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rdf:type |
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lifeskim:mentions |
umls-concept:C0008633,
umls-concept:C0009528,
umls-concept:C0017258,
umls-concept:C0017337,
umls-concept:C0023206,
umls-concept:C0036720,
umls-concept:C0086418,
umls-concept:C0208973,
umls-concept:C0449432,
umls-concept:C0449444,
umls-concept:C1179435,
umls-concept:C1517892,
umls-concept:C1524073,
umls-concept:C1548799,
umls-concept:C1704666,
umls-concept:C1705248
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pubmed:issue |
3
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pubmed:dateCreated |
2001-6-26
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pubmed:databankReference |
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pubmed:abstractText |
The proteases of the lectin pathway of complement activation, MASP-1 and MASP-2, are encoded by two separate genes. The MASP1 gene is located on chromosome 3q27, the MASP2 gene on chromosome 1p36.23-31. The genes for the classical complement activation pathway proteases, C1r and C1s, are linked on chromosome 12p13. We have shown that the MASP2 gene encodes two gene products, the 76 kDa MASP-2 serine protease and a plasma protein of 19 kDa, termed MAp19 or sMAP. Both gene products are components of the lectin pathway activation complex. We present the complete primary structure of the human MASP2 gene and the tight cluster that this locus forms with non-complement genes. A comparison of the MASP2 gene with the previously characterised C1s gene revealed identical positions of introns separating orthologous coding sequences, underlining the hypothesis that the C1s and MASP2 genes arose by exon shuffling from one ancestral gene.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
1466-4879
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pubmed:author |
pubmed-author:ConstantinescuCC,
pubmed-author:EndoYY,
pubmed-author:FriedlHH,
pubmed-author:FujitaTT,
pubmed-author:GregorySS,
pubmed-author:HallRR,
pubmed-author:HankelnTT,
pubmed-author:LynchN JNJ,
pubmed-author:SchwaebleWW,
pubmed-author:StoverCC,
pubmed-author:TakahashiMM,
pubmed-author:ThielSS,
pubmed-author:Vorup-JensenTT
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pubmed:issnType |
Print
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pubmed:volume |
2
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
119-27
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:11426320-Base Sequence,
pubmed-meshheading:11426320-Carrier Proteins,
pubmed-meshheading:11426320-Chromosome Mapping,
pubmed-meshheading:11426320-Chromosomes, Artificial, Bacterial,
pubmed-meshheading:11426320-Chromosomes, Human, Pair 1,
pubmed-meshheading:11426320-Collectins,
pubmed-meshheading:11426320-Complement Activation,
pubmed-meshheading:11426320-Genetic Linkage,
pubmed-meshheading:11426320-Humans,
pubmed-meshheading:11426320-Mannose-Binding Protein-Associated Serine Proteases,
pubmed-meshheading:11426320-Molecular Sequence Data,
pubmed-meshheading:11426320-Multigene Family,
pubmed-meshheading:11426320-Promoter Regions, Genetic,
pubmed-meshheading:11426320-RNA Splicing,
pubmed-meshheading:11426320-Serine Endopeptidases,
pubmed-meshheading:11426320-Transcription, Genetic
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pubmed:year |
2001
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pubmed:articleTitle |
The human gene for mannan-binding lectin-associated serine protease-2 (MASP-2), the effector component of the lectin route of complement activation, is part of a tightly linked gene cluster on chromosome 1p36.2-3.
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pubmed:affiliation |
Department of Microbiology and Immunology, University of Leicester, Leicester, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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