Linked Life Data

9794427

Source:http://linkedlifedata.com/resource/pubmed/id/9794427

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
1998-11-18
pubmed:databankReference
pubmed:abstractText
Mannose-binding lectin-associated serine protease (MASP) is a newly identified member of the serine protease superfamily. MASP is involved in host defense against pathogens through a novel system of complement activation, designated the lectin pathway. To elucidate the origin of the lectin pathway and the molecular evolution of MASP, we cloned six MASP cDNAs from five vertebrate species going from mammal to cyclostome. An alignment of the amino acid sequences deduced from the cDNAs revealed the presence of two different lineages of the MASP gene. This classification was supported by the precise correlation with two types of exon organization for the protease domain. One of the two lineages is unique in that a single exon encodes the protease domain, unlike most other serine proteases. All members of this group, termed the AGY type, have an AGY codon at the active site serine. A phylogenetic tree suggests that the AGY type diverged from another lineage, termed the TCN type, before the emergence of primitive vertebrates. Furthermore, the presence of MASP or MASP-like sequences in most vertebrate species suggests that the lectin pathway functions extensively in vertebrates and that its origin is traced back to the invertebrate stage.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0022-1767
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
161
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4924-30
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:9794427-Amino Acid Sequence, pubmed-meshheading:9794427-Animals, pubmed-meshheading:9794427-Carps, pubmed-meshheading:9794427-DNA, Complementary, pubmed-meshheading:9794427-Evolution, Molecular, pubmed-meshheading:9794427-Lampreys, pubmed-meshheading:9794427-Lectins, pubmed-meshheading:9794427-Mannose-Binding Protein-Associated Serine Proteases, pubmed-meshheading:9794427-Mice, pubmed-meshheading:9794427-Molecular Sequence Data, pubmed-meshheading:9794427-Phylogeny, pubmed-meshheading:9794427-Sequence Alignment, pubmed-meshheading:9794427-Sequence Homology, Amino Acid, pubmed-meshheading:9794427-Serine Endopeptidases, pubmed-meshheading:9794427-Sharks, pubmed-meshheading:9794427-Species Specificity, pubmed-meshheading:9794427-Vertebrates, pubmed-meshheading:9794427-Xenopus laevis
pubmed:year
1998
pubmed:articleTitle
Two lineages of mannose-binding lectin-associated serine protease (MASP) in vertebrates.
pubmed:affiliation
Department of Biochemistry, Fukushima Medical College, Japan.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't