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- Hirofumi Chiba
- <!--label omitted: 1-->Department of Biochemistry,1
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- Hitomi Sano
- <!--label omitted: 1-->Department of Biochemistry,1
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- Daisuke Iwaki
- <!--label omitted: 1-->Department of Biochemistry,1
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- Seiji Murakami
- <!--label omitted: 1-->Department of Biochemistry,1
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- Hiroaki Mitsuzawa
- <!--label omitted: 1-->Department of Biochemistry,1
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- Toru Takahashi
- <!--label omitted: 1-->Department of Biochemistry,1
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- Masanori Konishi
- <!--label omitted: 1-->Department of Biochemistry,1
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- Hiroki Takahashi
- <!--label omitted: 2-->Third Department of Internal Medicine,2 and
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- Yoshio Kuroki
- <!--label omitted: 1-->Department of Biochemistry,1
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- R. N. Moore
- editor
抄録
<jats:title>ABSTRACT</jats:title><jats:p>Lipopolysaccharide (LPS) has been known to induce inflammation by interacting with CD14, which serves as a receptor for LPS. Mannose-binding protein (MBP) belongs to the collectin subgroup of the C-type lectin superfamily, along with surfactant proteins SP-A and SP-D. We have recently demonstrated that SP-A modulates LPS-induced cellular responses by interaction with CD14 (H. Sano, H. Sohma, T. Muta, S. Nomura, D. R. Voelker, and Y. Kuroki, J. Immunol. 163:387–395, 2000) and that SP-D also interacts with CD14 (H. Sano, H. Chiba, D. Iwaki, H. Sohma, D. R. Voelker, and Y. Kuroki, J. Biol. Chem. 275:22442–22451, 2000). In this study, we examined whether MBP, a collectin highly homologous to SP-A and SP-D, could bind CD14. Recombinant rat MBP-A bound recombinant human soluble CD14 in a concentration-dependent manner. Its binding was not inhibited in the presence of excess mannose or EDTA. MBP-A bound deglycosylated CD14 treated with<jats:italic>N</jats:italic>-glycosidase F, neuraminidase, and<jats:italic>O</jats:italic>-glycosidase, indicating that MBP-A interacts with the peptide portion of CD14. Since LPS was also a ligand for the collectins, we compared the characteristics of binding of MBP-A to LPS with those of binding to CD14. MBP-A bound to lipid A from<jats:italic>Salmonella enterica</jats:italic>serovar Minnesota and rough LPS (<jats:italic>S. enterica</jats:italic>serovar Minnesota Re595 and<jats:italic>Escherichia coli</jats:italic>J5, Rc), but not to smooth LPS (<jats:italic>E. coli</jats:italic>O26:B6 and O111:B4). Unlike CD14 binding, EDTA and excess mannose attenuated the binding of MBP-A to rough LPS. From these results, we conclude that CD14 is a novel ligand for MBP-A and that MBP-A utilizes a different mechanism for CD14 recognition from that for LPS.</jats:p>
収録刊行物
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- Infection and Immunity
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Infection and Immunity 69 (3), 1587-1592, 2001-03
American Society for Microbiology
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詳細情報 詳細情報について
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- CRID
- 1360011146601766656
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- NII論文ID
- 30020829152
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- ISSN
- 10985522
- 00199567
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- データソース種別
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