scholarly journals Bcr-Abl induces abnormal cytoskeleton remodeling, beta1 integrin clustering and increased cell adhesion to fibronectin through the Abl interactor 1 pathway

2007 ◽  
Vol 120 (8) ◽  
pp. 1436-1446 ◽  
Author(s):  
Y. Li ◽  
N. Clough ◽  
X. Sun ◽  
W. Yu ◽  
B. L. Abbott ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Integrin Clustering ◽  
Cytoskeleton Remodeling ◽  
Beta1 Integrin

Endothelial-monocyte activating polypeptide II alters fibronectin based endothelial cell adhesion and matrix assembly via alpha5 beta1 integrin

2005 ◽  
Vol 311 (2) ◽  
pp. 229-239 ◽  
Author(s):  
Margaret A. Schwarz ◽  
Hiahua Zheng ◽  
Jie Liu ◽  
Siobhan Corbett ◽  
Roderich E. Schwarz
Keyword(s):  
Cell Adhesion ◽  
Endothelial Cell ◽  
Matrix Assembly ◽  
Beta1 Integrin ◽  
Endothelial Cell Adhesion

Laminin E8 alveolarization site: heparin sensitivity, cell surface receptors, and role in cell spreading

1997 ◽  
Vol 272 (3) ◽  
pp. L494-L503
Author(s):  
L. Chen ◽  
V. Shick ◽  
M. L. Matter ◽  
S. M. Laurie ◽  
R. C. Ogle ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Cell Surface ◽  
Surface Proteins ◽  
Cell Surface Proteins ◽  
Surface Receptors ◽  
Beta1 Integrin ◽  
Alpha Dystroglycan ◽  
Alveolar Formation ◽  
Laminin 1

Cell adhesion to amino acids 2179-2198 (SN-peptide) of the laminin-1 alpha1-chain is required for lung alveolar formation in vitro (M. L. Matter and G. W. Laurie. J. Cell Biol. 124: 1083-1090, 1994). The nature of the SN-peptide receptor(s) was probed with neutralizing anti-integrin monoclonal antibodies (MAb), cells lacking integrin subunits, soluble heparin, and SN-peptide columns. Cell adhesion and spreading studies confirmed the specificity of SN-peptide and revealed adhesion to be unaffected by inclusion of anti-beta1-, anti-alpha(2-6)- or anti-alpha(V)beta5-integrin MAb. Cells lacking beta1- or alpha6-integrin subunits were fully adherent. Adhesion was heparin, but not chondroitin sulfate or heparinase, sensitive, much as is alpha-dystroglycan-laminin-1 binding. Heparin eluted approximately 155- and 180-kDa cell-surface proteins from SN-peptide columns. An additional approximately 91-kDa protein was eluted by EDTA. All were unrecognized by anti-beta1-integrin MAb. SN-peptide therefore interacts with three cell-surface proteins for which the identity remains to be determined.

scholarly journals Aurora B spatially regulates EB3 phosphorylation to coordinate daughter cell adhesion with cytokinesis

2013 ◽  
Vol 201 (5) ◽  
pp. 709-724 ◽  
Author(s):  
Jorge G. Ferreira ◽  
António J. Pereira ◽  
Anna Akhmanova ◽  
Helder Maiato
Keyword(s):  
Cell Adhesion ◽  
Daughter Cell ◽  
Cortical Microtubule ◽  
Focal Adhesions ◽  
Mitotic Exit ◽  
Aurora B ◽  
Microtubule Stability ◽  
Spatiotemporal Regulation ◽  
Cytoskeleton Remodeling ◽  
Microtubule Growth

During mitosis, human cells round up, decreasing their adhesion to extracellular substrates. This must be quickly reestablished by poorly understood cytoskeleton remodeling mechanisms that prevent detachment from epithelia, while ensuring the successful completion of cytokinesis. Here we show that the microtubule end-binding (EB) proteins EB1 and EB3 play temporally distinct roles throughout cell division. Whereas EB1 was involved in spindle orientation before anaphase, EB3 was required for stabilization of focal adhesions and coordinated daughter cell spreading during mitotic exit. Additionally, EB3 promoted midbody microtubule stability and, consequently, midbody stabilization necessary for efficient cytokinesis. Importantly, daughter cell adhesion and cytokinesis completion were spatially regulated by distinct states of EB3 phosphorylation on serine 176 by Aurora B. This EB3 phosphorylation was enriched at the midbody and shown to control cortical microtubule growth. These findings uncover differential roles of EB proteins and explain the importance of an Aurora B phosphorylation gradient for the spatiotemporal regulation of microtubule function during mitotic exit and cytokinesis.

scholarly journals Increased extracellular pressure enhances cancer cell integrin-binding affinity through phosphorylation of β1-integrin at threonine 788/789

2009 ◽  
Vol 296 (1) ◽  
pp. C193-C204 ◽  
Author(s):  
David H. Craig ◽  
Christopher P. Gayer ◽  
Keri L. Schaubert ◽  
Yanzhang Wei ◽  
Jinhua Li ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Binding Affinity ◽  
Cancer Cell ◽  
Elevated Pressure ◽  
Colon Cancer Cells ◽  
Wild Type ◽  
Cancer Cell Adhesion ◽  
Integrin Clustering ◽  
Murine Fibroblasts

Increased extracellular pressure stimulates β1-integrin-dependent cancer cell adhesion. We asked whether pressure-induced adhesion is mediated by changes in β1-integrin binding affinity or avidity and whether these changes are phosphorylation dependent. We evaluated integrin affinity and clustering in human SW620 colon cancer cells by measuring differences in binding between soluble Arg-Gly-Asp (RGD)-Fc ligands and RGD-Fc-F(ab′)2 multimeric complexes under ambient and 15-mmHg increased pressures. Phosphorylation of β1-integrin S785 and T788/9 residues in SW620 and primary malignant colonocytes was assessed in parallel. We further used GD25-β1-integrin-null murine fibroblasts stably transfected with either wild-type β1A-integrin, S785A, TT788/9AA, or T788D mutants to investigate the role of β1-integrin site-specific phosphorylation. SW620 binding of RGD-Fc-F(ab′)2 multimeric complexes, but not soluble RGD-Fc ligands, was sensitive to integrin clustering. RGD-Fc ligand binding was significantly increased under elevated pressure, suggesting that pressure modulates β1-integrin affinity. Pressure stimulated both β1-integrin S785 and T788/9 phosphorylation. GD25-β1A-integrin wild-type and S785A cells displayed an increase in adhesion to fibronectin under elevated pressure, an effect absent in β1-integrin-null and TT788/9AA cells. T788D substitution significantly elevated basal cell adhesion but displayed no further increase under pressure. These results suggest pressure-induced cell adhesion is mediated by β1-integrin T788/9 phosphorylation-dependent changes in integrin binding affinity.

scholarly journals Transglutaminase-mediated oligomerization of the fibrin(ogen) αC domains promotes integrin-dependent cell adhesion and signaling

Blood ◽  
2005 ◽  
Vol 105 (9) ◽  
pp. 3561-3568 ◽  
Author(s):  
Alexey M. Belkin ◽  
Galina Tsurupa ◽  
Evgeny Zemskov ◽  
Yuri Veklich ◽  
John W. Weisel ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Cell Adhesion ◽  
Tissue Transglutaminase ◽  
Covalent Modification ◽  
Factor Xiiia ◽  
Cross Linking ◽  
Extracellular Signal ◽  
Integrin Clustering ◽  
Dependent Cell ◽  
Integrin Ligands

AbstractInteractions of endothelial cells with fibrin(ogen) are implicated in inflammation, angiogenesis, and wound healing. Cross-linking of the fibrinogen αC domains with factor XIIIa generates ordered αC oligomers mimicking polymeric arrangement of the αC domains in fibrin. These oligomers and those prepared with tissue transglutaminase were used to establish a mechanism of the αC domain–mediated interaction of fibrin with endothelial cells. Cell adhesion and chemical cross-linking experiments revealed that oligomerization of the αC domains by both transglutaminases significantly increases their RGD (arginyl–glycyl–aspartate)–dependent interaction with endothelial αVβ3 and to a lesser extent with αVβ5 and α5β1 integrins. The oligomerization promotes integrin clustering, thereby increasing cell adhesion, spreading, formation of prominent peripheral focal contacts, and integrin-mediated activation of focal adhesion kinase (FAK) and extracellular signal-regulated kinase (ERK) signaling pathways. The enhanced integrin clustering is likely caused by ordered juxtaposition of RGD-containing integrin-binding sites upon oligomerization of the αC domains and increased affinity of these domains for integrins. Our findings provide new insights into the mechanism of the αC domain–mediated interaction of endothelial cells with fibrin and imply its potential involvement in cell migration. They also suggest a new role for transglutaminases in regulation of integrin-mediated adhesion and signaling via covalent modification of integrin ligands.

scholarly journals Cell adhesion or integrin clustering increases phosphorylation of a focal adhesion-associated tyrosine kinase.

1992 ◽  
Vol 267 (33) ◽  
pp. 23439-23442 ◽  
Author(s):  
L Kornberg ◽  
H.S. Earp ◽  
J.T. Parsons ◽  
M Schaller ◽  
R.L. Juliano
Keyword(s):  
Cell Adhesion ◽  
Tyrosine Kinase ◽  
Focal Adhesion ◽  
Integrin Clustering
Sign in / Sign up

Export Citation Format

Share Document