Erythroid developmental agglutinin is a protein lectin mediating specific cell–cell adhesion between differentiating rabbit erythroblasts

Nature ◽  
1980 ◽  
Vol 286 (5772) ◽  
pp. 502-504 ◽  
Author(s):  
F. Lynne Harrison ◽  
C. James Chesterton
Keyword(s):  
Cell Adhesion ◽  
Specific Cell ◽  
Cell Cell

Folate receptor-specific cell-cell adhesion by using a folate-modified peptide-based anchor

2019 ◽  
Vol 30 (11) ◽  
pp. 983-993
Author(s):  
Hiroko Nagai ◽  
Wataru Hatanaka ◽  
Masayoshi Matsuda ◽  
Akihiro Kishimura ◽  
Yoshiki Katayama ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Folate Receptor ◽  
Specific Cell ◽  
Cell Cell

scholarly journals Molecular Expression of bone marrow angiogenic factors, cell-cell adhesion molecules and matrix-metallo-proteinase plasma cellular disorders: a molecular panel to investigate disease progression

2018 ◽  
Vol 10 ◽  
pp. e2018059
Author(s):  
Maria Cristina Rapanotti
Keyword(s):  
Multiple Myeloma ◽  
Cell Adhesion ◽  
Adhesion Molecules ◽  
Cell Adhesion Molecules ◽  
Plasma Cells ◽  
Angiogenic Factors ◽  
Specific Cell ◽  
Angiogenic Potential ◽  
E Cadherin ◽  
Cell Cell

Increasing levels of angiogenesis play an important role in the pathogenesis and progression of multiple myeloma (MM). Malignant plasma cells promote a gradual increase in the degree of angiogenesis, modulation of specific cell-cell adhesion molecules and secretion of matrix-metallo-proteinases (MMPs), changing the BM composition from benign conditions, such as MGUS, to smouldering multiple myeloma (SM) and to active MM. We aimed to identify a gene expression profile, helpful to discriminate the “angiogenic potential” in BM and PB plasma cells from MGUS, SMM and active MM patients analyzed at diagnosis. We analyzed the expression of cell-cell adhesion molecules such as VE-Cadherin, E-Cadherin MCAM/MUC18/CD146 and of the MMP-2 and MMP-9. MCAM/MUC18 expression resulted mostly associated with that of the pivotal angiogenic factors VEGF and Ang2, and in MGUS the pattern was different in steady state, compared to progression towards SM. Furthermore, E-Cadherin, the main epithelial cell-cell-adhesion molecule, unexpectedly resulted overexpressed in MM.                                                                                                                                                                                                                                                

Biological Tissue-Inspired Living Self-Healing Hydrogels Based on Cadherin-Mediated Specific Cell–Cell Adhesion

2021 ◽  
pp. 1073-1079
Author(s):  
Koji Nagahama ◽  
Seika Aoyama ◽  
Natsumi Ueda ◽  
Yuka Kimura ◽  
Tokitaka Katayama ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Biological Tissue ◽  
Specific Cell ◽  
Self Healing ◽  
Cell Cell

scholarly journals A-CAM: a 135-kD receptor of intercellular adherens junctions. II. Antibody-mediated modulation of junction formation.

1986 ◽  
Vol 103 (4) ◽  
pp. 1451-1464 ◽  
Author(s):  
T Volk ◽  
B Geiger
Keyword(s):  
Cell Adhesion ◽  
Adherens Junctions ◽  
Adherens Junction ◽  
Recovery Phase ◽  
Inhibitory Effect ◽  
Cell Junctions ◽  
Specific Cell ◽  
Normal Medium ◽  
Junction Formation ◽  
Cell Cell

Intercellular adherens junctions between cultured lens epithelial cells are highly Ca2+-dependent and are readily dissociated upon chelation of extracellular Ca2+ ions. Addition of Ca2+ to EGTA-treated cells results in the recovery of cell-cell junctions including the reorganization of adherens junction-specific cell adhesion molecule (A-CAM), vinculin, and actin (Volk, T., and B. Geiger, 1986, J. Cell Biol., 103:000-000). Incubation of cells during the recovery phase with Fab' fragments of anti-A-CAM specifically inhibited the re-formation of cell-cell adherens junctions. This inhibition was accompanied by remarkable changes in microfilament organization manifested by an apparent deterioration of stress fibers and the appearance of fragmented actin bundles throughout the cytoplasm. Incubation of EGTA-dissociated cells with intact divalent anti-A-CAM antibodies in normal medium had no apparent inhibitory effect on junction formation and did not affect the assembly of actin microfilament bundles. Moreover, adherens junctions formed in the presence of the divalent antibodies became essentially Ca2+-independent, suggesting that cell-cell adhesion between them was primarily mediated by the antibodies. These studies suggest that A-CAM participates in intercellular adhesion in adherens-type junctions and point to its involvement in microfilament bundle assembly.

scholarly journals Involvement of cell surface phosphatidylinositol-anchored glycoproteins in cell-cell adhesion of chick embryo myoblasts.

1989 ◽  
Vol 109 (4) ◽  
pp. 1779-1786 ◽  
Author(s):  
K A Knudsen ◽  
L Smith ◽  
S McElwee
Keyword(s):  
Cell Adhesion ◽  
Cell Surface ◽  
Phospholipase C ◽  
Polyclonal Antiserum ◽  
Soluble Form ◽  
Specific Cell ◽  
Myotube Formation ◽  
Specific Proteins ◽  
Fusion Competent Myoblasts ◽  
Cell Cell

During myogenesis myoblasts fuse to form multinucleate cells that express muscle-specific proteins. A specific cell-cell adhesion process precedes lipid bilayer union during myoblast fusion (Knudsen, K. A., and A. F. Horwitz. 1977. Dev. Biol. 58:328-338) and is mediated by cell surface glycoproteins (Knudsen, K. A., 1985. J. Cell Biol. 101:891-897). In this paper we show that myoblast adhesion and myotube formation are inhibited by treating fusion-competent myoblasts with phosphatidylinositol-specific phospholipase C (PI-PLC). The effect of PI-PLC on myoblast adhesion is dose dependent and inhibited by D-myo-inositol 1-monophosphate and the effect on myotube formation is reversible, suggesting a specific, nontoxic effect on myogenesis by the enzyme. A soluble form of adhesion-related glycoproteins is released from fusion-competent myoblasts by treatment with PI-PLC as evidenced by (a) the ability of phospholipase C (PLC)-released material to block the adhesion-perturbing activity of a polyclonal antiserum to intact myoblasts; and (b) the ability of PLC-released glycoprotein to stimulate adhesion-perturbing antisera when injected into mice. PI-PLC treatment of fusion-competent myoblasts releases an isoform of N-CAM into the supernate, suggesting that N-CAM may participate in mediating myoblast interaction during myogenesis.

scholarly journals E-cadherin represses anchorage-independent growth in sarcomas through both signaling and mechanical mechanisms

2018 ◽  
Author(s):  
Mohit Kumar Jolly ◽  
Kathryn E Ware ◽  
Shengnan Xu ◽  
Shivee Gilja ◽  
Samantha Shetler ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Intracellular Signaling ◽  
Epithelial Mesenchymal Transition ◽  
Migration And Invasion ◽  
Specific Cell ◽  
Mesenchymal Transition ◽  
Anchorage Independent Growth ◽  
Sarcoma Cells ◽  
E Cadherin ◽  
Cell Cell

E-cadherin, an epithelial-specific cell-cell adhesion molecule, plays multiple roles in maintaining adherens junctions, regulating migration and invasion, and mediating intracellular signaling. Downregulation of E-cadherin is a hallmark of epithelial-mesenchymal transition (EMT) and correlates with poor prognosis in multiple carcinomas. Conversely, upregulation of E-cadherin is prognostic for improved survival in sarcomas. Yet, despite the prognostic benefit of E-cadherin expression in sarcoma, the mechanistic significance of E-cadherin in sarcomas remains poorly understood. Here, by combining mathematical models with wet-bench experiments, we identify the core regulatory networks mediated by E-cadherin in sarcomas, and decipher their functional consequences. Unlike in carcinomas, E-cadherin overexpression in sarcomas does not induce a mesenchymal-epithelial transition (MET). However, E-cadherin acts to reduce both anchorage-independent growth and spheroid formation of sarcoma cells. Ectopic E-cadherin expression acts to downregulate phosphorylated CREB (p-CREB) and the transcription factor, TBX2, to inhibit anchorage-independent growth. RNAi-mediated knockdown of TBX2 phenocopies the effect of E-cadherin on p-CREB levels and restores sensitivity to anchorage-independent growth in sarcoma cells. Beyond its signaling role, E-cadherin expression in sarcoma cells can also strengthen cell-cell adhesion and restricts spheroid growth through mechanical action. Together, our results demonstrate that E-cadherin inhibits sarcoma aggressiveness by preventing anchorage-independent growth.

scholarly journals Cytoplasmic Tail Regulates the Intercellular Adhesion Function of the Epithelial Cell Adhesion Molecule

1998 ◽  
Vol 18 (8) ◽  
pp. 4833-4843 ◽  
Author(s):  
Maarten Balzar ◽  
Hellen A. M. Bakker ◽  
Inge H. Briaire-de-Bruijn ◽  
Gert Jan Fleuren ◽  
Sven O. Warnaar ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Adhesion Molecule ◽  
Cell Adhesion Molecule ◽  
Solid Phase ◽  
Cytoplasmic Tail ◽  
Cytoplasmic Domain ◽  
Specific Cell ◽  
Actin Microfilaments ◽  
Intercellular Adhesions ◽  
Cell Cell

ABSTRACT Ep-CAM, an epithelium-specific cell-cell adhesion molecule (CAM) not structurally related to the major families of CAMs, contains a cytoplasmic domain of 26 amino acids. The chemical disruption of the actin microfilaments, but not of the microtubuli or intermediate filaments, affected the localization of Ep-CAM at the cell-cell boundaries, suggesting that the molecule interacts with the actin-based cytoskeleton. Mutated forms of Ep-CAM were generated with the cytoplasmic domain truncated at various lengths. All of the mutants were transported to the cell surface in the transfectants; however, the mutant lacking the complete cytoplasmic domain was not able to localize to the cell-cell boundaries, in contrast to mutants with partial deletions. Both the disruption of the actin microfilaments and a complete truncation of the cytoplasmic tail strongly affected the ability of Ep-CAM to mediate aggregation of L cells. The capability of direct aggregation was reduced for the partially truncated mutants but remained cytochalasin D sensitive. The tail truncation did not affect the ability of the transfectants to adhere to solid-phase-adsorbed Ep-CAM, suggesting that the ability to form stable adhesions and not the ligand specificity of the molecule was affected by the truncation. The formation of intercellular adhesions mediated by Ep-CAM induced a redistribution to the cell-cell boundaries of α-actinin, but not of vinculin, talin, filamin, spectrin, or catenins. Coprecipitation demonstrated direct association of Ep-CAM with α-actinin. Binding of α-actinin to purified mutated and wild-type Ep-CAMs and to peptides representing different domains of the cytoplasmic tail of Ep-CAM demonstrates two binding sites for α-actinin at positions 289 to 296 and 304 to 314 of the amino acid sequence. The results demonstrate that the cytoplasmic domain of Ep-CAM regulates the adhesion function of the molecule through interaction with the actin cytoskeleton via α-actinin.

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