scholarly journals Patterning of cell assemblies regulated by adhesion receptors of the cadherin superfamily

2000 ◽  
Vol 355 (1399) ◽  
pp. 885-890 ◽  
Author(s):  
Masatoshi Takeichi ◽  
Shinichi Nakagawa ◽  
Shinya Aono ◽  
Tadao Usui ◽  
Tadashi Uemura
Keyword(s):  
Cell Adhesion ◽  
Neural Tube ◽  
Planar Cell Polarity ◽  
Cell Types ◽  
Carcinoma Cells ◽  
Adhesion Receptors ◽  
Cell Assemblies ◽  
Cell Association ◽  
Cadherin Superfamily ◽  
Cell Cell

During morphogenesis, cell–cell association patterns are dynamically altered. We are interested in how cell adhesion molecules can regulate the patterning of cellular assemblies. Cadherins, a group of cell–cell adhesion receptors, are crucial for the organized assembly of many cell types, but they also regulate dynamic aspects of cell association. For example, during neural crest emigration from the neural tube, the cadherin subtypes expressed by crest cells are switched from one subtype to another. Artificial perturbation of this switch results in blocking of their escape from the neural tube. Intracellular modulations of cadherin activity also seem to play a role in regulation of cell adhesion. We identified p120 ctn as a regulator of cadherin function in carcinoma cells. With such regulators, cells may make a choice as to whether they should maintain stable cell contacts or disrupt their association. Finally, we found another type of cadherin–mediated cell patterning: Flamingo, a seven–pass transmembrane cadherin, regulates planar cell polarity in Drosophila imaginal discs. Thus, the cadherin superfamily receptors control the patterning of cell assemblies through a variety of mechanisms.

Invasive behaviour of glioblastoma cell lines is associated with altered organisation of the cadherin-catenin adhesion system

2002 ◽  
Vol 115 (16) ◽  
pp. 3331-3340 ◽  
Author(s):  
Carla Perego ◽  
Cristina Vanoni ◽  
Silvia Massari ◽  
Andrea Raimondi ◽  
Sandra Pola ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Cell Lines ◽  
Protein A ◽  
Cell Types ◽  
Glioblastoma Cell ◽  
Migration Assay ◽  
Adhesion System ◽  
Pdz Protein ◽  
Glioblastoma Cell Lines ◽  
Cell Cell

As little is known about the role of cadherin-mediated cell-cell adhesion in astrocytes and its alteration in migrating and invasive glioblastomas, we investigated its molecular composition and organisation in primary cultured astrocytes and the T98G and U373MG glioblastoma cell lines. Biochemical and morphological analysis indicated that all three cell types express all of the structural components of the adhesion system, including the LIN-7 PDZ protein,a novel component involved in the organisation of the junctional domain in epithelia and neurons. However, only the astrocytes and T98G cells generated and maintained mature adhesive junctional domains to which LIN-7 was recruited. Alterations in the junctional domain of U373MG cells were associated with higher motility in a poly-L-lysine migration assay. When the T98G cells were cultured on Matrigel matrix, they acquired invasive properties but, despite unchanged cadherin adhesion system protein levels, the invasive T98G cell-cell contacts failed to accumulate LIN-7 and failed to mature. These results identify the LIN-7 PDZ protein as a marker of cell adhesion maturity and cell invasion and indicate that instability and disorganisation of cadherin-mediated junctions rather than reduced expression of cadherin-catenin system components are required to promote migration and invasiveness in glioblastoma cell lines.

Differential expression of R- and N-cadherin in neural and mesodermal tissues during early chicken development

Development ◽  
1991 ◽  
Vol 113 (3) ◽  
pp. 959-967 ◽  
Author(s):  
H. Inuzuka ◽  
C. Redies ◽  
M. Takeichi
Keyword(s):  
Cell Adhesion ◽  
Differential Expression ◽  
Neural Tube ◽  
Immunoblot Analysis ◽  
Spatial Segregation ◽  
Differentially Expressed ◽  
Adhesion Receptors ◽  
Chicken Embryos ◽  
Neural Tissues ◽  
Chicken Development

R-cadherin is a newly identified member of the cadherin family of cell adhesion receptors. The expression of R-cadherin in early chicken embryos was studied using affinity-purified antibodies to this molecule, comparing it with that of N-cadherin. Immunoblot analysis of various organs of 10.5-day embryos showed that R-cadherin is most abundantly expressed in the retina and brain. Immunostaining of the cervical and thoracic regions of embryos revealed that R- and N-cadherin are expressed in all neural tissues. In the neural tube, R-cadherin appears at around stage 21, although N-cadherin expression begins at a much earlier stage. The distribution of R-cadherin in the neural tube differs from that of N-cadherin; for example, some regions of the tube express only R-cadherin, and other regions only N-cadherin. In the peripheral ganglia, these two cadherins are also expressed in different patterns which change during development. Some mesenchymal tissues including the notochord, the myotome, myotubes and perichondria also express these cadherins, again in different patterns. Thus, R- and N-cadherin are differentially expressed in all the tissues examined, and they may contribute to the spatial segregation of heterogeneous cells in a tissue.

scholarly journals Calcium-dependent cell-cell adhesion molecules common to hepatocytes and teratocarcinoma stem cells.

1983 ◽  
Vol 97 (3) ◽  
pp. 944-948 ◽  
Author(s):  
S I Ogou ◽  
C Yoshida-Noro ◽  
M Takeichi
Keyword(s):  
Stem Cells ◽  
Cell Adhesion ◽  
Cell Types ◽  
Surface Proteins ◽  
Calcium Dependent ◽  
Molecular Weights ◽  
Teratocarcinoma Cells ◽  
Dependent Cell ◽  
Molecular Constitution ◽  
Cell Cell

The molecules involved in Ca2+-dependent cell-cell adhesion systems (CDS) in mouse hepatocytes were characterized and compared with those in teratocarcinoma cells. Fab fragments of antibody raised against liver tissues (anti-liver) inhibited Ca2+-dependent aggregation of both liver and teratocarcinoma cells. A monoclonal antibody raised against teratocarcinoma CDS (ECCD-1) also inhibited the Ca2+-dependent aggregation of these two cell types equally. These antibodies induced disruption of cell-cell adhesion in monolayers of hepatocytes. Thus, CDS in these two cell types are not immunologically distinctive. Immunochemical analyses with these antibodies showed that CDS in both hepatocytes and teratocarcinoma cells involved at least two classes of cell surface proteins with molecular weights of 124,000 and 104,000. ECCD-1 selectively bound to hepatocytes but not to fibroblastic cells in liver cell cultures. Thus, the molecular constitution of CDS in hepatocytes and teratocarcinoma stem cells is identical. As ECCD-1 reacts with other classes of embryonic and fetal cells, the molecules identified here could have a major role in cell-cell adhesion in various tissues at any developmental stage of animals.

Aquaporin water channels as regulators of cell-cell adhesion proteins

2021 ◽  
Author(s):  
Sarannya Edamana ◽  
Frédéric H. Login ◽  
Soichiro Yamada ◽  
Tae-Hwan Kwon ◽  
Lene N. Nejsum
Keyword(s):  
Cell Adhesion ◽  
Poor Prognosis ◽  
Fat Metabolism ◽  
Cell Types ◽  
Water Channels ◽  
Osmotic Gradient ◽  
Cellular Processes ◽  
Junctional Proteins ◽  
Cell Adhesion Proteins ◽  
Cell Cell

Aquaporin (AQP) water channels facilitate passive transport of water across cellular membranes following an osmotic gradient. AQPs are expressed in a multitude of epithelia, endothelia, and other cell types where they play important roles in physiology, especially in the regulation of body water homeostasis, skin hydration, and fat metabolism. AQP dysregulation is associated with many pathophysiological conditions, including nephrogenic diabetes insipidus, chronic kidney disease, and congestive heart failure. Moreover, AQPs have emerged as major players in a multitude of cancers where high expression correlates with metastasis and poor prognosis. Besides water transport, AQPs have been shown to be involved in cellular signaling, cell migration, cell proliferation, and in regulation of junctional proteins involved in cell-cell adhesion; all cellular processes which are dysregulated in cancer. This Mini-Review focuses on AQPs as regulators of junctional proteins involved in cell-cell adhesion.

αT-Catenin: a novel tissue-specific β-catenin-binding protein mediating strong cell-cell adhesion

2001 ◽  
Vol 114 (17) ◽  
pp. 3177-3188 ◽  
Author(s):  
Barbara Janssens ◽  
Steven Goossens ◽  
Katrien Staes ◽  
Barbara Gilbert ◽  
Jolanda van Hengel ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Immunohistochemical Analysis ◽  
Cell Types ◽  
Resistant Cell ◽  
Colon Carcinoma Cells ◽  
Intercalated Discs ◽  
Different Cell Types ◽  
Cell Adhesion Proteins ◽  
Cell Cell

Cadherins are major cell-cell adhesion proteins whose cytoplasmic domains bind to catenin proteins. Strong intercellular adhesion depends on linkage of the cadherin/catenin complex to the actin cytoskeleton via α-catenin. To date, it is not clear how different cell types achieve the variable strength of cell-cell adhesion clearly needed in a multicellular organism. Here, we report the cloning and molecular characterization of αT(testis)-catenin, a novel human cDNA encoding a protein with homology to both human αE(epithelial)-catenin and αN(neural)-catenin. Although originally discovered in testis, αT-catenin is expressed in other tissues, the highest levels being observed in heart. Immunohistochemical analysis showed human αT-catenin localization at intercalated discs of cardiomyocytes and in peritubular myoid cells of testis. In cells transfected with αT-catenin cDNA, interaction with β-catenin was demonstrated by co-immunoprecipitation. Transfection of α-catenin-deficient colon carcinoma cells recruited E-cadherin and β-catenin to cell-cell contacts and functional cadherin-mediated cell-cell adhesion was restored in this way. Moreover, compaction of these cells was at least as prominent as in the case of cells expressing endogenous αE-catenin. We propose that αT-catenin is necessary for the formation of stretch-resistant cell-cell adhesion complexes, in particular, muscle cells.

scholarly journals Regulation of C-cadherin function during activin induced morphogenesis of Xenopus animal caps.

1994 ◽  
Vol 126 (2) ◽  
pp. 519-527 ◽  
Author(s):  
W M Brieher ◽  
B M Gumbiner
Keyword(s):  
Cell Adhesion ◽  
Single Cells ◽  
Cell Types ◽  
Aggregation Assay ◽  
Animal Pole ◽  
Mesodermal Cell ◽  
Calcium Dependent ◽  
L Cells ◽  
Steady State Levels ◽  
Cell Cell

Treatment of Xenopus animal pole tissue with activin results in the induction of mesodermal cell types and a dramatic elongation of the tissue. The morphogenetic movements involved in the elongation appear similar to those in normal gastrulation, which is driven by cell rearrangement and cell intercalations. We have used this system to explore the potential regulation of cell-cell adhesion and cadherin function during morphogenesis. Quantitative blastomere aggregation assays revealed that activin induction reduced the calcium-dependent adhesion between blastomeres. Activin-induced blastomeres formed smaller aggregates, and a greater proportion of the population remained as single cells compared to uninduced blastomeres. The aggregation was mediated by C-cadherin because C-cadherin was present in the blastomeres during the aggregation assay, and monoclonal antibodies against C-cadherin inhibited the calcium-dependent aggregation of blastomeres. E-cadherin was not detectable until after the completion of the assay and, therefore, does not explain the adhesive differences between induced and uninduced blastomeres. L cells stably expressing C-cadherin (LC cells) were used to demonstrate that C-cadherin activity was specifically altered after activin induction. Blastomeres induced with activin bound fewer LC cells than uninduced blastomers. L cells not expressing C-cadherin did not adhere to blastomeres. The changes in C-cadherin-mediated adhesion occurred without detectable changes in the steady-state levels of C-cadherin or the amount of C-cadherin present on the surface of the cell. Immunoprecipitation of C-cadherin and its associated catenins revealed that the ratio of C-cadherin and the catenins was not altered by activin induction. These results demonstrate that activin decreases the adhesive function of existing C-cadherin molecules on the surface of blastomeres and suggest that decreased cadherin mediated cell-cell adhesion is associated with increased morphogenetic movement.

scholarly journals DSCAM promotes self-avoidance in the developing mouse retina by masking the functions of cadherin superfamily members

2018 ◽  
Vol 115 (43) ◽  
pp. E10216-E10224 ◽  
Author(s):  
Andrew M. Garrett ◽  
Andre Khalil ◽  
David O. Walton ◽  
Robert W. Burgess
Keyword(s):  
Cell Adhesion ◽  
Neural Development ◽  
Individual Cell ◽  
Cell Types ◽  
Mouse Retina ◽  
Cell Level ◽  
The Individual ◽  
Cadherin Superfamily

During neural development, self-avoidance ensures that a neuron’s processes arborize to evenly fill a particular spatial domain. At the individual cell level, self-avoidance is promoted by genes encoding cell-surface molecules capable of generating thousands of diverse isoforms, such as Dscam1 (Down syndrome cell adhesion molecule 1) in Drosophila. Isoform choice differs between neighboring cells, allowing neurons to distinguish “self” from “nonself”. In the mouse retina, Dscam promotes self-avoidance at the level of cell types, but without extreme isoform diversity. Therefore, we hypothesize that DSCAM is a general self-avoidance cue that “masks” other cell type-specific adhesion systems to prevent overly exuberant adhesion. Here, we provide in vivo and in vitro evidence that DSCAM masks the functions of members of the cadherin superfamily, supporting this hypothesis. Thus, unlike the isoform-rich molecules tasked with self-avoidance at the individual cell level, here the diversity resides on the adhesive side, positioning DSCAM as a generalized modulator of cell adhesion during neural development.

Differential expression of cell-cell adhesion proteins and cyclin D in MEK1-transdifferentiated MDCK cells

2000 ◽  
Vol 279 (5) ◽  
pp. C1472-C1482 ◽  
Author(s):  
Ingrid Marschitz ◽  
Judith Lechner ◽  
Irene Mosser ◽  
Martina Dander ◽  
Roberto Montesano ◽  
...  
Keyword(s):  
Cell Proliferation ◽  
Cell Adhesion ◽  
Mdck Cells ◽  
Cell Types ◽  
Mek Inhibitor ◽  
Mitogen Activated Protein Kinase ◽  
Cyclin D ◽  
Invasive Phenotype ◽  
E Cadherin ◽  
Cell Cell

Overexpression of a constitutively active mutant of the mitogen-activated protein kinase kinase MEK1 (caMEK1) in epithelial Madin-Darby canine kidney (MDCK)-C7 cells disrupts morphogenesis, induces an invasive phenotype, and is associated with a reduced rate of cell proliferation. The role of cell-cell adhesion molecules and cell cycle proteins in these processes, however, has not been investigated. We now report loss of E-cadherin expression as well as a marked reduction of β- and α-catenin expression in transdifferentiated MDCK-C7 cells stably expressing caMEK1 (C7caMEK1) compared with epithelial mock-transfected MDCK-C7 (C7Mock1) cells. At least part of the remaining α-catenin was coimmunoprecipitated with β-catenin, whereas no E-cadherin was detected in β-catenin immunoprecipitates. In both cell types, the proteasome-specific protease inhibitors N-acetyl-Leu-Leu-norleucinal (ALLN) and lactacystin led to a time-dependent accumulation of β-catenin, including the appearance of high-molecular-weight β-catenin species. Quiescent as well as serum-stimulated C7caMEK1 cells showed a higher cyclin D expression than epithelial C7Mock1 cells. The MEK inhibitor U-0126 inhibited extracellular signal-regulated kinase phosphorylation and cyclin D expression in C7caMEK1 cells and almost abolished their already reduced cell proliferation rate. We conclude that the transdifferentiated and invasive phenotype of C7caMEK1 cells is associated with a diminished expression of proteins involved in cell-cell adhesion. Although β-catenin expression is reduced, C7caMEK1 cells show a higher expression of U-0126-sensitive cyclin D protein.

Sign in / Sign up

Export Citation Format

Share Document