Linked Life Data

17544822

Source:http://linkedlifedata.com/resource/pubmed/id/17544822

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4-5
pubmed:dateCreated
2007-6-4
pubmed:abstractText
Ficolin is a multimeric protein consisting of an N-terminal collagen-like domain and a C-terminal fibrinogen-like domain. The structure is similar to mannose-binding lectin (MBL) and complement C1q owing to the collagen-like stalk. Accumulating data indicate that a key function of ficolin is to recognize the carbohydrate moieties on pathogens as a pattern-recognition molecule. Two or three kinds of ficolin have been identified in each species of mammals. They are similar but with some differences in the expression site, location site, ligand-binding specificity and ability to form complexes with MBL-associated serine proteases (MASPs). Like MBL, some ficolins are serum lectins and can form a complex with MASPs and small MBL-associated protein (sMAP). This complex activates the complement through "the lectin pathway". Our recent study suggests that ficolin acts through two distinct routes: the lectin pathway and a primitive opsonophagocytosis. All these observations suggest that ficolins function in clearance of non-self, based on their location sites and their molecular features.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0171-2985
pubmed:author
pubmed:issnType
Print
pubmed:volume
212
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
371-9
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Role of ficolin in innate immunity and its molecular basis.
pubmed:affiliation
Department of Immunology, Fukushima Medical University School of Medicine, 1-Hikarigaoka, Fukushima 960-1295, Japan. yendo@fmu.ac.jp
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't