Changes in Gene Structure and Regulation of E-Cadherin during Epithelial Development, Differentiation, and Disease

https://doi.org/10.1016/S0079-6603(08)60281-0Get rights and content

Section snippets

Cadherin Structure

There are three main types of cell–cell junctions: occluding (tight), anchoring [desmosomal and zonula adherens (ZA)], and communication (GAP junctions or chemical synapses) (Fig. 1). Tight junctions seal off the basolateral aspects of the cell from fluids at the apical border, and this is usually achieved by a unique set of molecules, including ZO-1 and -2. Two subtypes of anchoring junctions are adhesion belts (cell–cell interaction) and basal focal contacts (cell–matrix interactions). The

Interactions between E-Cadherin and Other Cell Adhesion Molecules

In squamous epithelium, integrins and P-cadherin expression occur in the basal cell layer. In the parabasal layers E-cadherin is expressed as P-cadherin and the integrins are down-regulated 38., 39.. Although the exact mechanism of this regulation is not fully elucidated, it has been reported that cotransfection of rat 3Y1 cells with E-cadherin results in the expression of only one type of cadherin and the suppression of endogenous P-cadherin (40). Furthermore, expression of E-cadherin catenin

Adherens Junctions

The classical cadherins have widespread tissue distribution 12., 14., in contrast to the liver–intestine (LI) cadherins (96) (see Table I). The classical cadherins are present in the junctional complexes (both adherens and desmosomal junctions) and organize the actin cytoskeleton at the apical junctional complex. LI cadherins, on the other hand, exert adhesive properties in an even distribution on the basolateral membranes, probably at the desmosomal junctions (96).

Cell-Specific Recognition

Cadherins aet as cell–cell

Defects in Cell Adhesion during Colonic Inflammation—Spatial Changes of E-Cadherin in Vivo

It has been reported that intercellular adhesion molecules are down-regulated in UC (143). Similarly, there is up-regulation of nonfunctional cytoplasmic E-cadherin expression in UC during the inflammatory and granulation phases of epithelial adaptation, whereas the membranous expression decreases. As the disease activity progresses and enters the late remodeling phase, both cytoplasmic and membranous E-cadherin expression is lost altogether, reflecting in part the poor degree of cellular

Conclusions

Cadherins have highly conserved cytoplasmic and extracellular domains between species and among other members of the cadherin family. Each tissue has distinct cadherins and within the tissue; each cell subtype has specific quantities of particular cadherins.

There is qualitative, spatiotemporal expression of cadherins during renal development and subsequendy there is quantitative expression in the final stages of organogenesis 106., 179.. E-Cadherin is a reliable marker of differentiation when

ACKNOWLEDGMENTS

We would like to thank Dr. Inke Nathke, Cell and Molecular Biology Laboratory, University of Stanford, California, and Dr. Marion Bussemakers, Department of Urology, University of Nejmegen, The Netherlands, for participation in helpful discussions during the preparation of this manuscript. Without their comments, the completion of this article would not have been possible due to die complexity and rapid advances in the area of cadherin biology.

First page preview

First page preview
Click to open first page preview
View PDF

REFERENCES (192)

  • J. Jankowski et al.

    Sem. Cell. Biol.

    (1992)
  • I.A. King et al.

    J. Invest. Dermatol.

    (1995)
  • J. Behrens et al.

    J. Cell. Biol.

    (1993)
  • S. Miyatani et al.

    Proc. Natl. Acad. Sci. U.S.A.

    (1992)
  • S.J. Vermeulen et al.

    Br. J. Cancer

    (1995)
  • A.M. Fenyves et al.

    J. Cell. Biol.

    (1993)
  • K. Yoshiura et al.

    Proc. Natl. Acad. Sci. U.S.A.

    (1995)
  • L. Shapiro et al.

    Proc. Natl. Acad. Sci. U.S.A.

    (1995)
  • R.L. Juliano et al.

    J. Cell. Biol.

    (1993)
  • C. Murphy-Erdosh et al.

    J. Cell. Biol.

    (1994)
  • J.P. Doyle et al.

    Biol.

    (1995)
  • M. Kato et al.

    Mol. Biol. Cell

    (1995)
  • J.M. Trent et al.

    Cytogenet. Cell. Genet

    (1995)
  • K.R. Johnson et al.

    Exp. Cell Res.

    (1993)
  • I.S. Nathke et al.

    J. Cell. Biol.

    (1994)
  • L. Hinck et al.

    J. Cell. Biol.

    (1994)
  • G.M. Edelman et al.

    Annu. Rev. Biochem.

    (1991)
  • W.E. Pullman et al.

    Nature (London)

    (1993)
  • S. Shibamoto et al.

    J. Cell. Biol.

    (1995)
  • M. Nilsson et al.

    Exp. Cell. Res.

    (1995)
  • M. Pasdar et al.

    Cell Motil. Cytoskeleton

    (1993)
  • D.L. Rimm et al.

    Proc. Natl, Acad. Sci. U.S.A

    (1995)
  • K.A. Knudsen et al.

    J. Cell. Biol.

    (1995)
  • H. Sasaki et al.

    Proc. Annu. Meet. Am. Assoc

    Cancer Res.

    (1992)
  • M. Takeichi

    Science

    (1991)
  • M. Overduin et al.

    Science

    (1995)
  • J. Arnemann et al.

    J. Cell. Sci.

    (1993)
  • P.J.M.D. Koch et al.

    Proc. Natl. Acad. Sci. U.S.A.

    (1992)
  • K.H. Sano et al.

    EMBO J

    (1993)
  • B. Ranscht et al.

    Neuron

    (1991)
  • U.B. Frixen et al.

    J. Cell. Biol

    (1991)
  • J.M. Staddon et al.

    J. Cell. Sci.

    (1995)
  • G. Berx et al.

    Genomics

    (1995)
  • K. Hatta et al.

    Nucleic Acids Res.

    (1991)
  • D.L. Rimm et al.

    Mol. Biol.

    (1991)
  • K.F. Becker et al.

    Hum. Genet

    (1995)
  • J. Behrens et al.

    Proc. Natl. Acad. Sci. U.S.A

    (1991)
  • M.L. Faraldo et al.

    J. Mol. Biol.

    (1993)
  • B. D'souza et al.

    Proc. Natl. Acad. Sci. U.S.A.

    (1994)
  • J. Palacios et al.

    Virchows Arch.

    (1995)
  • G. Carruba et al.

    Biochem. Biophtjs. Res. Commun.

    (1995)
  • W.G. Jiang et al.

    Cancer Res.

    (1995)
  • S. Gopalakrishnan et al.

    Cell Growth Differen.

    (1995)
  • G. Hennig et al.

    Oncogene

    (1995)
  • G. Hennig et al.

    J. Biol. Chem.

    (1996)
  • C. Caulin et al.

    Cell Growth Differen.

    (1995)
  • W.I. Weis

    Structure

    (1995)
  • J.J. Deman et al.

    In Vitro Cell Deo. Biol. Anim.

    (1995)
  • S.H. Jaffe

    Proc. Natl. Acad. Sci. U.S.A.

    (1990)
  • T. Fujimori et al.

    Mol. Cell. Biol.

    (1993)

    • Cited by (24)

    • FOXM1 (Forkhead box M1) in tumorigenesis. Overexpression in human cancer, implication in tumorigenesis, oncogenic functions, tumor-suppressive properties, and target of anticancer therapy

      2013, Advances in Cancer Research
      Citation Excerpt :

      Consequently, the FOXM1c-induced E-cadherin expression (Wierstra, 2011a) may be important in the course of normal epithelial proliferation to ensure the maintainance of the normal E-cadherin level, for example, during permanent tissue renewal (e.g., skin, lining of gut and lung) or during accidental tissue repair after injury. In contrast to the general downregulation or loss of the E-cadherin expression in cancer cells (Agiostratidou et al., 2008; Baranwal and Alahari, 2009; Beavon, 2000; Berx and van Roy, 2009; Birchmeier, 1995; Buda and Pignatelli, 2011; Cavallaro and Christofori, 2004; Cavallaro et al., 2002; Christofori and Semb, 1999; Conacci-Sorrell et al., 2002; Giehl and Menke, 2008; Hajra and Fearon, 2002; Howard et al., 2008; Jankowski et al., 1997; Jeanes et al., 2008; Le Bras et al., 2012; Margineanu et al., 2008; Masterson and O’Dea, 2007; Moreno-Bueno et al., 2008; Paredes et al., 2012; Peinado et al., 2004, 2007; Salon et al., 2005; Schmalhofer et al., 2009; Sobrinho-Simeos and Oliveira, 2002; Stemmler, 2008; Strathdee, 2002; van Roy and Berx, 2008; Wheelock et al., 2007; Wood and Leong, 2003), there are a few exceptional tumor types, in which the expression of E-cadherin is not reduced or even elevated. For example, the E-cadherin expression is maintained in oral SCC (Ziober et al., 2001), in inflammatory breast cancer (Charafe-Jauffret et al., 2004, 2007; Colpaert et al., 2003; Garcia et al., 2007; Kleer et al., 2001; Nguyen et al., 2006; Tomlinson et al., 2001), and in biphasic synovial sarcoma (Kanemitsu et al., 2007; Laskin and Miettinen, 2002; Saito et al., 2000; Sato et al., 1999).

    • Transitions between epithelial and mesenchymal states in development and disease

      2008, Seminars in Cell and Developmental Biology

    • Different beta-catenin immunoexpression in carcinoid tumors of the appendix in comparison to other gastrointestinal carcinoid tumors

      2002, Pathology Research and Practice

    • The E-cadherin cell-cell adhesion complex and lung cancer invasion, metastasis, and prognosis

      2002, Lung Cancer

    • E-cadherin is a WT1 target gene

      2000, Journal of Biological Chemistry
      Citation Excerpt :

      The E-cadherin gene is frequently inactivated in human cancer, and its down-regulation is particularly associated with the acquisition of an invasive tumor phenotype (28, 34, 63). Allelic loss of heterozygosity of E-cadherin has been reported in cervical, prostrate, breast, hepatocellular, and colorectal carcinomas as well as in Wilms' tumor itself (28, 64-68). Point mutations of the E-cadherin gene were found in gastric, renal, lung, colorectal, and breast cancers (28, 66,69-74).

    • Dynamic regulation of adherens junctions: Implication in cell differentiation and tumor development

      2015, Intercellular Communication In Cancer
    View all citing articles on Scopus
    View full text
    Copyright © 1997 Academic Press. All rights reserved.