BEN, a surface glycoprotein of the immunoglobulin superfamily, is expressed in a variety of developing systems.

Pourquié, Olivier; Corbel, C.; Caer, Jean Pierre Le; Rossier, Jean; Douarin, Nicole M. Le

doi:10.1073/pnas.89.12.5261

Cited by 111 publications

(94 citation statements)

References 27 publications

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“…It has over 90% homology with the chicken adhesion molecule BEN/SC1/DM-GRASP (3)(4)(5), and it has 30% identity and 50% similarity with the human melanoma cell adhesion molecule Mel-CAM/MUC18/CD146 (6). Furthermore, ALCAM has 93% sequence identity with the candidate liver high density lipoprotein receptor HB2 (7).…”

mentioning

confidence: 99%

Molecular Basis for the Homophilic Activated Leukocyte Cell Adhesion Molecule (ALCAM)-ALCAM Interaction

Kempen¹,

Nelissen²,

Degen³

et al. 2001

Journal of Biological Chemistry

148

143

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Activated leukocyte cell adhesion molecule (ALCAM/ CD166), a member of the immunoglobulin superfamily with five extracellular immunoglobulin-like domains, facilitates heterophilic (ALCAM-CD6) and homophilic (ALCAM-ALCAM) cell-cell interactions. While expressed in a wide variety of tissues and cells, ALCAM is restricted to subsets of cells usually involved in dynamic growth and/or migration processes. A structure-function analysis, using two monoclonal anti-ALCAM antibodies and a series of amino-terminally deleted ALCAM constructs, revealed that homophilic cell adhesion depended on ligand binding mediated by the membranedistal amino-terminal immunoglobulin domain and on avidity controlled by ALCAM clustering at the cell surface involving membrane-proximal immunoglobulin domains. Co-expression of a transmembrane ALCAM deletion mutant, which lacks the ligand binding domain, and endogenous wild-type ALCAM inhibited homophilic cell-cell interactions by interference with ALCAM avidity, while homophilic, soluble ligand binding remained unaltered. The extracellular structures of ALCAM thus provide two structurally and functionally distinguishable modules, one involved in ligand binding and the other in avidity. Functionality of both modules is required for stable homophilic ALCAM-ALCAM cell-cell adhesion.Adhesion molecules play an important role in development, leukocyte function, and homeostasis in multicellular organisms, which are mainly governed by inter-and intracellular communication via cell-cell interactions. Alterations in cellular adhesion and communication can contribute to uncontrolled cell growth (1) and life-threatening syndromes like leukocyte adhesion deficiency (2). Activation of adhesion molecules generally involves both modulation of affinity and avidity. The affinity of adhesion molecules often reflects a specific conformation of the extracellular ligand-binding domain. Avidity modulation involves changes in the cell surface distribution of adhesion molecules (e.g. lateral oligomerization), which leads to clusters of molecules and thereby specifically increases the number of available receptors at the site of cell-cell interaction.Activated leukocyte cell adhesion molecule (ALCAM/MEMD/ CD166) 1 is a type I transmembrane protein and a member of the Ig superfamily. It has over 90% homology with the chicken adhesion molecule BEN/SC1/DM-GRASP (3-5), and it has 30% identity and 50% similarity with the human melanoma cell adhesion molecule Mel-CAM/MUC18/CD146 (6). Furthermore, ALCAM has 93% sequence identity with the candidate liver high density lipoprotein receptor HB2 (7). ALCAM is involved in various physiological processes including hematopoiesis (8, 9), thymus development (10), the immune response (11), neurite extension (12), neural cell migration (13), and osteogenesis (14).ALCAM has a short cytoplasmic tail and its extracellular part comprises five Ig domains: two amino-terminal variable (V) type Ig domains followed by three constant (C) type Ig domains (V 1 V 2 C 1 C 2 C 3 ). ALCAM was first ident...

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mentioning

confidence: 99%

Molecular Basis for the Homophilic Activated Leukocyte Cell Adhesion Molecule (ALCAM)-ALCAM Interaction

Kempen¹,

Nelissen²,

Degen³

et al. 2001

Journal of Biological Chemistry

148

143

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“…In accord with these observations, energy profile analysis suggested sequence-structure compatibility of the dimer. The bulge region sequences, hydrophobic residues, and charged residues implicated in dimer interactions are conserved in ALCAM's chicken homologue (Burns et al, 1991;Pourquie et al, 1992), suggesting the possibility of structural and/or functional relevance.…”

Section: J Bajorath Et Aimentioning

confidence: 99%

Molecular model of the N‐terminal receptor‐binding domain of the human CD6 ligand ALCAM

1995

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CD6-ligand interactions havebeen implicated in the regulation of T-cell adhesion and activation. CD6 is a member of the scavenger receptor family, whereas its human ligand (ALCAM) belongs to the immunoglobulin superfamily. The extracellular region of ALCAM includes five immunoglobulinlike domains. As a fusion protein, the N-terminal extracellular domain of ALCAM (ALCAMDl) binds specifically to CD6. We report the construction, assessment, and analysis of a molecular model of ALCAMDl. The model defines the CDR-analogous loops, the location of N-linked glycosylation sites, and residues that form the @-sheet faces of the immunoglobulin-like domain. Predicted structural characteristics of the A'GFCC'C" face of the model are consistent with the presence of monomeric and dimeric forms of ALCAMDI, which has implications for the receptor-ligand interactions.

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“…This molecule is identical to BEN and DM-GRASP, which were isolated separately by several research groups (4,5). SC1 is distinguished by an extracellular domain consisting of two V-type motifs following three C-2 type II Ig-like loops.…”

Section: Introductionmentioning

confidence: 96%

“…These adhesive properties of the SC1 protein are regulated by Ig-like loops modified by N-glycosylation in the extracellular domains. SC1 is transiently expressed during avian embryogenesis by a variety of cell types, and its expression is developmentally regulated in several cell types of the nervous and hematopoietic systems, as well as in certain epithelial cells (4,7,8).…”

Section: Introductionmentioning

confidence: 99%

Potential role of SC1, a cell adhesion molecule, in mammary gland tumors

Adachi¹,

Hagimori²,

Kato³

et al. 2008

Mol Med Report

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Abstract. SC1, an immunoglobulin superfamily cell adhesion molecule, is expressed in embryonic tissues and plays an important role in development through its cell adhesive activity. SC1 is also found in a variety of tumors and its expression is associated with a poor prognosis. The expressional patterns of SC1 were examined in sporadic cases of canine mammary gland tumors and it was found that this molecule is enriched in adenocarcinomas and is weaker in benign mixed tumors. SC1 might therefore be involved in the malignancy and progression of canine mammary gland tumors. To confirm this paradigm, the mammary gland cell line JYG-B was used as the recipient of SC1 cDNA. The resulting SC1-transfected cells were subsequently analyzed using a convenient in vitro model system. The self-aggregation activity of SC1-transfected cells was significantly increased and was blocked by an anti-SC1 antibody generated by hyper-immunized ostrich yolk. In addition, cell locomotion assays revealed an enhanced migration activity of SC1-transfected cells on SC1-coated transwell chambers. The in vivo activities of the cells were examined by subcutaneous implantation into nude mice. Tumor growth was significantly promoted in the mice after implantation with SC1-transfected cells, in comparison to parental-and mocktransfectants. This growth was inhibited by oral administration of gold-ion water. The invasion of SC1-transfectants into the surrounding muscular and adipose tissues was rigorously enhanced. These findings suggest that SC1 might promote the progression of mammary gland tumor cells by increasing cell adhesion.

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BEN, a surface glycoprotein of the immunoglobulin superfamily, is expressed in a variety of developing systems.

Cited by 111 publications

References 27 publications

Molecular Basis for the Homophilic Activated Leukocyte Cell Adhesion Molecule (ALCAM)-ALCAM Interaction

Molecular Basis for the Homophilic Activated Leukocyte Cell Adhesion Molecule (ALCAM)-ALCAM Interaction

Molecular model of the N‐terminal receptor‐binding domain of the human CD6 ligand ALCAM

Potential role of SC1, a cell adhesion molecule, in mammary gland tumors

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