CLEC4F Is an Inducible C-Type Lectin in F4/80-Positive Cells and Is Involved in Alpha-Galactosylceramide Presentation in Liver
CLEC4F, a member of C-type lectin, was first purified from rat liver extract with high binding affinity to fucose, galactose (Gal), N-acetylgalactosamine (GalNAc), and un-sialylated glucosphingolipids with GalNAc or Gal terminus. However, the biological functions of CLEC4F have not been elucidated....
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| Published in | PloS one Vol. 8; no. 6; p. e65070 |
|---|---|
| Main Authors | , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
Public Library of Science
06.06.2013
Public Library of Science (PLoS) |
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| Online Access | Get full text |
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| Abstract | CLEC4F, a member of C-type lectin, was first purified from rat liver extract with high binding affinity to fucose, galactose (Gal), N-acetylgalactosamine (GalNAc), and un-sialylated glucosphingolipids with GalNAc or Gal terminus. However, the biological functions of CLEC4F have not been elucidated. To address this question, we examined the expression and distribution of murine CLEC4F, determined its binding specificity by glycan array, and investigated its function using CLEC4F knockout (Clec4f-/-) mice. We found that CLEC4F is a heavily glycosylated membrane protein co-expressed with F4/80 on Kupffer cells. In contrast to F4/80, CLEC4F is detectable in fetal livers at embryonic day 11.5 (E11.5) but not in yolk sac, suggesting the expression of CLEC4F is induced as cells migrate from yolk cells to the liver. Even though CLEC4F is not detectable in tissues outside liver, both residential Kupffer cells and infiltrating mononuclear cells surrounding liver abscesses are CLEC4F-positive upon Listeria monocytogenes (L. monocytogenes) infection. While CLEC4F has strong binding to Gal and GalNAc, terminal fucosylation inhibits CLEC4F recognition to several glycans such as Fucosyl GM1, Globo H, Bb3∼4 and other fucosyl-glycans. Moreover, CLEC4F interacts with alpha-galactosylceramide (α-GalCer) in a calcium-dependent manner and participates in the presentation of α-GalCer to natural killer T (NKT) cells. This suggests that CLEC4F is a C-type lectin with diverse binding specificity expressed on residential Kupffer cells and infiltrating monocytes in the liver, and may play an important role to modulate glycolipids presentation on Kupffer cells. |
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| AbstractList | CLEC4F, a member of C-type lectin, was first purified from rat liver extract with high binding affinity to fucose, galactose (Gal), N-acetylgalactosamine (GalNAc), and un-sialylated glucosphingolipids with GalNAc or Gal terminus. However, the biological functions of CLEC4F have not been elucidated. To address this question, we examined the expression and distribution of murine CLEC4F, determined its binding specificity by glycan array, and investigated its function using CLEC4F knockout (Clec4f-/-) mice. We found that CLEC4F is a heavily glycosylated membrane protein co-expressed with F4/80 on Kupffer cells. In contrast to F4/80, CLEC4F is detectable in fetal livers at embryonic day 11.5 (E11.5) but not in yolk sac, suggesting the expression of CLEC4F is induced as cells migrate from yolk cells to the liver. Even though CLEC4F is not detectable in tissues outside liver, both residential Kupffer cells and infiltrating mononuclear cells surrounding liver abscesses are CLEC4F-positive upon Listeria monocytogenes (L. monocytogenes) infection. While CLEC4F has strong binding to Gal and GalNAc, terminal fucosylation inhibits CLEC4F recognition to several glycans such as Fucosyl GM1, Globo H, Bb3~4 and other fucosyl-glycans. Moreover, CLEC4F interacts with alpha-galactosylceramide ([alpha]-GalCer) in a calcium-dependent manner and participates in the presentation of [alpha]-GalCer to natural killer T (NKT) cells. This suggests that CLEC4F is a C-type lectin with diverse binding specificity expressed on residential Kupffer cells and infiltrating monocytes in the liver, and may play an important role to modulate glycolipids presentation on Kupffer cells. CLEC4F, a member of C-type lectin, was first purified from rat liver extract with high binding affinity to fucose, galactose (Gal), N-acetylgalactosamine (GalNAc), and un-sialylated glucosphingolipids with GalNAc or Gal terminus. However, the biological functions of CLEC4F have not been elucidated. To address this question, we examined the expression and distribution of murine CLEC4F, determined its binding specificity by glycan array, and investigated its function using CLEC4F knockout (Clec4f-/-) mice. We found that CLEC4F is a heavily glycosylated membrane protein co-expressed with F4/80 on Kupffer cells. In contrast to F4/80, CLEC4F is detectable in fetal livers at embryonic day 11.5 (E11.5) but not in yolk sac, suggesting the expression of CLEC4F is induced as cells migrate from yolk cells to the liver. Even though CLEC4F is not detectable in tissues outside liver, both residential Kupffer cells and infiltrating mononuclear cells surrounding liver abscesses are CLEC4F-positive upon Listeria monocytogenes (L. monocytogenes) infection. While CLEC4F has strong binding to Gal and GalNAc, terminal fucosylation inhibits CLEC4F recognition to several glycans such as Fucosyl GM1, Globo H, Bb3∼4 and other fucosyl-glycans. Moreover, CLEC4F interacts with alpha-galactosylceramide (α-GalCer) in a calcium-dependent manner and participates in the presentation of α-GalCer to natural killer T (NKT) cells. This suggests that CLEC4F is a C-type lectin with diverse binding specificity expressed on residential Kupffer cells and infiltrating monocytes in the liver, and may play an important role to modulate glycolipids presentation on Kupffer cells. CLEC4F, a member of C-type lectin, was first purified from rat liver extract with high binding affinity to fucose, galactose (Gal), N-acetylgalactosamine (GalNAc), and un-sialylated glucosphingolipids with GalNAc or Gal terminus. However, the biological functions of CLEC4F have not been elucidated. To address this question, we examined the expression and distribution of murine CLEC4F, determined its binding specificity by glycan array, and investigated its function using CLEC4F knockout (Clec4f-/-) mice. We found that CLEC4F is a heavily glycosylated membrane protein co-expressed with F4/80 on Kupffer cells. In contrast to F4/80, CLEC4F is detectable in fetal livers at embryonic day 11.5 (E11.5) but not in yolk sac, suggesting the expression of CLEC4F is induced as cells migrate from yolk cells to the liver. Even though CLEC4F is not detectable in tissues outside liver, both residential Kupffer cells and infiltrating mononuclear cells surrounding liver abscesses are CLEC4F-positive upon Listeria monocytogenes (L. monocytogenes) infection. While CLEC4F has strong binding to Gal and GalNAc, terminal fucosylation inhibits CLEC4F recognition to several glycans such as Fucosyl GM1, Globo H, Bb3∼4 and other fucosyl-glycans. Moreover, CLEC4F interacts with alpha-galactosylceramide (α-GalCer) in a calcium-dependent manner and participates in the presentation of α-GalCer to natural killer T (NKT) cells. This suggests that CLEC4F is a C-type lectin with diverse binding specificity expressed on residential Kupffer cells and infiltrating monocytes in the liver, and may play an important role to modulate glycolipids presentation on Kupffer cells.CLEC4F, a member of C-type lectin, was first purified from rat liver extract with high binding affinity to fucose, galactose (Gal), N-acetylgalactosamine (GalNAc), and un-sialylated glucosphingolipids with GalNAc or Gal terminus. However, the biological functions of CLEC4F have not been elucidated. To address this question, we examined the expression and distribution of murine CLEC4F, determined its binding specificity by glycan array, and investigated its function using CLEC4F knockout (Clec4f-/-) mice. We found that CLEC4F is a heavily glycosylated membrane protein co-expressed with F4/80 on Kupffer cells. In contrast to F4/80, CLEC4F is detectable in fetal livers at embryonic day 11.5 (E11.5) but not in yolk sac, suggesting the expression of CLEC4F is induced as cells migrate from yolk cells to the liver. Even though CLEC4F is not detectable in tissues outside liver, both residential Kupffer cells and infiltrating mononuclear cells surrounding liver abscesses are CLEC4F-positive upon Listeria monocytogenes (L. monocytogenes) infection. While CLEC4F has strong binding to Gal and GalNAc, terminal fucosylation inhibits CLEC4F recognition to several glycans such as Fucosyl GM1, Globo H, Bb3∼4 and other fucosyl-glycans. Moreover, CLEC4F interacts with alpha-galactosylceramide (α-GalCer) in a calcium-dependent manner and participates in the presentation of α-GalCer to natural killer T (NKT) cells. This suggests that CLEC4F is a C-type lectin with diverse binding specificity expressed on residential Kupffer cells and infiltrating monocytes in the liver, and may play an important role to modulate glycolipids presentation on Kupffer cells. CLEC4F, a member of C-type lectin, was first purified from rat liver extract with high binding affinity to fucose, galactose (Gal), N-acetylgalactosamine (GalNAc), and un-sialylated glucosphingolipids with GalNAc or Gal terminus. However, the biological functions of CLEC4F have not been elucidated. To address this question, we examined the expression and distribution of murine CLEC4F, determined its binding specificity by glycan array, and investigated its function using CLEC4F knockout (Clec4f−/−) mice. We found that CLEC4F is a heavily glycosylated membrane protein co-expressed with F4/80 on Kupffer cells. In contrast to F4/80, CLEC4F is detectable in fetal livers at embryonic day 11.5 (E11.5) but not in yolk sac, suggesting the expression of CLEC4F is induced as cells migrate from yolk cells to the liver. Even though CLEC4F is not detectable in tissues outside liver, both residential Kupffer cells and infiltrating mononuclear cells surrounding liver abscesses are CLEC4F-positive upon Listeria monocytogenes (L. monocytogenes) infection. While CLEC4F has strong binding to Gal and GalNAc, terminal fucosylation inhibits CLEC4F recognition to several glycans such as Fucosyl GM1, Globo H, Bb3∼4 and other fucosyl-glycans. Moreover, CLEC4F interacts with alpha-galactosylceramide (α-GalCer) in a calcium-dependent manner and participates in the presentation of α-GalCer to natural killer T (NKT) cells. This suggests that CLEC4F is a C-type lectin with diverse binding specificity expressed on residential Kupffer cells and infiltrating monocytes in the liver, and may play an important role to modulate glycolipids presentation on Kupffer cells. CLEC4F, a member of C-type lectin, was first purified from rat liver extract with high binding affinity to fucose, galactose (Gal), N-acetylgalactosamine (GalNAc), and un-sialylated glucosphingolipids with GalNAc or Gal terminus. However, the biological functions of CLEC4F have not been elucidated. To address this question, we examined the expression and distribution of murine CLEC4F, determined its binding specificity by glycan array, and investigated its function using CLEC4F knockout ( Clec4f−/− ) mice. We found that CLEC4F is a heavily glycosylated membrane protein co-expressed with F4/80 on Kupffer cells. In contrast to F4/80, CLEC4F is detectable in fetal livers at embryonic day 11.5 (E11.5) but not in yolk sac, suggesting the expression of CLEC4F is induced as cells migrate from yolk cells to the liver. Even though CLEC4F is not detectable in tissues outside liver, both residential Kupffer cells and infiltrating mononuclear cells surrounding liver abscesses are CLEC4F-positive upon Listeria monocytogenes ( L. monocytogenes ) infection. While CLEC4F has strong binding to Gal and GalNAc, terminal fucosylation inhibits CLEC4F recognition to several glycans such as Fucosyl GM1, Globo H, Bb3∼4 and other fucosyl-glycans. Moreover, CLEC4F interacts with alpha-galactosylceramide (α-GalCer) in a calcium-dependent manner and participates in the presentation of α-GalCer to natural killer T (NKT) cells. This suggests that CLEC4F is a C-type lectin with diverse binding specificity expressed on residential Kupffer cells and infiltrating monocytes in the liver, and may play an important role to modulate glycolipids presentation on Kupffer cells. |
| Audience | Academic |
| Author | Tsai, Ching-Yen Yang, Chih-Ya Liang, Pi-Hui Chen, Jiun-Bo Tsai, Ting-Fen Wong, Chi-Huey Hsu, Tsui-Ling Wu, Chung-Yi Hsieh, Shie-Liang Tsai, Yi-Chen Netea, Mihai G. |
| AuthorAffiliation | 10 The Institute for Cancer Biology and Drug Discovery, College of Medical Science and Technology, Taipei Medical University, Taipei, Taiwan 4 Transgenic Core Facility, Institute of Molecular Biology, Academia Sinica, Taipei, Taiwan 5 School of Pharmacy, College of Medicine, National Taiwan University, Taipei, Taiwan 3 Department of Life Sciences and Institute of Genome Sciences, National Yang-Ming University, Taipei, Taiwan 2 Program in Molecular Medicine, National Yang-Ming University and Academia Sinica, Taipei, Taiwan 8 Institute of Clinical Medicine & Infection and Immunity Center, National Yang-Ming University, Taipei, Taiwan King’s College London School of Medicine, United Kingdom 6 Genomics Research Center, Academia Sinica, Taipei, Taiwan 9 Immunology Center, Taipei Veterans General Hospital, Taipei, Taiwan 1 Institute of Microbiology and Immunology, National Yang-Ming University, Taipei, Taiwan 7 Department of Internal Medicine, Radboud University Nijmegen Medical Centre, Nijmegen, Neth |
| AuthorAffiliation_xml | – name: 10 The Institute for Cancer Biology and Drug Discovery, College of Medical Science and Technology, Taipei Medical University, Taipei, Taiwan – name: King’s College London School of Medicine, United Kingdom – name: 3 Department of Life Sciences and Institute of Genome Sciences, National Yang-Ming University, Taipei, Taiwan – name: 5 School of Pharmacy, College of Medicine, National Taiwan University, Taipei, Taiwan – name: 4 Transgenic Core Facility, Institute of Molecular Biology, Academia Sinica, Taipei, Taiwan – name: 1 Institute of Microbiology and Immunology, National Yang-Ming University, Taipei, Taiwan – name: 7 Department of Internal Medicine, Radboud University Nijmegen Medical Centre, Nijmegen, Netherlands – name: 8 Institute of Clinical Medicine & Infection and Immunity Center, National Yang-Ming University, Taipei, Taiwan – name: 6 Genomics Research Center, Academia Sinica, Taipei, Taiwan – name: 2 Program in Molecular Medicine, National Yang-Ming University and Academia Sinica, Taipei, Taiwan – name: 9 Immunology Center, Taipei Veterans General Hospital, Taipei, Taiwan |
| Author_xml | – sequence: 1 givenname: Chih-Ya surname: Yang fullname: Yang, Chih-Ya – sequence: 2 givenname: Jiun-Bo surname: Chen fullname: Chen, Jiun-Bo – sequence: 3 givenname: Ting-Fen surname: Tsai fullname: Tsai, Ting-Fen – sequence: 4 givenname: Yi-Chen surname: Tsai fullname: Tsai, Yi-Chen – sequence: 5 givenname: Ching-Yen surname: Tsai fullname: Tsai, Ching-Yen – sequence: 6 givenname: Pi-Hui surname: Liang fullname: Liang, Pi-Hui – sequence: 7 givenname: Tsui-Ling surname: Hsu fullname: Hsu, Tsui-Ling – sequence: 8 givenname: Chung-Yi surname: Wu fullname: Wu, Chung-Yi – sequence: 9 givenname: Mihai G. surname: Netea fullname: Netea, Mihai G. – sequence: 10 givenname: Chi-Huey surname: Wong fullname: Wong, Chi-Huey – sequence: 11 givenname: Shie-Liang surname: Hsieh fullname: Hsieh, Shie-Liang |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/23762286$$D View this record in MEDLINE/PubMed |
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| ContentType | Journal Article |
| Copyright | COPYRIGHT 2013 Public Library of Science 2013 Yang et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: https://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. 2013 Yang et al 2013 Yang et al |
| Copyright_xml | – notice: COPYRIGHT 2013 Public Library of Science – notice: 2013 Yang et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: https://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. – notice: 2013 Yang et al 2013 Yang et al |
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| DOI | 10.1371/journal.pone.0065070 |
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| Snippet | CLEC4F, a member of C-type lectin, was first purified from rat liver extract with high binding affinity to fucose, galactose (Gal), N-acetylgalactosamine... |
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| SubjectTerms | Abscesses Acetylgalactosamine - chemistry Acetylgalactosamine - immunology Animal tissues Animals Antigens Antigens, Differentiation - genetics Antigens, Differentiation - immunology Binding Binding Sites Biology Calcium Carbohydrate Sequence Cell migration Embryo, Mammalian Embryos Fetuses Fucose Galactose Galactose - chemistry Galactose - immunology Galactosylceramide Galactosylceramides - chemistry Galactosylceramides - immunology Gene Expression Regulation, Developmental Genomics Glycan Glycolipids Glycosylation Hepatocytes Immunology Infections Kupffer cells Kupffer Cells - immunology Kupffer Cells - metabolism Kupffer Cells - microbiology Laboratory animals Lectins Lectins, C-Type - chemistry Lectins, C-Type - genetics Lectins, C-Type - immunology Leukocytes (mononuclear) Listeria Listeria monocytogenes Listeria monocytogenes - immunology Listeriosis - genetics Listeriosis - immunology Listeriosis - metabolism Listeriosis - microbiology Liver Liver - immunology Liver - metabolism Liver - microbiology Liver diseases Medicine Membrane lipids Membrane proteins Mice Mice, Knockout Molecular Sequence Data Monocytes Monocytes - immunology Monocytes - metabolism Monocytes - microbiology N-Acetylgalactosamine Natural killer cells Natural Killer T-Cells - immunology Natural Killer T-Cells - metabolism Natural Killer T-Cells - microbiology Plant lipids Polysaccharides Protein Binding Rodents Studies T cell receptors Yolk Yolk sac |
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| Title | CLEC4F Is an Inducible C-Type Lectin in F4/80-Positive Cells and Is Involved in Alpha-Galactosylceramide Presentation in Liver |
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