC chemokine shares greatest homology with macrophage inflammatory protein (MIP)-2αβ, hence is designated as MIP-2γ. Mouse MIP-2γ was identified by electrocloning and is highly homologous to human MIP-2γ. Northern blotting revealed that MIP-2γ was constitutively and widely expressed in most normal tissues with the greatest expression in kidney, but undetectable in most tumor cell lines except THP-1 cells. In situ hybridization analysis demonstrated that MIP-2γ was mainly expressed by the epithelium of tubules in the kidney and hepatocytes in the liver. Although no detectable expression was observed in freshly isolated or PMA-treated monocytes, RT-PCR analysis revealed MIP-2γ expression by monocyte-derived DC. Recombinant MIP-2γ from 293 cells is about 9.5 kDa in size and specifically detectable by its polyclonal Ab developed by the immunization with its 6His-tagged fusion protein. The eukaryotically expressed MIP-2γ is a potent chemoattractant for neutrophils, and weaker for DC, but inactive to monocytes, NK cells, and T and B lymphocytes. Receptor binding assays showed that MIP-2γ does not bind to CXCR2. This implies that DC might contribute to the innate immunity through the production of neutrophil-attracting chemokines and extends the knowledge about the regulation of DC migration.</jats:p> |
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| author | Cao, Xuetao, Zhang, Weiping, Wan, Tao, He, Long, Chen, Taoyong, Yuan, Zhenglong, Ma, Shihua, Yu, Yizhi, Chen, Guoyou |
| author_facet | Cao, Xuetao, Zhang, Weiping, Wan, Tao, He, Long, Chen, Taoyong, Yuan, Zhenglong, Ma, Shihua, Yu, Yizhi, Chen, Guoyou, Cao, Xuetao, Zhang, Weiping, Wan, Tao, He, Long, Chen, Taoyong, Yuan, Zhenglong, Ma, Shihua, Yu, Yizhi, Chen, Guoyou |
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| description | <jats:title>Abstract</jats:title><jats:p>Chemokines play important roles in leukocyte trafficking as well as function regulation. In this study, we described the identification and characterization of a novel CXC chemokine from a human dendritic cell (DC) cDNA library, the full-length cDNA of which contains an open reading frame encoding 111 aa with a putative signal peptide of 34 aa. This CXC chemokine shares greatest homology with macrophage inflammatory protein (MIP)-2αβ, hence is designated as MIP-2γ. Mouse MIP-2γ was identified by electrocloning and is highly homologous to human MIP-2γ. Northern blotting revealed that MIP-2γ was constitutively and widely expressed in most normal tissues with the greatest expression in kidney, but undetectable in most tumor cell lines except THP-1 cells. In situ hybridization analysis demonstrated that MIP-2γ was mainly expressed by the epithelium of tubules in the kidney and hepatocytes in the liver. Although no detectable expression was observed in freshly isolated or PMA-treated monocytes, RT-PCR analysis revealed MIP-2γ expression by monocyte-derived DC. Recombinant MIP-2γ from 293 cells is about 9.5 kDa in size and specifically detectable by its polyclonal Ab developed by the immunization with its 6His-tagged fusion protein. The eukaryotically expressed MIP-2γ is a potent chemoattractant for neutrophils, and weaker for DC, but inactive to monocytes, NK cells, and T and B lymphocytes. Receptor binding assays showed that MIP-2γ does not bind to CXCR2. This implies that DC might contribute to the innate immunity through the production of neutrophil-attracting chemokines and extends the knowledge about the regulation of DC migration.</jats:p> |
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| imprint | The American Association of Immunologists, 2000 |
| imprint_str_mv | The American Association of Immunologists, 2000 |
| institution | DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1, DE-L229 |
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| spelling | Cao, Xuetao Zhang, Weiping Wan, Tao He, Long Chen, Taoyong Yuan, Zhenglong Ma, Shihua Yu, Yizhi Chen, Guoyou 0022-1767 1550-6606 The American Association of Immunologists Immunology Immunology and Allergy http://dx.doi.org/10.4049/jimmunol.165.5.2588 <jats:title>Abstract</jats:title><jats:p>Chemokines play important roles in leukocyte trafficking as well as function regulation. In this study, we described the identification and characterization of a novel CXC chemokine from a human dendritic cell (DC) cDNA library, the full-length cDNA of which contains an open reading frame encoding 111 aa with a putative signal peptide of 34 aa. This CXC chemokine shares greatest homology with macrophage inflammatory protein (MIP)-2αβ, hence is designated as MIP-2γ. Mouse MIP-2γ was identified by electrocloning and is highly homologous to human MIP-2γ. Northern blotting revealed that MIP-2γ was constitutively and widely expressed in most normal tissues with the greatest expression in kidney, but undetectable in most tumor cell lines except THP-1 cells. In situ hybridization analysis demonstrated that MIP-2γ was mainly expressed by the epithelium of tubules in the kidney and hepatocytes in the liver. Although no detectable expression was observed in freshly isolated or PMA-treated monocytes, RT-PCR analysis revealed MIP-2γ expression by monocyte-derived DC. Recombinant MIP-2γ from 293 cells is about 9.5 kDa in size and specifically detectable by its polyclonal Ab developed by the immunization with its 6His-tagged fusion protein. The eukaryotically expressed MIP-2γ is a potent chemoattractant for neutrophils, and weaker for DC, but inactive to monocytes, NK cells, and T and B lymphocytes. Receptor binding assays showed that MIP-2γ does not bind to CXCR2. This implies that DC might contribute to the innate immunity through the production of neutrophil-attracting chemokines and extends the knowledge about the regulation of DC migration.</jats:p> Molecular Cloning and Characterization of a Novel CXC Chemokine Macrophage Inflammatory Protein-2γ Chemoattractant for Human Neutrophils and Dendritic Cells The Journal of Immunology |
| spellingShingle | Cao, Xuetao, Zhang, Weiping, Wan, Tao, He, Long, Chen, Taoyong, Yuan, Zhenglong, Ma, Shihua, Yu, Yizhi, Chen, Guoyou, The Journal of Immunology, Molecular Cloning and Characterization of a Novel CXC Chemokine Macrophage Inflammatory Protein-2γ Chemoattractant for Human Neutrophils and Dendritic Cells, Immunology, Immunology and Allergy |
| title | Molecular Cloning and Characterization of a Novel CXC Chemokine Macrophage Inflammatory Protein-2γ Chemoattractant for Human Neutrophils and Dendritic Cells |
| title_full | Molecular Cloning and Characterization of a Novel CXC Chemokine Macrophage Inflammatory Protein-2γ Chemoattractant for Human Neutrophils and Dendritic Cells |
| title_fullStr | Molecular Cloning and Characterization of a Novel CXC Chemokine Macrophage Inflammatory Protein-2γ Chemoattractant for Human Neutrophils and Dendritic Cells |
| title_full_unstemmed | Molecular Cloning and Characterization of a Novel CXC Chemokine Macrophage Inflammatory Protein-2γ Chemoattractant for Human Neutrophils and Dendritic Cells |
| title_short | Molecular Cloning and Characterization of a Novel CXC Chemokine Macrophage Inflammatory Protein-2γ Chemoattractant for Human Neutrophils and Dendritic Cells |
| title_sort | molecular cloning and characterization of a novel cxc chemokine macrophage inflammatory protein-2γ chemoattractant for human neutrophils and dendritic cells |
| title_unstemmed | Molecular Cloning and Characterization of a Novel CXC Chemokine Macrophage Inflammatory Protein-2γ Chemoattractant for Human Neutrophils and Dendritic Cells |
| topic | Immunology, Immunology and Allergy |
| url | http://dx.doi.org/10.4049/jimmunol.165.5.2588 |