scholarly journals Regulation of epithelial cell organization by tuning cell–substrate adhesion

2015 ◽  
Vol 7 (10) ◽  
pp. 1228-1241 ◽  
Author(s):  
Andrea Ravasio ◽  
Anh Phuong Le ◽  
Thuan Beng Saw ◽  
Victoria Tarle ◽  
Hui Ting Ong ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Live Cell Imaging ◽  
Cell Imaging ◽  
Particle Image ◽  
Substrate Adhesion ◽  
Cell Substrate ◽  
Image Velocimetry ◽  
Cell Organization ◽  
Cell Substrate Adhesion

Combining live cell imaging, particle image velocimetry and numerical simulations, we show the role of extracellular matrix and intercellular adhesion on the expansion of epithelial cells.

Integrin-Mediated Fibroblast Adhesion Strength: Role of the β1 Subunit

1993 ◽  
Vol 331 ◽  
Author(s):  
Kelly A. Ward ◽  
Jun-Lin Guan ◽  
Daniel A. Hammer
Keyword(s):  
Extracellular Matrix ◽  
Adhesion Strength ◽  
Cytoplasmic Domain ◽  
Integrin Receptors ◽  
Substrate Adhesion ◽  
Focal Contacts ◽  
Cell Substrate ◽  
Extracellular Matrix Molecules ◽  
Integrin Ligand ◽  
Cell Substrate Adhesion

AbstractCell-substratum adhesion is important in wound healing [4], embryogenic development [11], tissue architecture [6], and metastasis [7]. Integrins constitute a major class of heterodimeric cell-surface glycoproteins involved in receptor-mediated adhesion to the extracellular matrix (ECM). Focal contacts are regions of the cell-substratum adhesion in which clusters of integrin receptors connect the cytoskeleton to extracellular matrix molecules such as fibronectin. Focal contacts strengthen cell-substrate adhesion, and are sites of biochemical activity. Since cell adhesion strength in part depends on the cell's ability to cluster receptors and cytoskeleton into focal contacts, the integrity of the focal contact, and hence a cell's adhesive strength, will depend both on integrin-cytoskeletal binding as well as integrin-ligand binding.Using a centrifugation assay, we have quantified cell-substratum adhesion strength of mouse 3T3 cells transfected with the avian β1 integrin receptor (wild type), including various deletion mutants of its cytoplasmic domain, to surfaces containing varying concentrations of CSAT, a monoclonal antibody against the extracellular domain of the avian β1 subunit. For all the transfectants, adhesion strength decreases with decreasing CSAT concentration and increasing centrifugal strength. Different truncations of the cytoplasmic domain lead to different levels of adhesion. There is no simple correlation between the length of the cytoplasmic domain and the strength of adhesion.

scholarly journals The crosstalk between microtubules, actin and membranes shapes cell division

Open Biology ◽  
2020 ◽  
Vol 10 (3) ◽  
pp. 190314 ◽  
Author(s):  
Francesca Rizzelli ◽  
Maria Grazia Malabarba ◽  
Sara Sigismund ◽  
Marina Mapelli
Keyword(s):  
Membrane Trafficking ◽  
Mitotic Progression ◽  
Isolated Cells ◽  
Spindle Positioning ◽  
Substrate Adhesion ◽  
Cell Substrate ◽  
Epithelial Sheets ◽  
Cell Substrate Adhesion ◽  
Extracellular Signalling

Mitotic progression is orchestrated by morphological and mechanical changes promoted by the coordinated activities of the microtubule (MT) cytoskeleton, the actin cytoskeleton and the plasma membrane (PM). MTs assemble the mitotic spindle, which assists sister chromatid separation, and contact the rigid and tensile actomyosin cortex rounded-up underneath the PM. Here, we highlight the dynamic crosstalk between MTs, actin and cell membranes during mitosis, and discuss the molecular connections between them. We also summarize recent views on how MT traction forces, the actomyosin cortex and membrane trafficking contribute to spindle positioning in isolated cells in culture and in epithelial sheets. Finally, we describe the emerging role of membrane trafficking in synchronizing actomyosin tension and cell shape changes with cell–substrate adhesion, cell–cell contacts and extracellular signalling events regulating proliferation.

scholarly journals The Role of Mitotic Cell-Substrate Adhesion Re-modeling in Animal Cell Division

2018 ◽  
Vol 45 (1) ◽  
pp. 132-145.e3 ◽  
Author(s):  
Christina L. Dix ◽  
Helen K. Matthews ◽  
Marina Uroz ◽  
Susannah McLaren ◽  
Lucie Wolf ◽  
...  
Keyword(s):  
Cell Division ◽  
Animal Cell ◽  
Mitotic Cell ◽  
Substrate Adhesion ◽  
Cell Substrate ◽  
Cell Substrate Adhesion

Formins and VASPs may co-operate in the formation of filopodia

2005 ◽  
Vol 33 (6) ◽  
pp. 1256-1259 ◽  
Author(s):  
A. Schirenbeck ◽  
R. Arasada ◽  
T. Bretschneider ◽  
M. Schleicher ◽  
J. Faix
Keyword(s):  
Actin Filaments ◽  
Actin Polymerization ◽  
Cell Types ◽  
Binding Partner ◽  
Substrate Adhesion ◽  
Cell Substrate ◽  
Dynamic Structures ◽  
Parallel Arrays ◽  
Cell Substrate Adhesion

Filopodia are finger-like cell protrusions composed of parallel arrays of actin filaments, which elongate through actin polymerization at their tips. These highly dynamic structures seem to be used by many cell types as sensing organs to explore environmental cues and have been implicated in cell motility as well as in cell–substrate adhesion. Formins are highly conserved multidomain proteins that play important roles in the nucleation of actin and the formation of linear actin filaments, yet their role in filopodia formation has remained poorly defined. The Dictyostelium diaphanous-related formin dDia2 is strongly enriched in filopodia tips. Genetic and biochemical analysis revealed that this protein is important for cell migration and cell adhesion, but most importantly for the formation of filopodia. Recently, we have identified the Dictyostelium VASP (vasodilator-stimulated phosphoprotein) orthologue as a binding partner of dDia2 and provide evidence for a co-operative role of both proteins in filopodia formation.

scholarly journals The Janus Role of Adhesion in Chondrogenesis

2020 ◽  
Vol 21 (15) ◽  
pp. 5269 ◽  
Author(s):  
Ignasi Casanellas ◽  
Anna Lagunas ◽  
Yolanda Vida ◽  
Ezequiel Pérez-Inestrosa ◽  
José A. Andrades ◽  
...  
Keyword(s):  
Cell Tracking ◽  
Tissue Adhesive ◽  
Pcr Analysis ◽  
Condensation Process ◽  
Local Surface ◽  
Substrate Adhesion ◽  
Cell Substrate ◽  
Cell Substrate Adhesion ◽  
Fluorescence Live Cell Imaging

Tackling the first stages of the chondrogenic commitment is essential to drive chondrogenic differentiation to healthy hyaline cartilage and minimize hypertrophy. During chondrogenesis, the extracellular matrix continuously evolves, adapting to the tissue adhesive requirements at each stage. Here, we take advantage of previously developed nanopatterns, in which local surface adhesiveness can be precisely tuned, to investigate its effects on prechondrogenic condensation. Fluorescence live cell imaging, immunostaining, confocal microscopy and PCR analysis are used to follow the condensation process on the nanopatterns. Cell tracking parameters, condensate morphology, cell–cell interactions, mechanotransduction and chondrogenic commitment are evaluated in response to local surface adhesiveness. Results show that only condensates on the nanopatterns of high local surface adhesiveness are stable in culture and able to enter the chondrogenic pathway, thus highlighting the importance of controlling cell–substrate adhesion in the tissue engineering strategies for cartilage repair.

scholarly journals Correlation of in vitro cell adhesion, local shear flow and cell density

RSC Advances ◽  
2019 ◽  
Vol 9 (1) ◽  
pp. 543-551
Author(s):  
A. M. Jötten ◽  
S. Angermann ◽  
M. E. M. Stamp ◽  
D. Breyer ◽  
F. G. Strobl ◽  
...  
Keyword(s):  
Particle Image Velocimetry ◽  
Cell Density ◽  
Live Cell Imaging ◽  
Cell Imaging ◽  
Particle Image ◽  
Microfluidic Chamber ◽  
Image Velocimetry ◽  
Local Shear ◽  
Geometrical Effects

By combination of particle image velocimetry and live cell imaging in an acoustically driven microfluidic chamber, we study shear and cell density dependent adhesion. We find excellent agreement with simulations considering pure geometrical effects.

scholarly journals Functional mapping of cytotactin: proteolytic fragments active in cell-substrate adhesion.

1988 ◽  
Vol 107 (6) ◽  
pp. 2329-2340 ◽  
Author(s):  
D R Friedlander ◽  
S Hoffman ◽  
G M Edelman
Keyword(s):  
Extracellular Matrix ◽  
Polyclonal Antibody ◽  
Limited Proteolysis ◽  
Cell Binding ◽  
Fab Fragments ◽  
Substrate Adhesion ◽  
Cell Substrate ◽  
A Cell ◽  
Fraction I ◽  
Cell Substrate Adhesion

Cytotactin is an extracellular matrix glycoprotein with a restricted distribution during development. In electron microscopic images, it appears as a hexabrachion with six arms extending from a central core. Cytotactin binds to other extracellular matrix proteins including a chondroitin sulfate proteoglycan (CTB proteoglycan) and fibronectin. Although cytotactin binds to a variety of cells including fibroblasts and neurons, in some cases it causes cells in culture to round up and it inhibits their migration. To relate these various effects of cytotactin on cell behavior to its binding regions, we have examined its ability to support cell-substrate adhesion and have mapped its cell-binding function onto its structure. In a cell-substrate adhesion assay, fibroblasts bound to cytotactin but remained round. In contrast, they both attached and spread on fibronectin. Neither neurons nor glia bound to cytotactin in this assay. In an assay in which cell-substrate contact was initiated by centrifugation, however, neurons and glia bound well to cytotactin; this binding was blocked by specific anti-cytotactin antibodies. The results suggest that neurons and glia can bind to cytotactin-coated substrates and that these cells, like fibroblasts, possess cell surface ligands for cytotactin. After applying methods of limited proteolysis and fractionation, these assays were used to map the binding functions of cytotactin onto its structure. Fragments produced by limited proteolysis were fractionated into two major pools: one (fraction I) contained disulfide-linked oligomers of a 100-kD fragment and two minor related fragments, and the second (fraction II) contained monomeric 90- and 65-kD fragments. The 90- and 65-kD fragments in fraction II were closely related to each other and were structurally and immunologically distinct from the fragments in fraction I. Only components in fraction I were recognized by mAb M1, which binds to an epitope located in the proximal portion of the arms of the hexabrachion and by a polyclonal antibody prepared against a 75-kD CNBr fragment of intact cytotactin. A mAb (1D8) and a polyclonal antibody prepared against a 35-kD CNBr fragment of cytotactin only recognized components present in fraction II. In cell-binding experiments, fibroblasts, neurons, and glia each adhered to substrates coated with fraction II, but did not adhere to substrates coated with fraction I. Fab fragments of the antibody to the 35-kD CNBr fragment strongly inhibited the binding of cells to cytotactin, supporting the conclusion that fraction II contains a cell-binding region. In addition, Fab fragments of this antibody inhibited the binding of cytotactin to CTB pr

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