RRC ID 10897
Author Jung YK, Jin JS, Jeong JH, Kim HN, Park NR, Choi JY.
Title DICAM, a novel dual immunoglobulin domain containing cell adhesion molecule interacts with alphavbeta3 integrin.
Journal J Cell Physiol
Abstract 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.
Volume 216(3)
Pages 603-14
Published 2008-9-1
DOI 10.1002/jcp.21438
PMID 18366072
MeSH Amino Acid Sequence Animals Cell Adhesion / physiology* Cell Adhesion Molecules / classification Cell Adhesion Molecules / genetics Cell Adhesion Molecules / metabolism* Cell Line Humans Immunoglobulins / metabolism Integrin alphaVbeta3 / genetics Integrin alphaVbeta3 / metabolism* Membrane Proteins / classification Membrane Proteins / genetics Membrane Proteins / metabolism* Molecular Sequence Data Phylogeny Protein Structure, Tertiary Sequence Alignment Tissue Distribution
IF 5.546
Times Cited 12
WOS Category PHYSIOLOGY CELL BIOLOGY
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Human and Animal Cells LLC(RCB0558)