scholarly journals Autocrine motility factor and the extracellular matrix. I. Coordinate regulation of melanoma cell adhesion, spreading and migration involves focal contact reorganization

1998 ◽  
Vol 76 (1) ◽  
pp. 120-128 ◽  
Author(s):  
Steve Silletti ◽  
Sandor Paku ◽  
Avraham Raz
Keyword(s):  
Extracellular Matrix ◽  
Cell Adhesion ◽  
Melanoma Cell ◽  
Focal Contact ◽  
Autocrine Motility Factor ◽  
Coordinate Regulation ◽  
Motility Factor ◽  
And Migration

Regulation of A375 melanoma cell adhesion and migration by EphB4 and EphrinB2 – insights from co-culture experiments

2019 ◽  
Vol 5 (1) ◽  
pp. 27-42
Author(s):  
Christin Neuber ◽  
Markus Laube ◽  
Constantin Mamat ◽  
Birgit Belter ◽  
Jens Pietzsch
Keyword(s):  
Cell Adhesion ◽  
Melanoma Cell ◽  
Cell Adhesion And Migration ◽  
And Migration ◽  
A375 Melanoma

scholarly journals Recreation of the terminal events in physiological integrin activation

2010 ◽  
Vol 188 (1) ◽  
pp. 157-173 ◽  
Author(s):  
Feng Ye ◽  
Guiqing Hu ◽  
Dianne Taylor ◽  
Boris Ratnikov ◽  
Andrey A. Bobkov ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Cell Adhesion ◽  
Integrin Signaling ◽  
Integrin Activation ◽  
Matrix Assembly ◽  
Integrin Αiibβ3 ◽  
Terminal Events ◽  
Cell Adhesion And Migration ◽  
And Migration

Increased affinity of integrins for the extracellular matrix (activation) regulates cell adhesion and migration, extracellular matrix assembly, and mechanotransduction. Major uncertainties concern the sufficiency of talin for activation, whether conformational change without clustering leads to activation, and whether mechanical force is required for molecular extension. Here, we reconstructed physiological integrin activation in vitro and used cellular, biochemical, biophysical, and ultrastructural analyses to show that talin binding is sufficient to activate integrin αIIbβ3. Furthermore, we synthesized nanodiscs, each bearing a single lipid-embedded integrin, and used them to show that talin activates unclustered integrins leading to molecular extension in the absence of force or other membrane proteins. Thus, we provide the first proof that talin binding is sufficient to activate and extend membrane-embedded integrin αIIbβ3, thereby resolving numerous controversies and enabling molecular analysis of reconstructed integrin signaling.

Binding of hexabrachion (tenascin) to the extracellular matrix and substratum and its effect on cell adhesion

1990 ◽  
Vol 95 (2) ◽  
pp. 263-277
Author(s):  
V.A. Lightner ◽  
H.P. Erickson
Keyword(s):  
Extracellular Matrix ◽  
Cell Adhesion ◽  
Cell Attachment ◽  
Solid Phase ◽  
Fluid Phase ◽  
Matrix Proteins ◽  
And Migration ◽  
Cover Up ◽  
Plastic Substratum

Hexabrachion is a large glycoprotein of the extracellular matrix (ECM) that is prominent in embryogenesis, wound healing and tumorigenesis. Because of the role of extracellular matrix proteins in the regulation of cell differentiation and migration, the interaction of hexabrachion with cells as well as with other components of the ECM is of great interest. Early reports suggested that hexabrachion does not bind to fibronectin or gelatin but does bind to chondroitin sulfate proteoglycans. However, more recent reports have suggested that hexabrachion binds to fibronectin and inhibits cell adhesion as well as cell migration on fibronectin. We have found no evidence of strong hexabrachion-fibronectin binding on either a solid-phase ELISA assay or in a fluid-phase sedimentation assay in which the reactants were allowed to dissociate. However, hexabrachion sedimentation was accelerated in a gradient containing fibronectin throughout. This demonstrates an association between hexabrachions and fibronectin, but the complex is apparently weak and readily reversible. The solid-phase ELISA also shows no evidence of hexabrachion binding to gelatin, laminin or types I, III, IV or V collagen. Hexabrachion does not support strong cell attachment of the cell lines tested. Moreover, hexabrachion can inhibit cell attachment to fibronectin. We demonstrate here that this inhibition requires the hexabrachion to be able to bind to the plastic substratum. The results suggest that hexabrachion inhibition is via a steric inhibition. When the hexabrachion molecules bind to the plastic, they cover up a significant fraction of the underlying fibronectin molecules. Antibody studies are presented that show that hexabrachion can nonspecifically block access of immunoglobulin G molecules to the underlying matrix. This steric blocking is not unique to hexabrachion.

Spatial and temporal expression of fibronecttns and integrins during Xenopus development

1992 ◽  
Vol 50 (1) ◽  
pp. 598-599
Author(s):  
Douglas W. DeSimone ◽  
M. Susan Dalton ◽  
Mark D. Hens ◽  
Bethanne Hill ◽  
Joe W. Ramos ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Cell Adhesion ◽  
Structure Function ◽  
Temporal Expression ◽  
Transmembrane Receptors ◽  
Cellular Processes ◽  
Basic Body ◽  
Cell Adhesion And Migration ◽  
Adhesive Interactions ◽  
And Migration

A central challenge in biology is to understand the cellular processes that direct morphogenesis and the formation of the basic body plan during development. These events are controlled to large extent, by adhesive interactions of cells with one another and with their extracellular environments. Specifically, we are investigating the structure, function and expression of two groups of molecules thought to play important roles in promoting cell adhesion and migration in the embryo: fibronectins (FNs), which are large extracellular matrix (ECM) glycoproteins with many adhesion related functions; and integrins, which are the cellular transmembrane-receptors for FNs and several other components of the ECM.

scholarly journals Hox Transcription Factors: Modulators of Cell-Cell and Cell-Extracellular Matrix Adhesion

2014 ◽  
Vol 2014 ◽  
pp. 1-12 ◽  
Author(s):  
Yasushi Taniguchi
Keyword(s):  
Extracellular Matrix ◽  
Transcription Factors ◽  
Cell Adhesion ◽  
Adhesion Molecules ◽  
Cell Adhesion Molecules ◽  
Cultured Cells ◽  
Hox Proteins ◽  
Cell Adhesion And Migration ◽  
And Migration ◽  
Cell Cell

Hoxgenes encode homeodomain-containing transcription factors that determine cell and tissue identities in the embryo during development.Hoxgenes are also expressed in various adult tissues and cancer cells. InDrosophila, expression of cell adhesion molecules, cadherins and integrins, is regulated by Hox proteins operating in hierarchical molecular pathways and plays a crucial role in segment-specific organogenesis. A number of studies using mammalian cultured cells have revealed that cell adhesion molecules responsible for cell-cell and cell-extracellular matrix interactions are downstream targets of Hox proteins. However, whether Hox transcription factors regulate expression of cell adhesion molecules during vertebrate development is still not fully understood. In this review, the potential roles Hox proteins play in cell adhesion and migration during vertebrate body patterning are discussed.

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