Simultaneous activation of complement and coagulation by MBL-associated serine protease 2
The complement system is an important immune mechanism mediating both recognition and elimination of foreign bodies. The lectin pathway is one pathway of three by which the complement system is activated. The characteristic protease of this pathway is Mannan-binding lectin (MBL)-associated serine pr...
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Published in | PloS one Vol. 2; no. 7; p. e623 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
United States
Public Library of Science
18.07.2007
Public Library of Science (PLoS) |
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Abstract | The complement system is an important immune mechanism mediating both recognition and elimination of foreign bodies. The lectin pathway is one pathway of three by which the complement system is activated. The characteristic protease of this pathway is Mannan-binding lectin (MBL)-associated serine protease 2 (MASP2), which cleaves complement proteins C2 and C4. We present a novel and alternative role of MASP2 in the innate immune system. We have shown that MASP2 is capable of promoting fibrinogen turnover by cleavage of prothrombin, generating thrombin. By using a truncated active form of MASP2 as well as full-length MASP2 in complex with MBL, we have shown that the thrombin generated is active and can cleave both factor XIII and fibrinogen, forming cross-linked fibrin. To explore the biological significance of these findings we showed that fibrin was covalently bound on a bacterial surface to which MBL/MASP2 complexes were bound. These findings suggest that, as has been proposed for invertebrates, limited clotting may contribute to the innate immune response. |
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AbstractList | The complement system is an important immune mechanism mediating both recognition and elimination of foreign bodies. The lectin pathway is one pathway of three by which the complement system is activated. The characteristic protease of this pathway is Mannan-binding lectin (MBL)-associated serine protease 2 (MASP2), which cleaves complement proteins C2 and C4. We present a novel and alternative role of MASP2 in the innate immune system. We have shown that MASP2 is capable of promoting fibrinogen turnover by cleavage of prothrombin, generating thrombin. By using a truncated active form of MASP2 as well as full-length MASP2 in complex with MBL, we have shown that the thrombin generated is active and can cleave both factor XIII and fibrinogen, forming cross-linked fibrin. To explore the biological significance of these findings we showed that fibrin was covalently bound on a bacterial surface to which MBL/MASP2 complexes were bound. These findings suggest that, as has been proposed for invertebrates, limited clotting may contribute to the innate immune response. |
Audience | Academic |
Author | Krarup, Anders Gál, Péter Presanis, Julia S Wallis, Russell Sim, Robert B |
AuthorAffiliation | 1 MRC Immunochemistry Unit, Department of Biochemistry, University of Oxford, Oxford, United Kingdom 2 Department of Infection, Immunity and Inflammation, University of Leicester, Leicester, United Kingdom Institut Pasteur Korea, Republic of Korea 3 Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest, Hungary |
AuthorAffiliation_xml | – name: 1 MRC Immunochemistry Unit, Department of Biochemistry, University of Oxford, Oxford, United Kingdom – name: 3 Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest, Hungary – name: 2 Department of Infection, Immunity and Inflammation, University of Leicester, Leicester, United Kingdom – name: Institut Pasteur Korea, Republic of Korea |
Author_xml | – sequence: 1 givenname: Anders surname: Krarup fullname: Krarup, Anders email: anders.krarup@bioch.ox.ac.uk organization: MRC Immunochemistry Unit, Department of Biochemistry, University of Oxford, Oxford, United Kingdom. anders.krarup@bioch.ox.ac.uk – sequence: 2 givenname: Russell surname: Wallis fullname: Wallis, Russell – sequence: 3 givenname: Julia S surname: Presanis fullname: Presanis, Julia S – sequence: 4 givenname: Péter surname: Gál fullname: Gál, Péter – sequence: 5 givenname: Robert B surname: Sim fullname: Sim, Robert B |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/17637839$$D View this record in MEDLINE/PubMed |
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ContentType | Journal Article |
Copyright | COPYRIGHT 2007 Public Library of Science 2007 Krarup et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License (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. Krarup et al. 2007 |
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Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Conceived and designed the experiments: RS AK. Performed the experiments: AK JP. Analyzed the data: RS AK PG. Contributed reagents/materials/analysis tools: RS AK RW PG. Wrote the paper: RS AK RW. |
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References | JA Huntington (ref6) 2005; 3 MR Downing (ref5) 1975; 250 MM Krem (ref7) 2000; 10 KB Reid (ref1) 1981; 50 J Travis (ref8) 1983 JS Presanis (ref10) 2004; 40 S Thiel (ref4) 1997; 386 CB Chen (ref13) 2004; 279 P Matsudaira (ref29) 1987; 262 RB Sim (ref30) 1981; C M Matsushita (ref3) 2002; 168 AB Kay (ref17) 1974; 27 L Tang (ref23) 1993; 178 RN Pike (ref16) 2005; 272 V Rossi (ref32) 2001; 276 G Ambrus (ref9) 2003; 170 CB Chen (ref12) 2001; 276 RJ Kaufman (ref31) 1991; 19 Y Masuda (ref18) 2001; 22 G Fairbanks (ref27) 1971; 10 RB Sim (ref35) 1981; C T Muta (ref11) 1996; 8 A Krarup (ref15) 2005; 73 K Hajela (ref24) 2002; 205 RM Senior (ref19) 1986; 77 M Huber-Lang (ref25) 2006; 12 UK Laemmli (ref26) 1970; 227 Y Pilatte (ref34) 1989; 120 MJ Flick (ref21) 2004; 113 WF Skogen (ref20) 1988; 71 L Bajzar (ref33) 1990; 265 A Krarup (ref2) 2004; 279 IK Mullarky (ref22) 2005; 73 PJ Fraker (ref28) 1978; 80 Z Bereczky (ref14) 2003; 33 |
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SubjectTerms | Animals Bacteria Biochemistry Biochemistry/Macromolecular Chemistry Blood Coagulation - genetics Blood Coagulation - physiology Clotting Coagulation Coagulation factors Complement Complement activation Complement Activation - physiology Complement component C2 Complement component C4 Cricetinae Crosslinking Enzymes Factor Xa - genetics Factor Xa - metabolism Factor XIII - metabolism Fibrin Fibrin - metabolism Fibrinogen Fibrinogen - metabolism Foreign bodies Hematology Immune response Immune system Immunology Immunology/Immunity to Infections Immunology/Innate Immunity Innate immunity Invertebrates Lectins Mannan Mannose-binding lectin Mannose-Binding Lectin - metabolism Mannose-Binding Protein-Associated Serine Proteases - genetics Mannose-Binding Protein-Associated Serine Proteases - metabolism MASP-2 protein Membranes Microorganisms Pathogens Peptide Fragments - metabolism Polypeptides Protease Proteases Proteins Prothrombin Prothrombin - genetics Prothrombin - metabolism Serine Serine proteinase Thrombin |
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Title | Simultaneous activation of complement and coagulation by MBL-associated serine protease 2 |
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