Accumulation of specific tight and adherens junction proteins is stimulated by antrum mucosal protein-18 in colonic epithelial cells in culture and mouse colon in vivo

2003 ◽  
Vol 124 (4) ◽  
pp. A315
Author(s):  
Margaret M. Walsh-Reitz ◽  
Erick Huang ◽  
Mark W. Musch ◽  
Eugene B. Chang ◽  
Terence E. Martin ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Adherens Junction ◽  
Colonic Epithelial Cells ◽  
Cells In Culture ◽  
Mouse Colon ◽  
Mucosal Protein ◽  
Adherens Junction Proteins ◽  
Junction Proteins

scholarly journals Interactions of a hemidesmosome component and actinin family members

2001 ◽  
Vol 114 (23) ◽  
pp. 4197-4206
Author(s):  
Annette M. Gonzalez ◽  
Carol Otey ◽  
Magnus Edlund ◽  
Jonathan C. R. Jones
Keyword(s):  
Epithelial Cells ◽  
Family Members ◽  
Adherens Junction ◽  
Cell Contact ◽  
Yeast Two Hybrid ◽  
Ef Hand ◽  
Adherens Junction Proteins ◽  
Two Hybrid ◽  
Junction Proteins ◽  
Cell Cell

Hemidesmosomes are multimeric protein complexes that attach epithelial cells to their underlying matrix and serve as cell surface anchorage sites for the keratin cytoskeleton. Two hemidesmosome components, the α6β4 integrin heterodimer and a human autoantigen termed BP180, are transmembrane proteins that link the extracellular matrix to the keratin network in cells. Here, we report that actinin-4, an actin-bundling protein, is a potential binding partner for BP180. Using yeast two-hybrid, we have mapped the binding site for BP180 to the C-terminal region of actinin-4. This site contains two EF-hand, Ca2+ regulation domains and shares 87% sequence homology with the same region in actinin-1. Consistent with this, BP180 can bind actinin-1 in both the yeast two-hybrid assay and in immunoprecipitation assays. To determine whether the EF-hand domain is a consensus binding sequence for BP180, we tested whether other proteins with this domain bind BP180. None of the proteins tested including calmodulin, with 4 EF-hand domains, and myosin regulatory light chain, with 1 EF-hand domain, interacts with BP180 in yeast two-hybrid system and immunoprecipitation studies, suggesting that the interaction between BP180 and actinin family members is specific. We have compared the distribution of actinin-1 and actinin-4 with that of BP180 in MCF-10A and pp126 cells. Surprisingly, BP180 localizes not only to sites of cell-substratum interaction, but is also present at sites of cell-cell contacts where it co-distributes with both actinin-1 and actinin-4 as well as other adherens junction proteins. In oral tissues, BP180 is present along the basement membrane and at cell-cell contact sites in basal epithelial cells where it co-distributes with adherens junction proteins. Since BP180 antibodies inhibit association of junction proteins at sites of cell-cell contact in oral keratinocytes, these results suggest that BP180 may play a role in establishing cell-cell interactions. We discuss a role for BP180 in crosstalk between cell-matrix and cell-cell junctions.

scholarly journals Drosophila p120catenin plays a supporting role in cell adhesion but is not an essential adherens junction component

2003 ◽  
Vol 160 (3) ◽  
pp. 433-449 ◽  
Author(s):  
Steven H. Myster ◽  
Robert Cavallo ◽  
Charles T. Anderson ◽  
Donald T. Fox ◽  
Mark Peifer
Keyword(s):  
Cell Adhesion ◽  
Adherens Junctions ◽  
Adherens Junction ◽  
Null Alleles ◽  
Juxtamembrane Region ◽  
Genes Encoding ◽  
Positive Modulator ◽  
Adherens Junction Proteins ◽  
Junction Structure ◽  
Junction Proteins

Cadherin–catenin complexes, localized to adherens junctions, are essential for cell–cell adhesion. One means of regulating adhesion is through the juxtamembrane domain of the cadherin cytoplasmic tail. This region is the binding site for p120, leading to the hypothesis that p120 is a key regulator of cell adhesion. p120 has also been suggested to regulate the GTPase Rho and to regulate transcription via its binding partner Kaiso. To test these hypothesized functions, we turned to Drosophila, which has only a single p120 family member. It localizes to adherens junctions and binds the juxtamembrane region of DE-cadherin (DE-cad). We generated null alleles of p120 and found that mutants are viable and fertile and have no substantial changes in junction structure or function. However, p120 mutations strongly enhance mutations in the genes encoding DE-cadherin or Armadillo, the β-catenin homologue. Finally, we examined the localization of p120 during embryogenesis. p120 localizes to adherens junctions, but its localization there is less universal than that of core adherens junction proteins. Together, these data suggest that p120 is an important positive modulator of adhesion but that it is not an essential core component of adherens junctions.

Ectopic expression of gastrokine 1 in gastric cancer cells up-regulates tight and adherens junction proteins network

2015 ◽  
Vol 211 (8) ◽  
pp. 577-583 ◽  
Author(s):  
Emilia Rippa ◽  
Filomena Altieri ◽  
Chiara Stella Di Stadio ◽  
Giuseppina Miselli ◽  
Annalisa Lamberti ◽  
...  
Keyword(s):  
Gastric Cancer ◽  
Cancer Cells ◽  
Ectopic Expression ◽  
Adherens Junction ◽  
Gastric Cancer Cells ◽  
Gastrokine 1 ◽  
Adherens Junction Proteins ◽  
Junction Proteins

scholarly journals DAAM mediates the assembly of long-lived, treadmilling stress fibers in collectively migrating epithelial cells in Drosophila

eLife ◽  
2021 ◽  
Vol 10 ◽  
Author(s):  
Kristin M Sherrard ◽  
Maureen Cetera ◽  
Sally Horne-Badovinac
Keyword(s):  
Epithelial Cells ◽  
Cell Movement ◽  
Stress Fibers ◽  
Linear Trajectory ◽  
Epithelial Migration ◽  
Cells In Culture ◽  
Multiple Cell ◽  
Developmental Switch ◽  
Over Time

Stress fibers (SFs) are actomyosin bundles commonly found in individually migrating cells in culture. However, whether and how cells use SFs to migrate in vivo or collectively is largely unknown. Studying the collective migration of the follicular epithelial cells in Drosophila, we found that the SFs in these cells show a novel treadmilling behavior that allows them to persist as the cells migrate over multiple cell lengths. Treadmilling SFs grow at their fronts by adding new integrin-based adhesions and actomyosin segments over time. This causes the SFs to have many internal adhesions along their lengths, instead of adhesions only at the ends. The front-forming adhesions remain stationary relative to the substrate and typically disassemble as the cell rear approaches. By contrast, a different type of adhesion forms at the SF’s terminus that slides with the cell’s trailing edge as the actomyosin ahead of it shortens. We further show that SF treadmilling depends on cell movement and identify a developmental switch in the formins that mediate SF assembly, with Dishevelled-associated activator of morphogenesis acting during migratory stages and Diaphanous acting during postmigratory stages. We propose that treadmilling SFs keep each cell on a linear trajectory, thereby promoting the collective motility required for epithelial migration.

Altered expression and interaction of adherens junction proteins in the developing OLM of the Rho(−/−) mouse

2007 ◽  
Vol 85 (5) ◽  
pp. 714-720 ◽  
Author(s):  
Matthew Campbell ◽  
Marian Humphries ◽  
Paul Kenna ◽  
Peter Humphries ◽  
Brenda Brankin
Keyword(s):  
Adherens Junction ◽  
Altered Expression ◽  
Adherens Junction Proteins ◽  
Junction Proteins

scholarly journals Effects of Atelocollagen Formulation Containing Oligonucleotide on Endothelial Permeability

2012 ◽  
Vol 2012 ◽  
pp. 1-9 ◽  
Author(s):  
Koji Hanai ◽  
Takashi Kojima ◽  
Mika Ota ◽  
Jun Onodera ◽  
Norimasa Sawada
Keyword(s):  
Drug Delivery ◽  
Size Structure ◽  
Biological Effects ◽  
Adherens Junction ◽  
Endothelial Permeability ◽  
Molecular Size ◽  
P38 Map Kinase ◽  
Delivery Technology ◽  
Junction Proteins

Atelocollagen is a major animal protein that is used as a highly biocompatible biomaterial. To date, atelocollagen has been used as an effective drug delivery technology to sustain the release of antitumor proteins and to enhance the antitumor activity of oligonucleotides in in vivo models. However, the biological effects of this technology are not fully understood. In the present study, we investigated the effects of atelocollagen on endothelial paracellular barrier function. An atelocollagen formulation containing oligonucleotides specifically increased the permeability of two types of endothelial cells, and the change was dependent on the molecular size, structure of the oligonucleotides used and the concentrations of the oligonucleotide and atelocollagen in the formulation. An immunohistochemical examination revealed that the formulation had effects on the cellular skeleton and intercellular structure although it did not affect the expression of adherens junction or tight junction proteins. These changes were induced through p38 MAP kinase signaling. It is important to elucidate the biological functions of atelocollagen in order to be able to exploit its drug delivery properties.

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