Linked Life Data

10224141

Source:http://linkedlifedata.com/resource/pubmed/id/10224141

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
19
pubmed:dateCreated
1999-6-3
pubmed:databankReference
pubmed:abstractText
Collectins are a C-lectin family with collagen-like sequences and carbohydrate recognition domains. These proteins can bind to carbohydrate antigens of microorganisms and inhibit their infection by direct neutralization and agglutination, the activation of complement through the lectin pathway, and opsonization by collectin receptors. Here we report the cloning of a cDNA encoding human collectin from liver (CL-L1 (collectin liver 1)) that has typical collectin structural characteristics, consisting of an N-terminal cysteine-rich domain, a collagen-like domain, a neck domain, and a carbohydrate recognition domain. The cDNA has an insert of 831 base pairs coding for a protein of 277 amino acid residues. The deduced amino acid sequence shows that this collectin has a unique repeat of four lysine residues in its C-terminal area. Northern blot, Western blot, and reverse transcription-polymerase chain reaction analyses showed that CL-L1 is present mainly in liver as a cytosolic protein and at low levels in placenta. More sensitive analyses by reverse transcription-polymerase chain reactions showed that most tissues (except skeletal muscle) have CL-L1 mRNA. Zoo-blot analysis indicated that CL-L1 is limited to mammals and birds. A chromosomal localization study indicated that the CL-L1 gene localizes to chromosome 8q23-q24.1, different from chromosome 10 of other human collectin genes. Expression studies of fusion proteins lacking the collagen and N-terminal domains produced in Escherichia coli affirmed that CL-L1 binds mannose weakly. CL-L1 and recombinant CL-L1 fusion proteins do not bind to mannan columns. Analysis of the phylogenetic tree of CL-L1 and other collectins indicated that CL-L1 belongs to a fourth subfamily of collectins following the mannan-binding protein, surfactant protein A, and surfactant protein D subfamilies including bovine conglutinin and collectin-43 (CL-43). These findings indicate that CL-L1 may be involved in different biological functions.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
7
pubmed:volume
274
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
13681-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:10224141-Amino Acid Sequence, pubmed-meshheading:10224141-Animals, pubmed-meshheading:10224141-Base Sequence, pubmed-meshheading:10224141-Blotting, Northern, pubmed-meshheading:10224141-Carrier Proteins, pubmed-meshheading:10224141-Chromosome Mapping, pubmed-meshheading:10224141-Chromosomes, Human, Pair 8, pubmed-meshheading:10224141-Cloning, Molecular, pubmed-meshheading:10224141-Collectins, pubmed-meshheading:10224141-DNA, Complementary, pubmed-meshheading:10224141-Escherichia coli, pubmed-meshheading:10224141-Humans, pubmed-meshheading:10224141-Liver, pubmed-meshheading:10224141-Molecular Sequence Data, pubmed-meshheading:10224141-Phylogeny, pubmed-meshheading:10224141-RNA, Messenger, pubmed-meshheading:10224141-Recombinant Proteins, pubmed-meshheading:10224141-Reverse Transcriptase Polymerase Chain Reaction, pubmed-meshheading:10224141-Sequence Homology, Amino Acid
pubmed:year
1999
pubmed:articleTitle
Molecular cloning of a novel human collectin from liver (CL-L1).
pubmed:affiliation
Department of Pathology, Research Institute for Microbial Diseases, Osaka University, Suita, Osaka 565, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't