scholarly journals hepaCAM, a novel immunoglobulin‐like cell adhesion molecule, is associated with the actin cytoskeleton and the lipid rafts and is involved in cell‐matrix interaction

2006 ◽  
Vol 20 (5) ◽  
Author(s):  
Mei Chung Moh ◽  
Shali Shen
Keyword(s):  
Cell Adhesion ◽  
Actin Cytoskeleton ◽  
Lipid Rafts ◽  
Adhesion Molecule ◽  
Cell Adhesion Molecule ◽  
Matrix Interaction ◽  
Cell Matrix

Vascular-endothelial-cadherin modulates endothelial monolayer permeability

1999 ◽  
Vol 112 (12) ◽  
pp. 1915-1923 ◽  
Author(s):  
P.L. Hordijk ◽  
E. Anthony ◽  
F.P. Mul ◽  
R. Rientsma ◽  
L.C. Oomen ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Actin Cytoskeleton ◽  
Adhesion Molecule ◽  
Cell Adhesion Molecule ◽  
Transendothelial Migration ◽  
Stress Fibers ◽  
Vascular Endothelial ◽  
Monolayer Permeability ◽  
Actin Stress Fibers ◽  
Cell Cell

Vascular endothelial (VE)-cadherin is the endothelium-specific member of the cadherin family of homotypic cell adhesion molecules. VE-cadherin, but not the cell adhesion molecule platelet/endothelial cell adhesion molecule (PECAM-1), markedly colocalizes with actin stress fibers at cell-cell junctions between human umbilical vein endothelial cells. Inhibition of VE-cadherin-mediated, but not PECAM-1-mediated, adhesion induced reorganization of the actin cytoskeleton, loss of junctional VE-cadherin staining and loss of cell-cell adhesion. In functional assays, inhibition of VE-cadherin caused increased monolayer permeability and enhanced neutrophil transendothelial migration. In a complementary set of experiments, modulation of the actin cytoskeleton was found to strongly affect VE-cadherin distribution. Brief stimulation of the beta2-adrenergic receptor with isoproterenol induced a loss of actin stress fibers resulting in a linear, rather than ‘jagged’, VE-cadherin distribution. The concomitant, isoproterenol-induced, reduction in monolayer permeability was alleviated by a VE-cadherin-blocking antibody. Finally, cytoskeletal reorganization resulting from the inactivation of p21Rho caused a diffuse localization of VE-cadherin, which was accompanied by reduced cell-cell adhesion. Together, these data show that monolayer permeability and neutrophil transendothelial migration are modulated by VE-cadherin-mediated cell-cell adhesion, which is in turn controlled by the dynamics of the actin cytoskeleton.

scholarly journals Involvement of Gangliosides in Glycosylphosphatidylinositol-anchored Neuronal Cell Adhesion Molecule TAG-1 Signaling in Lipid Rafts

2000 ◽  
Vol 275 (44) ◽  
pp. 34701-34709 ◽  
Author(s):  
Kohji Kasahara ◽  
Kazutada Watanabe ◽  
Kosei Takeuchi ◽  
Harumi Kaneko ◽  
Atsuhiko Oohira ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Lipid Rafts ◽  
Adhesion Molecule ◽  
Cell Adhesion Molecule ◽  
Neuronal Cell ◽  
Neuronal Cell Adhesion Molecule

scholarly journals Asymmetric distribution of Echinoid defines the epidermal leading edge during Drosophila dorsal closure

2011 ◽  
Vol 192 (2) ◽  
pp. 335-348 ◽  
Author(s):  
Caroline Laplante ◽  
Laura A. Nilson
Keyword(s):  
Drosophila Melanogaster ◽  
Cell Adhesion ◽  
Actin Cytoskeleton ◽  
Adhesion Molecule ◽  
Cell Adhesion Molecule ◽  
Leading Edge ◽  
Scaffolding Protein ◽  
Asymmetric Distribution ◽  
Dorsal Closure ◽  
Dorsal Midline

During Drosophila melanogaster dorsal closure, lateral sheets of embryonic epidermis assemble an actomyosin cable at their leading edge and migrate dorsally over the amnioserosa, converging at the dorsal midline. We show that disappearance of the homophilic cell adhesion molecule Echinoid (Ed) from the amnioserosa just before dorsal closure eliminates homophilic interactions with the adjacent dorsal-most epidermal (DME) cells, which comprise the leading edge. The resulting planar polarized distribution of Ed in the DME cells is essential for the localized accumulation of actin regulators and for actomyosin cable formation at the leading edge and for the polarized localization of the scaffolding protein Bazooka/PAR-3. DME cells with uniform Ed fail to assemble a cable and protrude dorsally, suggesting that the cable restricts dorsal migration. The planar polarized distribution of Ed in the DME cells thus provides a spatial cue that polarizes the DME cell actin cytoskeleton, defining the epidermal leading edge and establishing its contractile properties.

scholarly journals Ethanol causes the redistribution of L1 cell adhesion molecule in lipid rafts

2011 ◽  
Vol 119 (4) ◽  
pp. 859-867 ◽  
Author(s):  
Ningfeng Tang ◽  
Benjamin Farah ◽  
Min He ◽  
Stephanie Fox ◽  
Alfred Malouf ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Lipid Rafts ◽  
Adhesion Molecule ◽  
Cell Adhesion Molecule ◽  
L1 Cell Adhesion Molecule

scholarly journals Neural cell adhesion molecule (NCAM) association with PKCβ2 via βI spectrin is implicated in NCAM-mediated neurite outgrowth

2003 ◽  
Vol 161 (3) ◽  
pp. 625-639 ◽  
Author(s):  
Iryna Leshchyns'ka ◽  
Vladimir Sytnyk ◽  
Jon S. Morrow ◽  
Melitta Schachner
Keyword(s):  
Cell Adhesion ◽  
Neurite Outgrowth ◽  
Lipid Rafts ◽  
Adhesion Molecule ◽  
Hippocampal Neurons ◽  
Cell Adhesion Molecule ◽  
Neural Cell Adhesion Molecule ◽  
Neural Cell ◽  
Dominant Negative ◽  
Neural Cell Adhesion

In hippocampal neurons and transfected CHO cells, neural cell adhesion molecule (NCAM) 120, NCAM140, and NCAM180 form Triton X-100–insoluble complexes with βI spectrin. Heteromeric spectrin (αIβI) binds to the intracellular domain of NCAM180, and isolated spectrin subunits bind to both NCAM180 and NCAM140, as does the βI spectrin fragment encompassing second and third spectrin repeats (βI2–3). In NCAM120-transfected cells, βI spectrin is detectable predominantly in lipid rafts. Treatment of cells with methyl-β-cyclodextrin disrupts the NCAM120–spectrin complex, implicating lipid rafts as a platform linking NCAM120 and spectrin. NCAM140/NCAM180–βI spectrin complexes do not depend on raft integrity and are located both in rafts and raft-free membrane domains. PKCβ2 forms detergent-insoluble complexes with NCAM140/NCAM180 and spectrin. Activation of NCAM enhances the formation of NCAM140/NCAM180–spectrin–PKCβ2 complexes and results in their redistribution to lipid rafts. The complex is disrupted by the expression of dominant-negative βI2–3, which impairs binding of spectrin to NCAM, implicating spectrin as the bridge between PKCβ2 and NCAM140 or NCAM180. Redistribution of PKCβ2 to NCAM–spectrin complexes is also blocked by a specific fibroblast growth factor receptor inhibitor. Furthermore, transfection with βI2–3 inhibits NCAM-induced neurite outgrowth, showing that formation of the NCAM–spectrin–PKCβ2 complex is necessary for NCAM-mediated neurite outgrowth.

scholarly journals Syntenin-1 and Ezrin Proteins Link Activated Leukocyte Cell Adhesion Molecule to the Actin Cytoskeleton

2014 ◽  
Vol 289 (19) ◽  
pp. 13445-13460 ◽  
Author(s):  
Cicerone Tudor ◽  
Joost te Riet ◽  
Christina Eich ◽  
Rolf Harkes ◽  
Nick Smisdom ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Actin Cytoskeleton ◽  
Adhesion Molecule ◽  
Cell Adhesion Molecule
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