Source:http://linkedlifedata.com/resource/pubmed/id/21086138
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions |
umls-concept:C0008807,
umls-concept:C0009015,
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umls-concept:C0179586,
umls-concept:C0185117,
umls-concept:C0205314,
umls-concept:C0449432,
umls-concept:C0599577,
umls-concept:C0679622,
umls-concept:C1155266,
umls-concept:C1179435,
umls-concept:C1422073,
umls-concept:C1422760,
umls-concept:C1524073,
umls-concept:C1548799,
umls-concept:C1657858,
umls-concept:C1705248,
umls-concept:C1706092,
umls-concept:C1706433,
umls-concept:C1883220,
umls-concept:C2245693,
umls-concept:C2349975,
umls-concept:C2911684
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| pubmed:issue |
3
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| pubmed:dateCreated |
2010-12-3
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| pubmed:abstractText |
The CAP superfamily is a group of proteins that have been linked to several biological functions such as reproduction, cancer, and immune defense. A differential screening between lipopolysaccharide (LPS)-challenged and naive Ciona intestinalis has been performed to identify LPS-induced genes. This strategy has allowed the isolation of a full-length 1471-bp cDNA encoding for a 413-amino-acid protein (CiCAP). In silico analysis has shown that this polypeptide displays a modular structure with similarities to vertebrate CAP-superfamily proteins and to a collagen-binding adhesin of Streptococcus mutans. Domain organization analysis and alignment of CiCAP to other vertebrate CAP proteins have revealed a novel structure suggesting that this protein originated from a common ancestor gene that gave rise to many subfamilies of mosaic proteins with novel functions. Quantitative mRNA expression performed by real-time polymerase chain reaction analysis has demonstrated that this gene is rapidly activated in the pharynx of C. intestinalis a few hours after LPS injection. Moreover, in situ hybridization has shown that CiCAP mRNA is highly expressed by hemocytes with large granules contained inside the pharynx vessels. Thus, CiCAP represents a protein with novel structural domains involved in ascidian immune responses.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical | |
| pubmed:status |
MEDLINE
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| pubmed:month |
Dec
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| pubmed:issn |
1432-0878
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| pubmed:author | |
| pubmed:issnType |
Electronic
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| pubmed:volume |
342
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
411-21
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| pubmed:meshHeading |
pubmed-meshheading:21086138-Amino Acid Sequence,
pubmed-meshheading:21086138-Animals,
pubmed-meshheading:21086138-Base Sequence,
pubmed-meshheading:21086138-Ciona intestinalis,
pubmed-meshheading:21086138-Cloning, Molecular,
pubmed-meshheading:21086138-Hemocytes,
pubmed-meshheading:21086138-In Situ Hybridization,
pubmed-meshheading:21086138-Inflammation,
pubmed-meshheading:21086138-Lipopolysaccharides,
pubmed-meshheading:21086138-Molecular Sequence Data,
pubmed-meshheading:21086138-Phylogeny,
pubmed-meshheading:21086138-Polymerase Chain Reaction,
pubmed-meshheading:21086138-Proteins,
pubmed-meshheading:21086138-RNA, Messenger,
pubmed-meshheading:21086138-Sequence Alignment,
pubmed-meshheading:21086138-Sequence Analysis, DNA,
pubmed-meshheading:21086138-Sequence Homology, Amino Acid
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| pubmed:year |
2010
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| pubmed:articleTitle |
Cloning and expression of a novel component of the CAP superfamily enhanced in the inflammatory response to LPS of the ascidian Ciona intestinalis.
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| pubmed:affiliation |
Istituto di Biomedicina ed Immunologia Molecolare "Alberto Monroy" del Consiglio Nazionale delle Ricerche, Via Ugo La Malfa 153, 90146 Palermo, Italy.
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| pubmed:publicationType |
Journal Article
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