Sialylation on O-glycans protects platelets from clearance by liver Kupffer cells
Most platelet membrane proteins are modified by mucin-type core 1-derived glycans (O-glycans). However, the biological importance of O-glycans in platelet clearance is unclear. Here, we generated mice with a hematopoietic cell-specific loss of O-glycans (HC C1galt1 −/−). These mice lack O-glycans on...
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| Published in | Proceedings of the National Academy of Sciences - PNAS Vol. 114; no. 31; pp. 8360 - 8365 |
|---|---|
| Main Authors | , , , , , , , , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
National Academy of Sciences
01.08.2017
|
| Subjects | |
| Online Access | Get full text |
| ISSN | 0027-8424 1091-6490 1091-6490 |
| DOI | 10.1073/pnas.1707662114 |
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| Abstract | Most platelet membrane proteins are modified by mucin-type core 1-derived glycans (O-glycans). However, the biological importance of O-glycans in platelet clearance is unclear. Here, we generated mice with a hematopoietic cell-specific loss of O-glycans (HC C1galt1
−/−). These mice lack O-glycans on platelets and exhibit reduced peripheral platelet numbers. Platelets from HC C1galt1
−/− mice show reduced levels of α-2,3-linked sialic acids and increased accumulation in the liver relative to wild-type platelets. The preferential accumulation of HC C1galt1
−/− platelets in the liver was reduced in mice lacking the hepatic asialoglycoprotein receptor [Ashwell–Morell receptor (AMR)]. However, we found that Kupffer cells are the primary cells phagocytosing HC C1galt1
−/− platelets in the liver. Our results demonstrate that hepatic AMR promotes preferential adherence to and phagocytosis of desialylated and/or HC C1galt1
−/− platelets by the Kupffer cell through its C-type lectin receptor CLEC4F. These findings provide insights into an essential role for core 1 O-glycosylation of platelets in their clearance in the liver. |
|---|---|
| AbstractList | Most platelet membrane proteins are modified by mucin-type core 1-derived glycans (O-glycans). However, the biological importance of O-glycans in platelet clearance is unclear. Here, we generated mice with a hematopoietic cell-specific loss of O-glycans (HC C1galt1-/-). These mice lack O-glycans on platelets and exhibit reduced peripheral platelet numbers. Platelets from HC C1galt1-/- mice show reduced levels of α-2,3-linked sialic acids and increased accumulation in the liver relative to wild-type platelets. The preferential accumulation of HC C1galt1-/- platelets in the liver was reduced in mice lacking the hepatic asialoglycoprotein receptor [Ashwell-Morell receptor (AMR)]. However, we found that Kupffer cells are the primary cells phagocytosing HC C1galt1-/- platelets in the liver. Our results demonstrate that hepatic AMR promotes preferential adherence to and phagocytosis of desialylated and/or HC C1galt1-/- platelets by the Kupffer cell through its C-type lectin receptor CLEC4F. These findings provide insights into an essential role for core 1 O-glycosylation of platelets in their clearance in the liver. Most platelet membrane proteins are modified by mucin-type core 1-derived glycans (O-glycans). However, the biological importance of O-glycans in platelet clearance is unclear. Here, we generated mice with a hematopoietic cell-specific loss of O-glycans (HC C1galt1-/- ). These mice lack O-glycans on platelets and exhibit reduced peripheral platelet numbers. Platelets from HC C1galt1-/- mice show reduced levels of α-2,3-linked sialic acids and increased accumulation in the liver relative to wild-type platelets. The preferential accumulation of HC C1galt1-/- platelets in the liver was reduced in mice lacking the hepatic asialoglycoprotein receptor [Ashwell-Morell receptor (AMR)]. However, we found that Kupffer cells are the primary cells phagocytosing HC C1galt1-/- platelets in the liver. Our results demonstrate that hepatic AMR promotes preferential adherence to and phagocytosis of desialylated and/or HC C1galt1-/- platelets by the Kupffer cell through its C-type lectin receptor CLEC4F. These findings provide insights into an essential role for core 1 O-glycosylation of platelets in their clearance in the liver.Most platelet membrane proteins are modified by mucin-type core 1-derived glycans (O-glycans). However, the biological importance of O-glycans in platelet clearance is unclear. Here, we generated mice with a hematopoietic cell-specific loss of O-glycans (HC C1galt1-/- ). These mice lack O-glycans on platelets and exhibit reduced peripheral platelet numbers. Platelets from HC C1galt1-/- mice show reduced levels of α-2,3-linked sialic acids and increased accumulation in the liver relative to wild-type platelets. The preferential accumulation of HC C1galt1-/- platelets in the liver was reduced in mice lacking the hepatic asialoglycoprotein receptor [Ashwell-Morell receptor (AMR)]. However, we found that Kupffer cells are the primary cells phagocytosing HC C1galt1-/- platelets in the liver. Our results demonstrate that hepatic AMR promotes preferential adherence to and phagocytosis of desialylated and/or HC C1galt1-/- platelets by the Kupffer cell through its C-type lectin receptor CLEC4F. These findings provide insights into an essential role for core 1 O-glycosylation of platelets in their clearance in the liver. Although many platelet glycoproteins, such as GPIbα and GPIIb/IIIa, are predominately modified by O-glycans, the biological importance of O-glycans in platelet homeostasis is unclear. Here, we report that platelets lacking O-glycans exhibit a reduced life-span and increased clearance in the liver due to defective sialylation. We found that Kupffer cells play a major role in clearing desialylated O-glycan–deficient platelets in cooperation with hepatocytes via the hepatic asialoglycoprotein receptor. These findings reveal how O-glycosylation regulates platelet homeostasis and clearance; they may also provide insights into the pathogenesis of disorders with thrombocytopenia such as sepsis and immune thrombocytopenia refractory to splenectomy. Most platelet membrane proteins are modified by mucin-type core 1-derived glycans (O-glycans). However, the biological importance of O-glycans in platelet clearance is unclear. Here, we generated mice with a hematopoietic cell-specific loss of O-glycans (HC C1galt1 −/− ). These mice lack O-glycans on platelets and exhibit reduced peripheral platelet numbers. Platelets from HC C1galt1 −/− mice show reduced levels of α-2,3-linked sialic acids and increased accumulation in the liver relative to wild-type platelets. The preferential accumulation of HC C1galt1 −/− platelets in the liver was reduced in mice lacking the hepatic asialoglycoprotein receptor [Ashwell–Morell receptor (AMR)]. However, we found that Kupffer cells are the primary cells phagocytosing HC C1galt1 −/− platelets in the liver. Our results demonstrate that hepatic AMR promotes preferential adherence to and phagocytosis of desialylated and/or HC C1galt1 −/− platelets by the Kupffer cell through its C-type lectin receptor CLEC4F. These findings provide insights into an essential role for core 1 O-glycosylation of platelets in their clearance in the liver. Most platelet membrane proteins are modified by mucin-type core 1-derived glycans (O-glycans). However, the biological importance of O-glycans in platelet clearance is unclear. Here, we generated mice with a hematopoietic cell-specific loss of O-glycans (HC ). These mice lack O-glycans on platelets and exhibit reduced peripheral platelet numbers. Platelets from HC mice show reduced levels of α-2,3-linked sialic acids and increased accumulation in the liver relative to wild-type platelets. The preferential accumulation of HC platelets in the liver was reduced in mice lacking the hepatic asialoglycoprotein receptor [Ashwell-Morell receptor (AMR)]. However, we found that Kupffer cells are the primary cells phagocytosing HC platelets in the liver. Our results demonstrate that hepatic AMR promotes preferential adherence to and phagocytosis of desialylated and/or HC platelets by the Kupffer cell through its C-type lectin receptor CLEC4F. These findings provide insights into an essential role for core 1 O-glycosylation of platelets in their clearance in the liver. Most platelet membrane proteins are modified by mucin-type core 1-derived glycans (O-glycans). However, the biological importance of O-glycans in platelet clearance is unclear. Here, we generated mice with a hematopoietic cell-specific loss of O-glycans (HC C1galt1 −/−). These mice lack O-glycans on platelets and exhibit reduced peripheral platelet numbers. Platelets from HC C1galt1 −/− mice show reduced levels of α-2,3-linked sialic acids and increased accumulation in the liver relative to wild-type platelets. The preferential accumulation of HC C1galt1 −/− platelets in the liver was reduced in mice lacking the hepatic asialoglycoprotein receptor [Ashwell–Morell receptor (AMR)]. However, we found that Kupffer cells are the primary cells phagocytosing HC C1galt1 −/− platelets in the liver. Our results demonstrate that hepatic AMR promotes preferential adherence to and phagocytosis of desialylated and/or HC C1galt1 −/− platelets by the Kupffer cell through its C-type lectin receptor CLEC4F. These findings provide insights into an essential role for core 1 O-glycosylation of platelets in their clearance in the liver. |
| Author | Bai, Xia Li, Yun Sonon, Roberto McEver, Rodger P. Ruan, Changgeng Liu, Zhenghui Fu, Jianxin McGee, Samuel McDaniel, J. Michael Yago, Tadayuki Xia, Lijun Kondo, Yuji Ling, Yun Shao, Bojing Marth, Jamey D. Qin, Yannan Hoover, Christopher Azadi, Parastoo Song, Jianhua |
| Author_xml | – sequence: 1 givenname: Yun surname: Li fullname: Li, Yun organization: Jiangsu Institute of Hematology, Key Laboratory of Thrombosis and Hemostasis of Ministry of Health, The First Affiliated Hospital of Soochow University, Suzhou, Jiangsu 215006, China – sequence: 2 givenname: Jianxin surname: Fu fullname: Fu, Jianxin organization: Jiangsu Institute of Hematology, Key Laboratory of Thrombosis and Hemostasis of Ministry of Health, The First Affiliated Hospital of Soochow University, Suzhou, Jiangsu 215006, China – sequence: 3 givenname: Yun surname: Ling fullname: Ling, Yun organization: The First People’s Hospital of Changzhou, Changzhou, Jiangsu 213000, China – sequence: 4 givenname: Tadayuki surname: Yago fullname: Yago, Tadayuki organization: Cardiovascular Biology Research Program, Oklahoma Medical Research Foundation, Oklahoma City, OK 73104 – sequence: 5 givenname: J. Michael surname: McDaniel fullname: McDaniel, J. Michael organization: Cardiovascular Biology Research Program, Oklahoma Medical Research Foundation, Oklahoma City, OK 73104 – sequence: 6 givenname: Jianhua surname: Song fullname: Song, Jianhua organization: Cardiovascular Biology Research Program, Oklahoma Medical Research Foundation, Oklahoma City, OK 73104 – sequence: 7 givenname: Xia surname: Bai fullname: Bai, Xia organization: Jiangsu Institute of Hematology, Key Laboratory of Thrombosis and Hemostasis of Ministry of Health, The First Affiliated Hospital of Soochow University, Suzhou, Jiangsu 215006, China – sequence: 8 givenname: Yuji surname: Kondo fullname: Kondo, Yuji organization: Cardiovascular Biology Research Program, Oklahoma Medical Research Foundation, Oklahoma City, OK 73104 – sequence: 9 givenname: Yannan surname: Qin fullname: Qin, Yannan organization: Department of Cell Biology and Genetics, School of Basic Medical Science, Xi’an Jiaotong University Health Science Center, Xi’an 710061, China – sequence: 10 givenname: Christopher surname: Hoover fullname: Hoover, Christopher organization: Cardiovascular Biology Research Program, Oklahoma Medical Research Foundation, Oklahoma City, OK 73104 – sequence: 11 givenname: Samuel surname: McGee fullname: McGee, Samuel organization: Cardiovascular Biology Research Program, Oklahoma Medical Research Foundation, Oklahoma City, OK 73104 – sequence: 12 givenname: Bojing surname: Shao fullname: Shao, Bojing organization: Cardiovascular Biology Research Program, Oklahoma Medical Research Foundation, Oklahoma City, OK 73104 – sequence: 13 givenname: Zhenghui surname: Liu fullname: Liu, Zhenghui organization: Cardiovascular Biology Research Program, Oklahoma Medical Research Foundation, Oklahoma City, OK 73104 – sequence: 14 givenname: Roberto surname: Sonon fullname: Sonon, Roberto organization: Complex Carbohydrate Research Center, University of Georgia, Athens, GA 30602 – sequence: 15 givenname: Parastoo surname: Azadi fullname: Azadi, Parastoo organization: Complex Carbohydrate Research Center, University of Georgia, Athens, GA 30602 – sequence: 16 givenname: Jamey D. surname: Marth fullname: Marth, Jamey D. organization: Department of Molecular, Cellular, and Developmental Biology, University of California, Santa Barbara, CA 93106 – sequence: 17 givenname: Rodger P. surname: McEver fullname: McEver, Rodger P. organization: Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104 – sequence: 18 givenname: Changgeng surname: Ruan fullname: Ruan, Changgeng organization: Jiangsu Institute of Hematology, Key Laboratory of Thrombosis and Hemostasis of Ministry of Health, The First Affiliated Hospital of Soochow University, Suzhou, Jiangsu 215006, China – sequence: 19 givenname: Lijun surname: Xia fullname: Xia, Lijun organization: Jiangsu Institute of Hematology, Key Laboratory of Thrombosis and Hemostasis of Ministry of Health, The First Affiliated Hospital of Soochow University, Suzhou, Jiangsu 215006, China |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/28716912$$D View this record in MEDLINE/PubMed |
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| Cites_doi | 10.1371/journal.pone.0160563 10.1074/jbc.M109056200 10.1182/blood-2011-05-355628 10.1016/j.cell.2007.01.037 10.1093/glycob/cwj126 10.1182/blood-2010-01-266080 10.1016/S0076-6879(06)16021-8 10.1073/pnas.0607872103 10.1186/1476-5926-1-1 10.1182/blood-2014-04-572107 10.1074/mcp.M500324-MCP200 10.1073/pnas.84.16.5615 10.1126/science.1085322 10.1007/978-3-642-29423-5_2 10.1371/journal.pone.0065070 10.1172/JCI36077 10.1182/blood-2007-12-129262 10.1016/0014-4827(86)90602-6 10.1182/blood-2010-02-270876 10.1038/ncomms8737 10.1073/pnas.1313905110 10.1038/282621a0 10.1182/blood-2009-02-203828 10.1038/nature12501 10.1038/nature13319 10.1002/hep.21378 10.1073/pnas.142005099 10.4049/jimmunol.1500775 10.1038/nm.2030 10.1093/glycob/cwr080 10.1371/journal.pone.0138655 10.1182/blood-2009-01-199414 10.1182/bloodadvances.2016002121 10.1182/blood-2013-11-462432 10.1016/S0308-2261(21)00131-4 10.1182/blood.V86.10.3789.bloodjournal86103789 10.1172/JCI45538 10.1083/jcb.200311112 10.1038/nm1760 10.1182/blood-2012-12-471102 10.1073/pnas.1208253109 10.1172/JCI110727 |
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| Notes | SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 14 ObjectType-Article-1 ObjectType-Feature-2 content type line 23 Author contributions: Y. Li, J.F., Y. Ling, T.Y., C.R., and L.X. designed research; Y. Li, J.F., Y. Ling, T.Y., J.M.M., J.S., Y.K., C.H., S.M., B.S., Z.L., R.S., and P.A. performed research; X.B. and J.D.M. contributed new reagents/analytic tools; Y. Li, J.F., Y. Ling, T.Y., Y.Q., R.S., P.A., J.D.M., R.P.M., and L.X. analyzed data; and T.Y. and L.X. wrote the paper. Edited by Barry S. Coller, The Rockefeller University, New York, NY, and approved June 23, 2017 (received for review May 10, 2017) 1Y. Li, J.F., and Y. Ling contributed equally to this work. |
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| References | de Gaetano G (e_1_3_3_1_2) 2001; 86 e_1_3_3_17_2 e_1_3_3_16_2 e_1_3_3_19_2 e_1_3_3_38_2 e_1_3_3_18_2 e_1_3_3_39_2 e_1_3_3_13_2 e_1_3_3_36_2 e_1_3_3_12_2 e_1_3_3_37_2 e_1_3_3_15_2 e_1_3_3_34_2 e_1_3_3_14_2 e_1_3_3_35_2 e_1_3_3_32_2 e_1_3_3_33_2 e_1_3_3_11_2 e_1_3_3_30_2 e_1_3_3_10_2 e_1_3_3_31_2 e_1_3_3_40_2 e_1_3_3_6_2 e_1_3_3_5_2 e_1_3_3_8_2 e_1_3_3_7_2 e_1_3_3_28_2 e_1_3_3_9_2 e_1_3_3_27_2 e_1_3_3_29_2 e_1_3_3_24_2 e_1_3_3_23_2 e_1_3_3_26_2 e_1_3_3_25_2 e_1_3_3_2_2 e_1_3_3_20_2 e_1_3_3_43_2 e_1_3_3_4_2 e_1_3_3_22_2 e_1_3_3_41_2 e_1_3_3_3_2 e_1_3_3_21_2 e_1_3_3_42_2 |
| References_xml | – ident: e_1_3_3_9_2 doi: 10.1371/journal.pone.0160563 – ident: e_1_3_3_27_2 doi: 10.1074/jbc.M109056200 – ident: e_1_3_3_14_2 doi: 10.1182/blood-2011-05-355628 – ident: e_1_3_3_10_2 doi: 10.1016/j.cell.2007.01.037 – ident: e_1_3_3_21_2 doi: 10.1093/glycob/cwj126 – ident: e_1_3_3_31_2 doi: 10.1182/blood-2010-01-266080 – ident: e_1_3_3_29_2 doi: 10.1016/S0076-6879(06)16021-8 – ident: e_1_3_3_34_2 doi: 10.1073/pnas.0607872103 – ident: e_1_3_3_38_2 doi: 10.1186/1476-5926-1-1 – ident: e_1_3_3_28_2 doi: 10.1182/blood-2014-04-572107 – ident: e_1_3_3_18_2 doi: 10.1074/mcp.M500324-MCP200 – ident: e_1_3_3_22_2 doi: 10.1073/pnas.84.16.5615 – ident: e_1_3_3_39_2 doi: 10.1126/science.1085322 – ident: e_1_3_3_17_2 doi: 10.1007/978-3-642-29423-5_2 – ident: e_1_3_3_32_2 doi: 10.1371/journal.pone.0065070 – ident: e_1_3_3_25_2 doi: 10.1172/JCI36077 – ident: e_1_3_3_8_2 doi: 10.1182/blood-2007-12-129262 – ident: e_1_3_3_37_2 doi: 10.1016/0014-4827(86)90602-6 – ident: e_1_3_3_2_2 doi: 10.1182/blood-2010-02-270876 – ident: e_1_3_3_7_2 doi: 10.1038/ncomms8737 – ident: e_1_3_3_12_2 doi: 10.1073/pnas.1313905110 – ident: e_1_3_3_42_2 doi: 10.1038/282621a0 – ident: e_1_3_3_19_2 doi: 10.1182/blood-2009-02-203828 – ident: e_1_3_3_3_2 doi: 10.1038/nature12501 – ident: e_1_3_3_20_2 doi: 10.1038/nature13319 – ident: e_1_3_3_40_2 doi: 10.1002/hep.21378 – ident: e_1_3_3_11_2 doi: 10.1073/pnas.142005099 – ident: e_1_3_3_41_2 doi: 10.4049/jimmunol.1500775 – ident: e_1_3_3_15_2 doi: 10.1038/nm.2030 – ident: e_1_3_3_30_2 doi: 10.1093/glycob/cwr080 – ident: e_1_3_3_36_2 doi: 10.1371/journal.pone.0138655 – ident: e_1_3_3_16_2 doi: 10.1182/blood-2009-01-199414 – ident: e_1_3_3_23_2 doi: 10.1182/bloodadvances.2016002121 – ident: e_1_3_3_4_2 doi: 10.1182/blood-2013-11-462432 – ident: e_1_3_3_5_2 doi: 10.1016/S0308-2261(21)00131-4 – ident: e_1_3_3_6_2 doi: 10.1182/blood.V86.10.3789.bloodjournal86103789 – ident: e_1_3_3_26_2 doi: 10.1172/JCI45538 – ident: e_1_3_3_24_2 doi: 10.1083/jcb.200311112 – volume: 86 start-page: 349 year: 2001 ident: e_1_3_3_1_2 article-title: Historical overview of the role of platelets in hemostasis and thrombosis publication-title: Haematologica – ident: e_1_3_3_13_2 doi: 10.1038/nm1760 – ident: e_1_3_3_35_2 doi: 10.1182/blood-2012-12-471102 – ident: e_1_3_3_33_2 doi: 10.1073/pnas.1208253109 – ident: e_1_3_3_43_2 doi: 10.1172/JCI110727 |
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| Snippet | Most platelet membrane proteins are modified by mucin-type core 1-derived glycans (O-glycans). However, the biological importance of O-glycans in platelet... Although many platelet glycoproteins, such as GPIbα and GPIIb/IIIa, are predominately modified by O-glycans, the biological importance of O-glycans in platelet... |
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| SubjectTerms | Accumulation Animals Asialoglycoprotein Receptor - metabolism Biological Sciences Blood platelets Blood Platelets - metabolism Cells Galactosyltransferases - genetics Glycosylation Hepatocytes Hepatocytes - metabolism Homeostasis - physiology Kupffer cells Kupffer Cells - metabolism Lectins, C-Type - metabolism Liver Liver - metabolism Membrane proteins Mice Mice, Inbred C57BL Mice, Knockout Mucin N-Acetylneuraminic Acid - metabolism Phagocytosis Platelets Polysaccharides Polysaccharides - metabolism Proteins Rodents Sialic acids Thrombocytopenia - pathology |
| Title | Sialylation on O-glycans protects platelets from clearance by liver Kupffer cells |
| URI | https://www.jstor.org/stable/26487218 https://www.ncbi.nlm.nih.gov/pubmed/28716912 https://www.proquest.com/docview/1946433821 https://www.proquest.com/docview/1921136968 https://pubmed.ncbi.nlm.nih.gov/PMC5547648 |
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