scholarly journals RGD-independent Cell Adhesion via a Tissue Transglutaminase-Fibronectin Matrix Promotes Fibronectin Fibril Deposition and Requires Syndecan-4/2 and α5β1 Integrin Co-signaling

2010 ◽  
Vol 285 (51) ◽  
pp. 40212-40229 ◽  
Author(s):  
Zhuo Wang ◽  
Russell J. Collighan ◽  
Stephane R. Gross ◽  
Erik H. J. Danen ◽  
Gertraud Orend ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Tissue Transglutaminase ◽  
Fibronectin Matrix ◽  
Α5β1 Integrin

scholarly journals A Novel RGD-independent Cell Adhesion Pathway Mediated by Fibronectin-bound Tissue Transglutaminase Rescues Cells from Anoikis

2003 ◽  
Vol 278 (43) ◽  
pp. 42604-42614 ◽  
Author(s):  
Elisabetta A. M. Verderio ◽  
Dilek Telci ◽  
Afam Okoye ◽  
Gerry Melino ◽  
Martin Griffin
Keyword(s):  
Cell Adhesion ◽  
Tissue Transglutaminase

scholarly journals Mena binds α5 integrin directly and modulates α5β1 function

2012 ◽  
Vol 198 (4) ◽  
pp. 657-676 ◽  
Author(s):  
Stephanie L. Gupton ◽  
Daisy Riquelme ◽  
Shannon K. Hughes-Alford ◽  
Jenny Tadros ◽  
Shireen S. Rudina ◽  
...  
Keyword(s):  
Cell Migration ◽  
Cell Adhesion ◽  
Growth Factor Receptor ◽  
Focal Adhesions ◽  
Fibronectin Receptor ◽  
Focal Adhesion Proteins ◽  
Carboxy Terminal ◽  
Bidirectional Interactions ◽  
Dependent Processes ◽  
Α5β1 Integrin

Mena is an Ena/VASP family actin regulator with roles in cell migration, chemotaxis, cell–cell adhesion, tumor cell invasion, and metastasis. Although enriched in focal adhesions, Mena has no established function within these structures. We find that Mena forms an adhesion-regulated complex with α5β1 integrin, a fibronectin receptor involved in cell adhesion, motility, fibronectin fibrillogenesis, signaling, and growth factor receptor trafficking. Mena bound directly to the carboxy-terminal portion of the α5 cytoplasmic tail via a 91-residue region containing 13 five-residue “LERER” repeats. In fibroblasts, the Mena–α5 complex was required for “outside-in” α5β1 functions, including normal phosphorylation of FAK and paxillin and formation of fibrillar adhesions. It also supported fibrillogenesis and cell spreading and controlled cell migration speed. Thus, fibroblasts require Mena for multiple α5β1-dependent processes involving bidirectional interactions between the extracellular matrix and cytoplasmic focal adhesion proteins.

Fibronectin Distribution in Human Bone Marrow Stroma: Matrix Assembly and Tumor Cell Adhesion via α5β1 Integrin

1997 ◽  
Vol 230 (1) ◽  
pp. 111-120 ◽  
Author(s):  
D. Van der Velde-Zimmermann ◽  
M.A.M. Verdaasdonk ◽  
L.H.P.M. Rademakers ◽  
R.A. De Weger ◽  
J.G. Van den Tweel ◽  
...  
Keyword(s):  
Bone Marrow ◽  
Cell Adhesion ◽  
Tumor Cell ◽  
Human Bone ◽  
Human Bone Marrow ◽  
Bone Marrow Stroma ◽  
Matrix Assembly ◽  
Tumor Cell Adhesion ◽  
Marrow Stroma ◽  
Α5β1 Integrin

EFFECT OF GROWTH FACTOR-FIBRONECTIN MATRIX INTERACTION ON RAT TYPE II CELL ADHESION AND DNA SYNTHESIS

2002 ◽  
Vol 28 (2) ◽  
pp. 69-84 ◽  
Author(s):  
Ines Pagan ◽  
Jody Khosla ◽  
Cheng-Ming Li ◽  
Philip L. Sannes
Keyword(s):  
Cell Adhesion ◽  
Growth Factor ◽  
Dna Synthesis ◽  
Type Ii ◽  
Matrix Interaction ◽  
Fibronectin Matrix ◽  
Type Ii Cell

scholarly journals Fibronectin-mediated upregulation of α5β1 integrin and cell adhesion during differentiation of mouse embryonic stem cells

2011 ◽  
Vol 5 (1) ◽  
pp. 73-82 ◽  
Author(s):  
Pimchanok Pimton ◽  
Saheli Sarkar ◽  
Nidhi Sheth ◽  
Anat Perets ◽  
Cezary Marcinkiewicz ◽  
...  
Keyword(s):  
Stem Cells ◽  
Cell Adhesion ◽  
Embryonic Stem Cells ◽  
Embryonic Stem ◽  
Mouse Embryonic Stem Cells ◽  
Α5β1 Integrin

Localization of BCR-ABL to F-actin regulates cell adhesion but does not attenuate CML development

Blood ◽  
2003 ◽  
Vol 102 (6) ◽  
pp. 2220-2228 ◽  
Author(s):  
Jason A. Wertheim ◽  
Samanthi A. Perera ◽  
Daniel A. Hammer ◽  
Ruibao Ren ◽  
David Boettiger ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Function Analysis ◽  
Coiled Coil ◽  
Myelogenous Leukemia ◽  
Actin Binding ◽  
Murine Bone Marrow ◽  
Actin Binding Domain ◽  
Transplantation Assay ◽  
Α5β1 Integrin ◽  
Actin Localization

Abstract We have previously found that P210BCR-ABL increases the adhesion of hematopoietic cell lines to fibronectin by a mechanism that is independent of tyrosine kinase activity. To investigate the pathway(s) by which P210BCR-ABL influences cell adhesion, we used a quantitative cell adhesion device that can discern small changes in cell adhesion to assay P210BCR-ABL with mutations in several critical domains. We expressed P210BCR-ABL mutants in 32D myeloblast cells and found that binding to fibronectin is mediated primarily by the α5β1 integrin. We performed a structure/function analysis to map domains important for cell adhesion. Increased adhesion was mediated by 3 domains: (1) the N-terminal coiled-coil domain that facilitates oligomerization and F-actin localization; (2) bcr sequences between aa 163 to 210; and (3) F-actin localization through the C-terminal actin-binding domain of c-abl. We compared our adhesion results with the ability of these mutants to cause a chronic myelogenous leukemia (CML)–like disease in a murine bone marrow transplantation assay and found that adhesion to fibronectin did not correlate with the ability of these mutants to cause CML. Together, our results suggest that F-actin localization may play a pivotal role in modulating adhesion but that it is dispensable for the development of CML.

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.

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