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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
1999-4-13
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pubmed:databankReference |
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pubmed:abstractText |
Mannan-binding lectin (MBL) forms a multimolecular complex with at least two MBL-associated serine proteases, MASP-1 and MASP-2. This complex initiates the MBL pathway of complement activation by binding to carbohydrate structures present on bacteria, yeast, and viruses. MASP-1 and MASP-2 are composed of modular structural motifs similar to those of the C1q-associated serine proteases C1r and C1s. Another protein of 19 kDa with the same N-terminal sequence as the 76-kDa MASP-2 protein is consistently detected as part of the MBL/MASP complex. In this study, we present the primary structure of this novel MBL-associated plasma protein of 19 kDa, MAp19, and demonstrate that MAp19 and MASP-2 are encoded by two different mRNA species generated by alternative splicing/polyadenylation from one structural gene.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Blood Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Collectins,
http://linkedlifedata.com/resource/pubmed/chemical/Lectins,
http://linkedlifedata.com/resource/pubmed/chemical/MASP2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Mannans,
http://linkedlifedata.com/resource/pubmed/chemical/Mannose-Binding Protein-Associated...,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Serine Endopeptidases
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0022-1767
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
162
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3481-90
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pubmed:dateRevised |
2010-8-25
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pubmed:meshHeading |
pubmed-meshheading:10092804-Alternative Splicing,
pubmed-meshheading:10092804-Amino Acid Sequence,
pubmed-meshheading:10092804-Animals,
pubmed-meshheading:10092804-Base Sequence,
pubmed-meshheading:10092804-Blood Proteins,
pubmed-meshheading:10092804-Carrier Proteins,
pubmed-meshheading:10092804-Collectins,
pubmed-meshheading:10092804-Complement Activation,
pubmed-meshheading:10092804-Exons,
pubmed-meshheading:10092804-Genes,
pubmed-meshheading:10092804-Humans,
pubmed-meshheading:10092804-Introns,
pubmed-meshheading:10092804-Lectins,
pubmed-meshheading:10092804-Mannans,
pubmed-meshheading:10092804-Mannose-Binding Protein-Associated Serine Proteases,
pubmed-meshheading:10092804-Molecular Sequence Data,
pubmed-meshheading:10092804-Molecular Weight,
pubmed-meshheading:10092804-RNA, Messenger,
pubmed-meshheading:10092804-Rats,
pubmed-meshheading:10092804-Sequence Analysis, DNA,
pubmed-meshheading:10092804-Serine Endopeptidases,
pubmed-meshheading:10092804-Transcription, Genetic
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pubmed:year |
1999
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pubmed:articleTitle |
Two constituents of the initiation complex of the mannan-binding lectin activation pathway of complement are encoded by a single structural gene.
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pubmed:affiliation |
Department of Microbiology and Immunology, University of Leicester, United Kingdom.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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