scholarly journals Multivalent Ligands: Integrin Clustering Matters: A Review of Biomaterials Functionalized with Multivalent Integrin-Binding Ligands to Improve Cell Adhesion, Migration, Differentiation, Angiogenesis, and Biomedical Device Integration (Adv. Healthcare Mate

2018 ◽  
Vol 7 (12) ◽  
pp. 1870048 ◽  
Author(s):  
Fatemeh Karimi ◽  
Andrea J. O'Connor ◽  
Greg G. Qiao ◽  
Daniel E. Heath
Keyword(s):  
Cell Adhesion ◽  
Multivalent Ligands ◽  
Biomedical Device ◽  
Device Integration ◽  
Integrin Clustering

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.

Reproducible and arbitrary patterning of transparent ZnO nanorod arrays for optic and biomedical device integration

2021 ◽  
pp. 163003
Author(s):  
Yuting Xiong ◽  
Minghe Fang ◽  
Qingfeng Zhang ◽  
Wenfei Liu ◽  
Xiaoshi Liu ◽  
...  
Keyword(s):  
Zno Nanorod ◽  
Nanorod Arrays ◽  
Zno Nanorod Arrays ◽  
Biomedical Device ◽  
Device Integration

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

scholarly journals Integrin Dimerization and Ligand Organization: Key Components in Integrin Clustering for Cell Adhesion

2005 ◽  
Vol 11 (5-6) ◽  
pp. 865-876 ◽  
Author(s):  
Christopher J. Brinkerhoff ◽  
Jennifer J. Linderman
Keyword(s):  
Cell Adhesion ◽  
Integrin Clustering

Substrate Stiffness as a Regulator in Catalyzing Integrin-Mediated Cell Adhesion Nucleation: A Mechanochemical Model

2013 ◽  
Vol 459 ◽  
pp. 555-559
Author(s):  
Xiao Ling Peng
Keyword(s):  
Cell Adhesion ◽  
Energy Input ◽  
Experimental Studies ◽  
Substrate Stiffness ◽  
Dependent Manner ◽  
Integrin Activation ◽  
A Value ◽  
Integrin Clustering ◽  
Mechanochemical Model

We provide here a simplified mechanochemical model to describe the role of substrate stiffness in mediating the chemical reactions between integrins on cell membrane and ligands immobilized on the substrate. By taking into account the energy input for integrin activation on a compliant substrate, Our simulation shows that integrin activation and the downstream integrin clustering can be regulated by substrate stiffness in a value-dependent manner, which is consistent with previous experimental studies.

scholarly journals The F1 loop of the talin head domain acts as a gatekeeper in integrin activation and clustering

2020 ◽  
Vol 133 (19) ◽  
pp. jcs239202 ◽  
Author(s):  
Sampo Kukkurainen ◽  
Latifeh Azizi ◽  
Pingfeng Zhang ◽  
Marie-Claude Jacquier ◽  
Mo Baikoghli ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Cytoplasmic Tail ◽  
First Person ◽  
Integrin Activation ◽  
Inner Membrane ◽  
Flexible Loop ◽  
Head Domain ◽  
Integrin Clustering ◽  
Membrane Bound ◽  
Β3 Integrin

ABSTRACTIntegrin activation and clustering by talin are early steps of cell adhesion. Membrane-bound talin head domain and kindlin bind to the β integrin cytoplasmic tail, cooperating to activate the heterodimeric integrin, and the talin head domain induces integrin clustering in the presence of Mn2+. Here we show that kindlin-1 can replace Mn2+ to mediate β3 integrin clustering induced by the talin head, but not that induced by the F2–F3 fragment of talin. Integrin clustering mediated by kindlin-1 and the talin head was lost upon deletion of the flexible loop within the talin head F1 subdomain. Further mutagenesis identified hydrophobic and acidic motifs in the F1 loop responsible for β3 integrin clustering. Modeling, computational and cysteine crosslinking studies showed direct and catalytic interactions of the acidic F1 loop motif with the juxtamembrane domains of α- and β3-integrins, in order to activate the β3 integrin heterodimer, further detailing the mechanism by which the talin–kindlin complex activates and clusters integrins. Moreover, the F1 loop interaction with the β3 integrin tail required the newly identified compact FERM fold of the talin head, which positions the F1 loop next to the inner membrane clasp of the talin-bound integrin heterodimer.This article has an associated First Person interview with the first author of the paper.

PI3K is involved in β1 integrin clustering by PSGL-1 and promotes β1 integrin-mediated Jurkat cell adhesion to fibronectin

2013 ◽  
Vol 385 (1-2) ◽  
pp. 287-295 ◽  
Author(s):  
Jixian Luo ◽  
Chunfeng Li ◽  
Tingshuang Xu ◽  
Wenai Liu ◽  
Xueqing Ba ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Jurkat Cell ◽  
Β1 Integrin ◽  
Integrin Clustering
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