Source:http://linkedlifedata.com/resource/pubmed/id/18424734
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
9
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pubmed:dateCreated |
2008-4-21
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pubmed:abstractText |
The complement system plays an important role in innate immunity. In the lectin complement pathway, mannose-binding lectin (MBL) and ficolins act as recognition molecules, and MBL-associated serine protease (MASP) is a key enzyme. It has been suggested that MASP-2 is responsible for the activation of C4. Other serine proteases (MASP-1 and MASP-3) are also associated with MBL or ficolins; however, their functions are still controversial. In this study, a MASP-1- and MASP-3-deficient mouse model (MASP1/3(-/-)) was generated by a gene targeting strategy to investigate the roles of MASP-1 and MASP-3 in the lectin pathway. Serum derived from MASP1/3(-/-) mice showed significantly lower activity of both C4 and C3 deposition on mannan-agarose, and this low activity was restored by the addition of recombinant MASP-1. MASP-1/3-deficient serum showed a significant delay for activation of MASP-2 compared with normal serum. Reconstitution of recombinant MASP-1 in MASP-1/3-deficient serum was able to promote the activation of MASP-2. From these results, we propose that MASP-1 contributes to the activation of the lectin pathway, probably through the activation of MASP-2.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Complement C3,
http://linkedlifedata.com/resource/pubmed/chemical/Complement C4,
http://linkedlifedata.com/resource/pubmed/chemical/Lectins,
http://linkedlifedata.com/resource/pubmed/chemical/Mannose-Binding Lectin,
http://linkedlifedata.com/resource/pubmed/chemical/Mannose-Binding Protein-Associated...,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/ficolin
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0022-1767
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pubmed:author |
pubmed-author:EndoYuichiY,
pubmed-author:FujitaTeizoT,
pubmed-author:IshidaYumiY,
pubmed-author:IshiiNaotoN,
pubmed-author:IwakiDaisukeD,
pubmed-author:KannoKazukoK,
pubmed-author:MatsushitaMisaoM,
pubmed-author:MiuraShigetoS,
pubmed-author:SugamuraKazuoK,
pubmed-author:TakahashiMinoruM,
pubmed-author:XiongJieJ
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
180
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
6132-8
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pubmed:meshHeading |
pubmed-meshheading:18424734-Animals,
pubmed-meshheading:18424734-Complement C3,
pubmed-meshheading:18424734-Complement C4,
pubmed-meshheading:18424734-Complement Pathway, Mannose-Binding Lectin,
pubmed-meshheading:18424734-Lectins,
pubmed-meshheading:18424734-Mannose-Binding Lectin,
pubmed-meshheading:18424734-Mannose-Binding Protein-Associated Serine Proteases,
pubmed-meshheading:18424734-Mice,
pubmed-meshheading:18424734-Recombinant Proteins
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pubmed:year |
2008
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pubmed:articleTitle |
Mannose-binding lectin (MBL)-associated serine protease (MASP)-1 contributes to activation of the lectin complement pathway.
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pubmed:affiliation |
Department of Immunology, Fukushima Medical University School of Medicine, 1 Hikarigaoka, Fukushima, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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