Source:http://linkedlifedata.com/resource/pubmed/id/18366072
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2008-6-23
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pubmed:abstractText |
Immunoglobulin (Ig) superfamily members are abundant with diverse functions including cell adhesion in various tissues. Here, we identified and characterized a novel adhesion molecule that belongs to the CTX protein family and named as DICAM (Dual Ig domain containing cell adhesion molecule). DICAM is a type I transmembrane protein with two V-type Ig domains in the extracellular region and a short cytoplasmic tail of 442 amino acids. DICAM is found to be expressed ubiquitously in various organs and cell lines. Subcellular localization of DICAM was observed in the cell-cell contact region and nucleus of cultured epithelial cells. Cell-cell contact region was colocalized with tight junction protein, ZO-1. The DICAM increased MDCK cell adhesion to 60% levels of fibronectin. DICAM mediated cell adhesion was specific for the alphavbeta3 integrin; other integrins, alpha2, alpha5, beta1, alpha2beta1, alpha5beta1, were not involved in cell adhesion. In identifying the interacting domain of DICAM with alphavbeta3, the Ig domain 2 showed higher cell adhesion activity than that of Ig domain 1. Although RGD motif in Ig domain 2 was engaged in cell adhesion, it was not participated in DICAM-alphavbeta3 mediated cell adhesion. Furthermore, differentially expressing DICAM stable cells showed well correlated cell to cell adhesion capability with integrin beta3-overexpressing cells. Collectively, these results indicate that DICAM, a novel dual Ig domain containing adhesion molecule, mediates cell adhesion via alphavbeta3 integrin.
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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 |
Sep
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pubmed:issn |
1097-4652
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
216
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
603-14
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pubmed:meshHeading |
pubmed-meshheading:18366072-Amino Acid Sequence,
pubmed-meshheading:18366072-Animals,
pubmed-meshheading:18366072-Cell Adhesion,
pubmed-meshheading:18366072-Cell Adhesion Molecules,
pubmed-meshheading:18366072-Cell Line,
pubmed-meshheading:18366072-Humans,
pubmed-meshheading:18366072-Immunoglobulins,
pubmed-meshheading:18366072-Integrin alphaVbeta3,
pubmed-meshheading:18366072-Membrane Proteins,
pubmed-meshheading:18366072-Molecular Sequence Data,
pubmed-meshheading:18366072-Phylogeny,
pubmed-meshheading:18366072-Protein Structure, Tertiary,
pubmed-meshheading:18366072-Sequence Alignment,
pubmed-meshheading:18366072-Tissue Distribution
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pubmed:year |
2008
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pubmed:articleTitle |
DICAM, a novel dual immunoglobulin domain containing cell adhesion molecule interacts with alphavbeta3 integrin.
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pubmed:affiliation |
Department of Biochemistry and Cell Biology, Kyungpook National University, Daegu, Republic of Korea.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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