Runx2 deficiency in junctional epithelium of mouse molars decreases the expressions of E-cadherin and junctional adhesion molecule 1

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.

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Association of the HGF/SF Receptor, c-met, with the Cell-Surface Adhesion Molecule, E-Cadherin, and Catenins in Human Tumor Cells

Biochemical and Biophysical Research Communications ◽

10.1006/bbrc.1999.1002 ◽

1999 ◽

Vol 261 (2) ◽

pp. 406-411 ◽

Cited By ~ 70

Author(s):

S. Hiscox ◽

W.G. Jiang

Keyword(s):

Cell Surface ◽

Tumor Cells ◽

Adhesion Molecule ◽

Human Tumor ◽

Surface Adhesion ◽

Human Tumor Cells ◽

Cell Surface Adhesion Molecule ◽

E Cadherin

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Expression of E-cadherin adhesion molecule in oral suquamous cell carcinoma. Association with metastasis to regional lymph nodes and the influence of cancer chemotherapy on E-cadherin expression

Journal of Oral and Maxillofacial Surgery ◽

10.1016/s0278-2391(96)90374-2 ◽

1996 ◽

Vol 54 (10) ◽

pp. 1261

Author(s):

T Nakajima

Keyword(s):

Lymph Nodes ◽

Cell Carcinoma ◽

Cancer Chemotherapy ◽

Adhesion Molecule ◽

Regional Lymph Nodes ◽

E Cadherin

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Aberrant cell adhesion molecule expression in human bronchopulmonary sequestration and congenital cystic adenomatoid malformation

AJP Lung Cellular and Molecular Physiology ◽

10.1152/ajplung.90618.2008 ◽

2009 ◽

Vol 297 (1) ◽

pp. L143-L152 ◽

Cited By ~ 18

Author(s):

MaryAnn V. Volpe ◽

Eunice Chung ◽

Jason P. Ulm ◽

Brian F. Gilchrist ◽

Steven Ralston ◽

...

Keyword(s):

Cell Adhesion ◽

Adhesion Molecule ◽

Cell Adhesion Molecule ◽

Human Lung ◽

Congenital Cystic Adenomatoid Malformation ◽

Adhesion Molecule Expression ◽

Protein Levels ◽

Normal Human ◽

Hox Protein ◽

E Cadherin

In many organs, integrins and cadherins are partly regulated by Hox genes, but their interactions in airway morphogenesis and congenital lung diseases are unknown. We previously showed that the Hox protein HoxB5 is abnormally increased in bronchopulmonary sequestration (BPS) and congenital cystic adenomatoid malformation (CCAM), congenital lung lesions with abnormal airway branching. We now report on α2-, α3-, and β1-integrin and E-cadherin expression in normal human lung and in BPS and CCAM tissue previously shown to have abnormal HoxB5 expression and on the relationship of cell adhesion molecule expression to Hoxb5 regulation. α2-, α3-, and β1-integrins and E-cadherin expression in normal human lung and BPS and CCAM were evaluated using Western blot and immunohistochemistry. Fetal mouse lung fibroblasts with Hoxb5-specific siRNA downregulation were evaluated for α2-integrin protein levels by Western blot. Compared with normal human lung, a previously undetected α2-integrin isoform potentially lacking essential cytoplasmic sequences was significantly increased in BPS and CCAM, and α2-integrin spatial and cellular expression was more intense. E-cadherin protein levels were also significantly increased, whereas α3 increased in CCAM compared with canalicular, but not with alveolar, stage lung. β1-integrin levels were unchanged. We conclude that in BPS and CCAM, altered α2-integrin cytoplasmic signaling contributes to abnormal cellular behavior in these lung lesions. Aberrant cell adhesion molecule and Hox protein regulation are likely part of the mechanism involved in the development of BPS and CCAM.

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Expression of cell adhesion molecule E-cadherin in Xenopus embryos begins at gastrulation and predominates in the ectoderm.

The Journal of Cell Biology ◽

10.1083/jcb.108.6.2449 ◽

1989 ◽

Vol 108 (6) ◽

pp. 2449-2458 ◽

Cited By ~ 66

Author(s):

Y S Choi ◽

B Gumbiner

Keyword(s):

Cell Adhesion ◽

Epithelial Cell ◽

Xenopus Laevis ◽

Adhesion Molecule ◽

Cell Adhesion Molecule ◽

Cell Layer ◽

Outer Cell ◽

A6 Cells ◽

Xenopus Embryos ◽

E Cadherin

The expression of the Ca2+-dependent epithelial cell adhesion molecule E-cadherin (also known as uvomorulin and L-CAM) in the early stages of embryonic development of Xenopus laevis was examined. E-Cadherin was identified in the Xenopus A6 epithelial cell line by antibody cross-reactivity and several biochemical characteristics. Four independent mAbs were generated against purified Xenopus E-cadherin. All four mAbs recognized the same polypeptides in A6 cells, adult epithelial tissues, and embryos. These mAbs inhibited the formation of cell contacts between A6 cells and stained the basolateral plasma membranes of A6 cells, hepatocytes, and alveolar epithelial cells. The time of E-cadherin expression in early Xenopus embryos was determined by immunoblotting. Unlike its expression in early mouse embryos, E-cadherin was not present in the eggs or early blastula of Xenopus laevis. These findings indicate that a different Ca2+-dependent cell adhesion molecule, perhaps another member of the cadherin gene family, is responsible for the Ca2+-dependent adhesion between cleavage stage Xenopus blastomeres. Detectable accumulation of E-cadherin started just before gastrulation at stage 9 1/2 and increased rapidly up to the end of gastrulation at stage 15. In stage 15 embryos, specific immunofluorescence staining of E-cadherin was discernible only in ectoderm, but not in mesoderm and endoderm. The ectoderm at this stage consists of two cell layers. The outer cell layer of ectoderm was stained intensely, and staining was localized to the basolateral plasma membrane of these cells. Lower levels of staining were observed in the inner cell layer of ectoderm. The coincidence of E-cadherin expression with the process of gastrulation and its restriction to the ectoderm indicate that it may play a role in the morphogenetic movements of gastrulation and resulting segregation of embryonic germ layers.

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