E-cadherin N-glycosylation Modulates the Strength of Adherens Junctions

2010 ◽  
Author(s):  
Sarah J. Shareef ◽  
Mihai Nita-Lazar ◽  
Maria A. Kukuruzinska
Keyword(s):  
Cell Adhesion ◽  
Cancer Cells ◽  
Solid Tumor ◽  
Adherens Junctions ◽  
The Body ◽  
Junction Formation ◽  
E Cadherin

Metastasis, the spread of cancer cells throughout the body, claims 90% of solid tumor deaths. During metastasis, cancer cells undergo discohesion. An understanding of how to control and strengthen cell adhesion through junction formation could lead to methods for decreasing metastatic tendencies.

622: Von Hippel-Lindau Inactivation Downregulates the Cell-Cell Adhesion Molecule E Cadherin in Renal Cancer Cells

2005 ◽  
Vol 173 (4S) ◽  
pp. 170-170
Author(s):  
Maxine G. Tran ◽  
Miguel A. Esteban ◽  
Peter D. Hill ◽  
Ashish Chandra ◽  
Tim S. O'Brien ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Cancer Cells ◽  
Renal Cancer ◽  
Adhesion Molecule ◽  
Cell Adhesion Molecule ◽  
Von Hippel Lindau ◽  
E Cadherin ◽  
Cell Cell

scholarly journals T cell adhesion and cytolysis of pancreatic cancer cells: a role for E-cadherin in immunotherapy?

2002 ◽  
Vol 87 (9) ◽  
pp. 1034-1041 ◽  
Author(s):  
J J French ◽  
J Cresswell ◽  
W K Wong ◽  
K Seymour ◽  
R M Charnley ◽  
...  
Keyword(s):  
Pancreatic Cancer ◽  
Cell Adhesion ◽  
T Cell ◽  
Cancer Cells ◽  
Pancreatic Cancer Cells ◽  
E Cadherin ◽  
T Cell Adhesion

scholarly journals Role of Nectin in Formation of E-Cadherin–based Adherens Junctions in Keratinocytes: Analysis with the N-Cadherin Dominant Negative Mutant

2003 ◽  
Vol 14 (4) ◽  
pp. 1597-1609 ◽  
Author(s):  
Yoshinari Tanaka ◽  
Hiroyuki Nakanishi ◽  
Shigeki Kakunaga ◽  
Noriko Okabe ◽  
Tomomi Kawakatsu ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Adhesion Molecule ◽  
Cell Adhesion Molecule ◽  
Adherens Junctions ◽  
Dominant Negative ◽  
Dominant Negative Mutant ◽  
Adhesion Activity ◽  
Negative Mutant ◽  
E Cadherin ◽  
Cell Cell

E-Cadherin is a Ca2+-dependent cell-cell adhesion molecule at adherens junctions (AJs) of epithelial cells. A fragment of N-cadherin lacking its extracellular region serves as a dominant negative mutant (DN) and inhibits cell-cell adhesion activity of E-cadherin, but its mode of action remains to be elucidated. Nectin is a Ca2+-independent immunoglobulin-like cell-cell adhesion molecule at AJs and is associated with E-cadherin through their respective peripheral membrane proteins, afadin and catenins, which connect nectin and cadherin to the actin cytoskeleton, respectively. We showed here that overexpression of nectin capable of binding afadin, but not a mutant incapable of binding afadin, reduced the inhibitory effect of N-cadherin DN on the cell-cell adhesion activity of E-cadherin in keratinocytes. Overexpressed nectin recruited N-cadherin DN to the nectin-based cell-cell adhesion sites in an afadin-dependent manner. Moreover, overexpression of nectin enhanced the E-cadherin–based cell-cell adhesion activity. These results suggest that N-cadherin DN competitively inhibits the association of the endogenous nectin-afadin system with the endogenous E-cadherin-catenin system and thereby reduces the cell-cell adhesion activity of E-cadherin. Thus, nectin plays a role in the formation of E-cadherin–based AJs in keratinocytes.

scholarly journals The force-sensitive protein Ajuba regulates cell adhesion during epithelial morphogenesis

2018 ◽  
Vol 217 (10) ◽  
pp. 3715-3730 ◽  
Author(s):  
William Razzell ◽  
Maria E. Bustillo ◽  
Jennifer A. Zallen
Keyword(s):  
Cell Adhesion ◽  
Adherens Junctions ◽  
The Body ◽  
Epithelial Morphogenesis ◽  
Mechanical Forces ◽  
Lim Domain ◽  
Lim Domains ◽  
High Tension ◽  
Axis Elongation ◽  
Epithelial Sheets

The reorganization of cells in response to mechanical forces converts simple epithelial sheets into complex tissues of various shapes and dimensions. Epithelial integrity is maintained throughout tissue remodeling, but the mechanisms that regulate dynamic changes in cell adhesion under tension are not well understood. In Drosophila melanogaster, planar polarized actomyosin forces direct spatially organized cell rearrangements that elongate the body axis. We show that the LIM-domain protein Ajuba is recruited to adherens junctions in a tension-dependent fashion during axis elongation. Ajuba localizes to sites of myosin accumulation at adherens junctions within seconds, and the force-sensitive localization of Ajuba requires its N-terminal domain and two of its three LIM domains. We demonstrate that Ajuba stabilizes adherens junctions in regions of high tension during axis elongation, and that Ajuba activity is required to maintain cell adhesion during cell rearrangement and epithelial closure. These results demonstrate that Ajuba plays an essential role in regulating cell adhesion in response to mechanical forces generated by epithelial morphogenesis.

Effects of hepatocyte growth factor on E-cadherin-mediated cell-cell adhesion in DU145 prostate cancer cells

Urology ◽  
2001 ◽  
Vol 58 (6) ◽  
pp. 1064-1069 ◽  
Author(s):  
Hidenobu Miura ◽  
Kenji Nishimura ◽  
Akira Tsujimura ◽  
Kiyomi Matsumiya ◽  
Kunio Matsumoto ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Cell Adhesion ◽  
Growth Factor ◽  
Hepatocyte Growth Factor ◽  
Cancer Cells ◽  
Prostate Cancer Cells ◽  
Hepatocyte Growth ◽  
E Cadherin ◽  
Cell Cell

scholarly journals Levels of Soluble E-Cadherin in Breast, Gastric, and Colorectal Cancers

2014 ◽  
Vol 2014 ◽  
pp. 1-7 ◽  
Author(s):  
Ombretta Repetto ◽  
Paolo De Paoli ◽  
Valli De Re ◽  
Vincenzo Canzonieri ◽  
Renato Cannizzaro
Keyword(s):  
Cell Adhesion ◽  
Cancer Cells ◽  
Body Fluids ◽  
Colorectal Cancers ◽  
Protein Fragment ◽  
Epithelial Cadherin ◽  
Cancer Dynamics ◽  
E Cadherin

Soluble E-cadherin is a 80 kDa protein fragment coming from the proteolytic cleavage of the extracellular domain of the full length epithelial cadherin, a molecule involved in cell adhesion/polarity and tissue morphogenesis. In comparison with normal epithelia, cancer cells show a decreased cadherin-mediated intercellular adhesion, and sE-cad levels normally increase in body fluids (blood and urine). This review focuses on soluble E-cadherin in sera of patients affected by three solid cancers (breast, gastric, and colorectal cancers) and how its levels correlate or not with some cancer parameters (e.g., dimension, progression, and localisation). We will describe the main proteomics approaches adopted to measure sE-cad bothin vivoandin vitroand the most important findings about its behaviour in cancer dynamics.

scholarly journals RAC1 Regulates Adherens Junctions through Endocytosis of E-Cadherin

2001 ◽  
Vol 12 (4) ◽  
pp. 847-862 ◽  
Author(s):  
Nasreen Akhtar ◽  
Neil A. Hotchin
Keyword(s):  
Cell Adhesion ◽  
Fluorescent Protein ◽  
Adherens Junctions ◽  
Expression Vectors ◽  
Epidermal Keratinocytes ◽  
Human Epidermal Keratinocytes ◽  
Cell Contacts ◽  
Green Fluorescent ◽  
E Cadherin ◽  
Cell Cell

The establishment of cadherin-dependent cell–cell contacts in human epidermal keratinocytes are known to be regulated by the Rac1 small GTP-binding protein, although the mechanisms by which Rac1 participates in the assembly or disruption of cell–cell adhesion are not well understood. In this study we utilized green fluorescent protein (GFP)-tagged Rac1 expression vectors to examine the subcellular distribution of Rac1 and its effects on E-cadherin–mediated cell–cell adhesion. Microinjection of keratinocytes with constitutively active Rac1 resulted in cell spreading and disruption of cell–cell contacts. The ability of Rac1 to disrupt cell–cell adhesion was dependent on colony size, with large established colonies being resistant to the effects of active Rac1. Disruption of cell–cell contacts in small preconfluent colonies was achieved through the selective recruitment of E-cadherin–catenin complexes to the perimeter of multiple large intracellular vesicles, which were bounded by GFP-tagged L61Rac1. Similar vesicles were observed in noninjected keratinocytes when cell–cell adhesion was disrupted by removal of extracellular calcium or with the use of an E-cadherin blocking antibody. Moreover, formation of these structures in noninjected keratinocytes was dependent on endogenous Rac1 activity. Expression of GFP-tagged effector mutants of Rac1 in keratinocytes demonstrated that reorganization of the actin cytoskeleton was important for vesicle formation. Characterization of these Rac1-induced vesicles revealed that they were endosomal in nature and tightly colocalized with the transferrin receptor, a marker for recycling endosomes. Expression of GFP-L61Rac1 inhibited uptake of transferrin-biotin, suggesting that the endocytosis of E-cadherin was a clathrin-independent mechanism. This was supported by the observation that caveolin, but not clathrin, localized around these structures. Furthermore, an inhibitory form of dynamin, known to inhibit internalization of caveolae, inhibited formation of cadherin vesicles. Our data suggest that Rac1 regulates adherens junctions via clathrin independent endocytosis of E-cadherin.

scholarly journals Regulation of cell–cell adhesion in prostate cancer cells by microRNA-96 through upregulation of E-Cadherin and EpCAM

2019 ◽  
Vol 41 (7) ◽  
pp. 865-874
Author(s):  
Gjendine Voss ◽  
Benedikta S Haflidadóttir ◽  
Helena Järemo ◽  
Margareta Persson ◽  
Tina Catela Ivkovic ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Cell Adhesion ◽  
Bone Metastasis ◽  
Cancer Cells ◽  
Molecular Mechanisms ◽  
Cell Interaction ◽  
Metastatic Progression ◽  
Prostate Cancer Cells ◽  
E Cadherin ◽  
Cell Cell

Abstract Prostate cancer is one of the most common cancers in men, yet the biology behind lethal disease progression and bone metastasis is poorly understood. In this study, we found elevated levels of microRNA-96 (miR-96) in prostate cancer bone metastasis samples. To determine the molecular mechanisms by which miR-96 deregulation contributes to metastatic progression, we performed an Argonaute2-immunoprecipitation assay, in which mRNAs associated with cell–cell interaction were enriched. The expression of two cell adhesion molecules, E-Cadherin and EpCAM, was upregulated by miR-96, and potential targets sites were identified in the coding sequences of their mRNAs. We further showed that miR-96 enhanced cell–cell adhesion between prostate cancer cells as well as their ability to bind to osteoblasts. Our findings suggest that increased levels of miR-96 give prostate cancer cells an advantage at forming metastases in the bone microenvironment due to increased cell–cell interaction. We propose that miR-96 promotes bone metastasis in prostate cancer patients by facilitating the outgrowth of macroscopic tumours in the bone.

‘MCC’ protein interacts with E-cadherin and β-catenin strengthening cell–cell adhesion of HCT116 colon cancer cells

Oncogene ◽  
2017 ◽  
Vol 37 (5) ◽  
pp. 663-672 ◽  
Author(s):  
F A Benthani ◽  
D Herrmann ◽  
P N Tran ◽  
L Pangon ◽  
M C Lucas ◽  
...  
Keyword(s):  
Colon Cancer ◽  
Cell Adhesion ◽  
Cancer Cells ◽  
Colon Cancer Cells ◽  
E Cadherin ◽  
Cell Cell

scholarly journals A Putative Catenin–Cadherin System Mediates Morphogenesis of the Caenorhabditis elegans Embryo

1998 ◽  
Vol 141 (1) ◽  
pp. 297-308 ◽  
Author(s):  
Michael Costa ◽  
William Raich ◽  
Cristina Agbunag ◽  
Ben Leung ◽  
Jeff Hardin ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Caenorhabditis Elegans ◽  
Cell Shape ◽  
Shape Change ◽  
Adherens Junctions ◽  
The Body ◽  
C Elegans ◽  
Cell Shape Change ◽  
Filament Bundles ◽  
Cell Adhesion Proteins

During morphogenesis of the Caenorhabditis elegans embryo, hypodermal (or epidermal) cells migrate to enclose the embryo in an epithelium and, subsequently, change shape coordinately to elongate the body (Priess, J.R., and D.I. Hirsh. 1986. Dev. Biol. 117:156– 173; Williams-Masson, E.M., A.N. Malik, and J. Hardin. 1997. Development [Camb.]. 124:2889–2901). We have isolated mutants defective in morphogenesis that identify three genes required for both cell migration during body enclosure and cell shape change during body elongation. Analyses of hmp-1, hmp-2, and hmr-1 mutants suggest that products of these genes anchor contractile actin filament bundles at the adherens junctions between hypodermal cells and, thereby, transmit the force of bundle contraction into cell shape change. The protein products of all three genes localize to hypodermal adherens junctions in embryos. The sequences of the predicted HMP-1, HMP-2, and HMR-1 proteins are related to the cell adhesion proteins α-catenin, β-catenin/Armadillo, and classical cadherin, respectively. This putative catenin–cadherin system is not essential for general cell adhesion in the C. elegans embryo, but rather mediates specific aspects of morphogenetic cell shape change and cytoskeletal organization.

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