THE ISOLATION OF SURFACE COMPONENTS INVOLVED IN SPECIFIC CELL-CELL ADHESION AND CELLULAR RECOGNITION

1974 ◽  
pp. 509-528 ◽  
Author(s):  
Max M. Burger
Keyword(s):  
Cell Adhesion ◽  
Specific Cell ◽  
Cellular Recognition ◽  
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.

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