E-cadherin expression pattern during zebrafish embryonic epidermis development

Background: E-cadherin is the major adhesion receptor in epithelial adherens junctions (AJs). On established epidermis, E-cadherin performs fine-tuned cell-cell contact remodeling to maintain tissue integrity, which is characterized by modulation of cell shape, size and packing density. In zebrafish, the organization and distribution of E-cadherin in AJs during embryonic epidermis development remain scarcely described. Methods: Combining classical immunofluorescence, deconvolution microscopy and 3D-segmentation of AJs in epithelial cells, a quantitative approach was implemented to assess the spatial and temporal distribution of E-cadherin across zebrafish epidermis between 24 and 72 hpf. Results: increasing levels of E-cadh protein parallel higher cell density and the appearance of hexagonal cells in the enveloping layer (EVL) as well as the establishments of new cell-cell contacts in the epidermal basal layer (EBL), being significantly between 31 and 48 hpf. Conclusions: Increasing levels of E-cadherin in AJs correlates with extensive changes in cell morphology towards hexagonal packing during the epidermis morphogenesis.

Download Full-text

E-cadherin expression pattern during zebrafish embryonic epidermis development

F1000Research ◽

10.12688/f1000research.15932.2 ◽

2018 ◽

Vol 7 ◽

pp. 1489

Author(s):

María Florencia Sampedro ◽

María Fernanda Izaguirre ◽

Valeria Sigot

Keyword(s):

Cell Shape ◽

Basal Layer ◽

Temporal Distribution ◽

Cell Contact ◽

3D Segmentation ◽

Adhesion Receptor ◽

Hexagonal Packing ◽

Tissue Integrity ◽

E Cadherin ◽

Cell Cell

Background: E-cadherin is the major adhesion receptor in epithelial adherens junctions (AJs). On established epidermis, E-cadherin performs fine-tuned cell-cell contact remodeling to maintain tissue integrity, which is characterized by modulation of cell shape, size and packing density. In zebrafish, the organization and distribution of E-cadherin in AJs during embryonic epidermis development remain scarcely described. Methods: Combining classical immunofluorescence, deconvolution microscopy and 3D-segmentation of AJs in epithelial cells, a quantitative approach was implemented to assess the spatial and temporal distribution of E-cadherin across zebrafish epidermis between 24 and 72 hpf. Results: increasing levels of E-cadh protein parallel higher cell density and the appearance of hexagonal cells in the enveloping layer (EVL) as well as the establishments of new cell-cell contacts in the epidermal basal layer (EBL), being significantly between 31 and 48 hpf. Conclusions: Increasing levels of E-cadherin in AJs correlates with extensive changes in cell morphology towards hexagonal packing during the epidermis morphogenesis.

Download Full-text

Remodeling the cell surface distribution of membrane proteins during the development of epithelial cell polarity.

The Journal of Cell Biology ◽

10.1083/jcb.116.4.889 ◽

1992 ◽

Vol 116 (4) ◽

pp. 889-899 ◽

Cited By ~ 60

Author(s):

D A Wollner ◽

K A Krzeminski ◽

W J Nelson

Keyword(s):

Epithelial Cell ◽

Membrane Proteins ◽

Cell Surface ◽

Mdck Cells ◽

Apical Cell ◽

Cell Contact ◽

Surface Polarity ◽

Lateral Membrane ◽

E Cadherin ◽

Cell Cell

The development of polarized epithelial cells from unpolarized precursor cells follows induction of cell-cell contacts and requires resorting of proteins into different membrane domains. We show that in MDCK cells the distributions of two membrane proteins, Dg-1 and E-cadherin, become restricted to the basal-lateral membrane domain within 8 h of cell-cell contact. During this time, however, 60-80% of newly synthesized Dg-1 and E-cadherin is delivered directly to the forming apical membrane and then rapidly removed, while the remainder is delivered to the basal-lateral membrane and has a longer residence time. Direct delivery of greater than 95% of these proteins from the Golgi complex to the basal-lateral membrane occurs greater than 48 h later. In contrast, we show that two apical proteins are efficiently delivered and restricted to the apical cell surface within 2 h after cell-cell contact. These results provide insight into mechanisms involved in the development of epithelial cell surface polarity, and the establishment of protein sorting pathways in polarized cells.

Download Full-text

Changes in E-cadherin rigidity sensing regulate cell adhesion

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.1618676114 ◽

2017 ◽

Vol 114 (29) ◽

pp. E5835-E5844 ◽

Cited By ~ 34

Author(s):

Caitlin Collins ◽

Aleksandra K. Denisin ◽

Beth L. Pruitt ◽

W. James Nelson

Keyword(s):

Cell Adhesion ◽

Signaling Molecules ◽

Membrane Dynamics ◽

Cell Contact ◽

Adhesion Assay ◽

Cell Periphery ◽

Actin Organization ◽

Rigidity Sensing ◽

E Cadherin ◽

Cell Cell

Mechanical cues are sensed and transduced by cell adhesion complexes to regulate diverse cell behaviors. Extracellular matrix (ECM) rigidity sensing by integrin adhesions has been well studied, but rigidity sensing by cadherins during cell adhesion is largely unexplored. Using mechanically tunable polyacrylamide (PA) gels functionalized with the extracellular domain of E-cadherin (Ecad-Fc), we showed that E-cadherin–dependent epithelial cell adhesion was sensitive to changes in PA gel elastic modulus that produced striking differences in cell morphology, actin organization, and membrane dynamics. Traction force microscopy (TFM) revealed that cells produced the greatest tractions at the cell periphery, where distinct types of actin-based membrane protrusions formed. Cells responded to substrate rigidity by reorganizing the distribution and size of high-traction-stress regions at the cell periphery. Differences in adhesion and protrusion dynamics were mediated by balancing the activities of specific signaling molecules. Cell adhesion to a 30-kPa Ecad-Fc PA gel required Cdc42- and formin-dependent filopodia formation, whereas adhesion to a 60-kPa Ecad-Fc PA gel induced Arp2/3-dependent lamellipodial protrusions. A quantitative 3D cell–cell adhesion assay and live cell imaging of cell–cell contact formation revealed that inhibition of Cdc42, formin, and Arp2/3 activities blocked the initiation, but not the maintenance of established cell–cell adhesions. These results indicate that the same signaling molecules activated by E-cadherin rigidity sensing on PA gels contribute to actin organization and membrane dynamics during cell–cell adhesion. We hypothesize that a transition in the stiffness of E-cadherin homotypic interactions regulates actin and membrane dynamics during initial stages of cell–cell adhesion.

Download Full-text

RNAi-Mediated Knock-Down of Arylamine N-acetyltransferase-1 Expression Induces E-cadherin Up-Regulation and Cell-Cell Contact Growth Inhibition

PLoS ONE ◽

10.1371/journal.pone.0017031 ◽

2011 ◽

Vol 6 (2) ◽

pp. e17031 ◽

Cited By ~ 40

Author(s):

Jacky M. Tiang ◽

Neville J. Butcher ◽

Carleen Cullinane ◽

Patrick O. Humbert ◽

Rodney F. Minchin

Keyword(s):

Growth Inhibition ◽

Cell Contact ◽

Knock Down ◽

E Cadherin ◽

Cell Cell

Download Full-text

E-cadherin mediated cell adhesion recruits SAP97 into the cortical cytoskeleton

Journal of Cell Science ◽

10.1242/jcs.111.8.1071 ◽

1998 ◽

Vol 111 (8) ◽

pp. 1071-1080 ◽

Cited By ~ 6

Author(s):

S.M. Reuver ◽

C.C. Garner

Keyword(s):

Cell Adhesion ◽

Model Systems ◽

Molecular Organization ◽

Cell Contact ◽

Adhesion Sites ◽

Associated Proteins ◽

Adhesion Complex ◽

Cortical Cytoskeleton ◽

E Cadherin ◽

Cell Cell

Members of the SAP family of synapse-associated proteins have recently emerged as central players in the molecular organization of synapses. In this study, we have examined the mechanism that localizes one member, SAP97, to sites of cell-cell contact. Utilizing epithelial CACO-2 cells and fibroblast L-cells as model systems, we demonstrate that SAP97 is associated with the submembranous cortical cytoskeleton at cell-cell adhesion sites. Furthermore, we show that its localization into this structure is triggered by E-cadherin. Although SAP97 can be found in an E-cadherin/catenin adhesion complex, this interaction seems to be mediated by the attachment of SAP97 to the cortical cytoskeleton. Our results are consistent with a model in which SAP97 is recruited to sites of cell-cell contact via an E-cadherin induced assembly of the cortical cytoskeleton.

Download Full-text

p120-Catenin Is a Key Component of the Cadherin–γ-Secretase Supercomplex

Molecular Biology of the Cell ◽

10.1091/mbc.e08-04-0394 ◽

2008 ◽

Vol 19 (10) ◽

pp. 4042-4050 ◽

Cited By ~ 8

Author(s):

Alexi Kiss ◽

Regina B. Troyanovsky ◽

Sergey M. Troyanovsky

Keyword(s):

Proteolytic Activity ◽

Cell Contact ◽

Compelling Evidence ◽

P120 Catenin ◽

Low Level ◽

High Affinity ◽

Affinity Interaction ◽

E Cadherin ◽

Cell Cell

In this work, we show several previously unknown features of p120-catenin in a cadherin–catenin complex that are critical for our understanding of cadherin-based adhesion and signaling. We show that in human epithelial A-431 cells, nearly all p120 molecules engage in high-affinity interaction with E-cadherin–catenin complexes located at the cellular surface. p120 is positioned in proximity to α-catenin in the complex with cadherin. These findings suggest a functional cooperation between p120 and α-catenin in cadherin-based adhesion. A low level of cadherin-free p120 molecules, in contrast, could facilitate p120-dependent signaling. Finally, we present compelling evidence that p120 is a key linker cementing the E-cadherin–catenin complex with the transmembrane protease γ-secretase. The cell–cell contact location of this supercomplex makes it an important candidate for conducting different signals that rely on γ-secretase proteolytic activity.

Download Full-text

Regulation of matrilysin expression in cells of squamous cell carcinoma by E-cadherin-mediated cell-cell contact

Journal of Cancer Research and Clinical Oncology ◽

10.1007/bf01212609 ◽

1997 ◽

Vol 123 (1) ◽

pp. 13-20 ◽

Cited By ~ 16

Author(s):

Alexander H. Borchers ◽

Lisa A. Sanders ◽

G. Tim Bowden

Keyword(s):

Squamous Cell Carcinoma ◽

Cell Carcinoma ◽

Squamous Cell ◽

Cell Contact ◽

In Cells ◽

E Cadherin ◽

Cell Cell

Download Full-text

The Epidermal Stem Cell Compartment: Variation in Expression Levels of E–Cadherin and Catenins Within the Basal Layer of Human Epidermis

Journal of Histochemistry & Cytochemistry ◽

10.1177/002215549704500611 ◽

1997 ◽

Vol 45 (6) ◽

pp. 867-874 ◽

Cited By ~ 54

Author(s):

Jean-Pierre Molès ◽

Fiona M. Watt

Keyword(s):

Stem Cells ◽

Stem Cell ◽

Basal Layer ◽

Human Epidermis ◽

Proliferative Potential ◽

Stem Cell Markers ◽

Cell Compartment ◽

Stem Cell Compartment ◽

E Cadherin ◽

Cell Cell

The basal layer of the epidermis contains two types of proliferating keratinocyte: stem cells, with high proliferative potential, and transit amplifying cells, which are destined to undergo terminal differentiation after a few rounds of division. It has been shown previously that two- to three-fold differences in the average staining intensity of fluorescein-conjugated antibodies to β1 integrin subunits reflect profound differences in the proliferative potential of keratinocytes, with integrin-bright populations being enriched for stem cells. In the search for additional stem cell markers, we have stained sections of normal human epidermis with antibodies to proteins involved in intercellular adhesion and quantitated the fluorescence of individual cell-cell borders. In the basal layer, patches of brightly labeled cells were detected with antibodies to E-cadherin, β-catenin, and γ-catenin, but not with antibodies to P-cadherin, α-catenin, or with pan-desmocollin and pan-desmoglein antibodies. In the body sites examined, palm and foreskin, integrinbright regions were strongly labeled for γ-catenin and weakly labeled for E-cadherin and β-catenin. Our data suggest that there are gradients of both cell-cell and cell-extracellular matrix adhesiveness within the epidermal basal layer and that the levels of E-cadherin and of β-and γ-catenin may provide markers for the stem cell compartment, stem cells expressing relatively higher levels of γ-catenin and lower levels of E-cadherin and β-catenin than other basal keratinocytes.

Download Full-text