Caherin Function
Published by Anonymous on 2007/9/27 (2138 reads)
1: FEBS Lett. 2007 Jan 23;581(2):167-74. Epub 2007 Jan 3.
Beyond the epithelium: cadherin function in fibrous connective tissues.
El Sayegh TY, Kapus A, McCulloch CA.
CIHR Group in Matrix Dynamics, University of Toronto, Room 243, Fitzgerald Building, 150 College Street, Toronto, Ont., Canada M5S 3E2. t.elsayegh@utoronto.ca
In fibrous connective tissues, fibroblasts are organized into syncytia, cellular networks that enable matrix remodeling and that are interconnected by intercellular adherens junctions (AJs). The AJs of fibroblasts are mediated by N-cadherin, a broadly expressed classical cadherin that is critically involved in developmental processes, wound healing and several diseases of mesenchymal tissues. In contrast to E-cadherin-dependent junctions of epithelia, the formation of AJs in fibrous connective tissues is relatively uncharacterized. Work over the last several years has documented an expanding list of molecules which function to regulate N-cadherin mediated junctions such as: Fer, PTP1B, cortactin, calcium, gelsolin, PIP5KIgamma, PIP2, and the Rho family of GTPases. We present an overview on the regulation of N-cadherin-mediated junction formation that highlights recent molecular advances in the field and rationalizes the roles of N-cadherin in connective tissue function.
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 17217950 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
2: Seikagaku. 2006 Jul;78(7):609-14.
[Loss of adhesive function of desmosomal cadherin and skin diseases in humans and animals]
[Article in Japanese]
Nishifuji K, Amagai M.
Department of Dermatology, Keio University School of Medicine, 35 Shinanomachi, Shinjuku-ku, Tokyo 160-8582, Japan.
Publication Types:
Review
PMID: 16910554 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
3: Seikagaku. 2006 Jul;78(7):579-87.
[Structure and function of cadherin-catenin complex]
[Article in Japanese]
Nagafuchi A.
Division of Cellular Interactions, Institute of Molecular Embryology and Genetics, Kumamoto University, Honjo 2-2-1, Kumamoto 860-0811, Japan.
Publication Types:
Review
PMID: 16910550 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
4: Inflammopharmacology. 2005;13(1-3):91-101.
Polyamines regulate expression of E-cadherin and play an important role in control of intestinal epithelial barrier function.
Wang JY.
Surgical Service, Baltimore Veterans Affairs Medical Center, 10 North Greene Street, Baltimore, MD 21201, USA. jwang@smail.umaryland.edu
Epithelial cells line the gastrointestinal mucosa and form an important barrier that protects the subepithelial tissue against a wide array of noxious substances, allergens, viruses and luminal microbial pathogens. Restoration of mucosal integrity following injury and various environmental stresses requires epithelial cell decisions that regulate signaling networks controlling gene expression, survival, migration and proliferation. Recently, it has been shown that polyamines play an important role in the regulation of cell-cell interactions and are critical for maintenance of intestinal epithelial integrity. Both the function of polyamines in expression of adherens junction proteins and their possible mechanisms, especially in implication of intracellular Ca2+ and c-Myc transcription factor, are the subject of this review article.
Publication Types:
Research Support, N.I.H., Extramural
Research Support, U.S. Gov't, Non-P.H.S.
Review
PMID: 16259731 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
5: Heart Fail Rev. 2000 Oct;5(3):251-7.
N-Cadherin: structure, function and importance in the formation of new intercalated disc-like cell contacts in cardiomyocytes.
Zuppinger C, Eppenberger-Eberhardt M, Eppenberger HM.
Dept. of Biology, Institute of Cell Biology, Swiss Federal Institute of Technology ETH, CH-8093, Zurich, Switzerland.
N-Cadherin belongs to a superfamily of calcium-dependent transmembrane adhesion proteins. It mediates adhesion in the intercalated discs at the termini of cardiomyocytes thereby serving as anchor for myofibrils at cell-cell contacts. A large body of data on the molecular structure and function of N-cadherin exists, however, little is known concerning spatial and temporal interactions between the different junctional structures during formation of the intercalated disc and its maturation in postnatal development. The progression of compensated left ventricular hypertrophy to congestive left heart failure is accompanied by intercalated disc remodeling and has been demonstrated in animal models and in patients. The long-term culture of adult rat cardiomyocytes allows to investigate the development of de novo intercalated disc-like structures. In order to analyze the dynamics of the cytoskeletal redifferentiation in living cells, we used the expression of chimeric proteins tagged with the green fluorescent protein reporter. This technique is becoming a routine method in basic research and complements video time-lapse and confocal microscopy. Cultured cardiomyocytes have been used for a variety of studies in cell biology and pharmacology. Their ability to form an electrically coupled beating tissue-like network in culture possibly allows reimplantation of such cells into injured myocardium, where they eventually will form new contacts with the healthy muscle tissue. Several groups have already shown that cardiomyocytes can be grafted successfully into sites of myocardial infarcts or cryoinjuries. Autologous adult cardiomyocyte implantation, might indeed contribute to cardiac repair after infarction, thanks to advances in tissue engineering.
Publication Types:
Comparative Study
Research Support, Non-U.S. Gov't
Review
PMID: 16228908 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
6: Zhong Nan Da Xue Xue Bao Yi Xue Ban. 2004 Jun;29(3):338-42.
[Structure and function of cadherin]
[Article in Chinese]
Huang YL, Song ZX.
Publication Types:
Review
PMID: 16136975 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
7: J Mol Histol. 2004 Mar;35(3):263-75.
Role of subtilisin-like convertases in cadherin processing or the conundrum to stall cadherin function by convertase inhibitors in cancer therapy.
Müller EJ, Caldelari R, Posthaus H.
Institute of Animal Pathology, University of Berne, Bern, Switzerland.
Cadherins are a family of intercellular adhesion receptors. Produced as inactive precursors, they become functional adhesion molecules after proteolytic cleavage by subtilisin-like pro-protein convertases (PCs). Owing to their activation and assembly into multiprotein adhesion complexes at sites of cell contacts, adhesion-competent cadherins are prerequisite for tissue integrity. In recent years evidence has accumulated that intercellular junctions not only provide mechanical linkage, but in addition are potent modulators of signalling cascades. This infers a biological role to intercellular adhesion complexes that is significantly more complex and powerful. Currently, the broad implications of disturbances in somatic tissue adhesion components are only just beginning to emerge. Prominent examples of adhesion defects include autoimmune diseases, or tumour invasion and metastasis and malignant transformation. This review reports on our current knowledge of cadherin function and their maturation by pro-protein convertases, and puts special emphasis on the consequences of pro-protein convertase inhibition for epithelial tissue homeostasis.
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 15339046 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
8: Cancer Cell. 2003 Apr;3(4):307-10.
Connecting estrogen receptor function, transcriptional repression, and E-cadherin expression in breast cancer.
Fearon ER.
Division of Molecular Medicine and Genetics and the Cancer Center, Department of Internal Medicine, University of Michigan Medical School, Ann Arbor, MI 48109, USA. fearon@umich.edu
A recent paper in Cell (Fujita et al., 2003) demonstrates that MTA3, a novel component of the Mi-2/NuRD transcriptional repression complex, is an estrogen receptor-regulated inhibitor of the Snail zinc finger transcription factor in breast cancer. Given the important role of Snail in repressing E-cadherin transcription and the function of E-cadherin as a tumor suppressor protein and regulator of epithelial architecture, the findings offer potentially significant new insights into cancer pathogenesis.
Publication Types:
Review
PMID: 12726856 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
9: Front Biosci. 2003 Jan 1;8:d306-55.
The cadherin superfamily in neural development: diversity, function and interaction with other molecules.
Hirano S, Suzuki ST, Redies C.
Recognition and Formation PRESTO, Japan Science and Technology Corporation, Saitama 332-0012, Japan. hirano@cdb.riken.go.jp
Cell-cell interactions are crucial steps for the development of the highly complex nervous system. A variety of cell-cell adhesion molecules of the cadherin superfamily have been found to be expressed in the developing nervous system. Recently it was proposed classic cadherins are involved in various aspects of neural development such as regionalization, brain nucleus formation, neurite outgrowth, target recognition and synaptogenesis. Classic cadherins preferentially bind to the same cadherin subtype ("homophilic adhesion"), and this binding specificity can provide an "adhesive code" that can account for various aspects of neural morphogenesis. In addition, novel members of the cadherin superfamily are also involved in various steps of neural development. The function of these cadherins molecules is orchestrated in the cellular context by a complex network of signaling pathways such as the small GTPase pathway. Here, we will review the molecular properties of the cadherin superfamily and their coordinated roles in the formation of the nervous system along with the accumulated knowledge in non-neuronal systems.
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 12456358 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
10: Nat Cell Biol. 2002 Oct;4(10):E227-30.
Comment on:
Nat Cell Biol. 2002 Oct;4(10):798-805.
Robo is Abl to block N-Cadherin function.
Emerson MM, Van Vactor D.
Publication Types:
Comment
Review
PMID: 12360300 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
11: Curr Biol. 2001 Jul 24;11(14):R569-72.
Cadherin function: breaking the barrier.
Ishii K, Green KJ.
Departments of Pathology and Dermatology, Northwestern University Medical School, 303 E. Chicago Avenue, Chicago, Illinois 60611, USA.
Three desmoglein isoforms collaborate with desmocollins to build the adhesive core of desmosomes. A recent study has shown that altering the ratio of desmoglein isoforms influences epidermal barrier function, suggesting distinct roles for these cadherins that extend beyond adhesion.
Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 11509257 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
12: Tanpakushitsu Kakusan Koso. 2001 Mar;46(3):197-207.
[Beta-catenin: its discovery as a cadherin-associated protein and its function as a transcription activator]
[Article in Japanese]
Ozawa M.
mozawa@m.kufm.kagoshima-u.ac.jp
Publication Types:
Review
PMID: 11244716 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
13: J Cell Sci. 2001 Feb;114(Pt 4):629-41.
The cadherin superfamily: diversity in form and function.
Angst BD, Marcozzi C, Magee AI.
Division of Membrane Biology, National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK. bangst@nimr.mrc.ac.uk
Over recent years cadherins have emerged as a growing superfamily of molecules, and a complex picture of their structure and their biological functions is becoming apparent. Variation in their extracellular region leads to the large potential for recognition properties of this superfamily. This is demonstrated strikingly by the recently discovered FYN-binding CNR-protocadherins; these exhibit alternative expression of the extracellular portion, which could lead to distinct cell recognition in different neuronal populations, whereas their cytoplasmic part, and therefore intracellular interactions, is constant. Diversity in the cytoplasmic moiety of the cadherins imparts specificity to their interactions with cytoplasmic components; for example, classical cadherins interact with catenins and the actin filament network, desmosomal cadherins interact with catenins and the intermediate filament system and CNR-cadherins interact with the SRC-family kinase FYN. Recent evidence suggests that CNR-cadherins, 7TM-cadherins and T-cadherin, which is tethered to the membrane by a GPI anchor, all localise to lipid rafts, specialised cell membrane domains rich in signalling molecules. Originally thought of as cell adhesion molecules, cadherin superfamily molecules are now known to be involved in many biological processes, such as cell recognition, cell signalling, cell communication, morphogenesis, angiogenesis and possibly even neurotransmission.
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 11171368 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
14: Eur J Cancer. 2000 Aug;36(13 Spec No):1607-20.
The E-cadherin-catenin complex in tumour metastasis: structure, function and regulation.
Beavon IR.
Department of Anatomical Pathology, School of Pathology, South African Institute for Medical Research and University of the Witwatersrand, Johannesburg, South Africa. nesinsa@global.co.za
E-cadherin and the associated catenin complex have been recognised as performing a key role in cell adhesion. Loss of cell adhesion is seen as a key step in the cascade leading to tumour metastasis. The ability of both extra- and intracellular factors to regulate E-cadherin-mediated cell adhesion in physiological processes has provided insight into both the interactions of the E-cadherin-catenin complex, and possible mechanisms utilised by tumours in the process of metastasis. The interaction of the E-cadherin-catenin complex with various regulating factors, their effect on cell signalling pathways, and the relationship with the metastatic potential of tumours are reviewed.
Publication Types:
Review
PMID: 10959047 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
15: Curr Opin Cell Biol. 1999 Oct;11(5):540-8.
Genetic analysis of cadherin function in animal morphogenesis.
Tepass U.
Department of Zoology University of Toronto 25 Harbord Street, Toronto, Ontario, M5S 3G5, Canada. utepass@zoo.utoronto.ca.
Cadherins are a superfamily of Ca(2+)-dependent adhesion molecules found in metazoans. Several classes of cadherins have been defined from which two - classic cadherins and Fat-like cadherins - have been studied by genetic approaches. Recent in vivo studies in Caenorhabditis elegans and Drosophila show that cadherins play an active role in a number of distinct morphogenetic processes. Classic cadherins function in epithelial polarization, epithelial sheet or tube fusion, cell migration, cell sorting, and axonal patterning. Fat-like cadherins are required for epithelial morphogenesis, proliferation control, and epithelial planar polarization.
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 10508657 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
16: Am J Hum Genet. 1998 Dec;63(6):1588-93.
The tumor-suppressor function of E-cadherin.
Semb H, Christofori G.
Institute of Medical Biochemistry, Gothenburg University, Sweden. Henrik.Semb@medkem.gu.se
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 9837810 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
17: Bioessays. 1997 Oct;19(10):883-91.
Tyrosine phosphorylation and cadherin/catenin function.
Daniel JM, Reynolds AB.
Dept of Cell Biology, Vanderbilt University School of Medicine, Nashville, TN 37232-2175, USA.
Cadherin-mediated cell-cell adhesion is perturbed in protein tyrosine kinase (PTK)-transformed cells. While cadherins themselves appear to be poor PTK substrates, their cytoplasmic binding partners, the Arm catenins, are excellent PTK substrates and therefore good candidates for mediating PTK-induced changes in cadherin behavior. These proteins, p120ctn, beta-catenin and plakoglobin, bind to the cytoplasmic region of classical cadherins and function to modulate adhesion and/or bridge cadherins to the actin cytoskeleton. In addition, as demonstrated recently for beta-catenin, these proteins also have crucial signaling roles that may or may not be related to their effects on cell-cell adhesion. Tyrosine phosphorylation of cadherin complexes is well documented and widely believed to modulate cell adhesiveness. The data to date, however, is largely correlative and the mechanism of action remains unresolved. In this review, we discuss the current literature and suggest models whereby tyrosine phosphorylation of Arm catenins contribute to regulation or perturbation of cadherin function.
Publication Types:
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 9363682 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
18: Curr Top Dev Biol. 1997;35:161-89.
beta-Catenin is a target for extracellular signals controlling cadherin function: the neurocan-GalNAcPTase connection.
Lilien J, Balsamo J, Hoffman S, Eisenberg C.
Department of Biological Sciences, Wayne State University, Detroit, Michigan 48230, USA.
Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 9292270 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
19: J Invest Dermatol. 1996 Sep;107(3):293-300.
Analysis of desmosomal cadherin-adhesive function and stoichiometry of desmosomal cadherin-plakoglobin complexes.
Kowalczyk AP, Borgwardt JE, Green KJ.
Department of Pathology, Northwestern University Medical School, Chicago, Illinois 60611, USA.
Desmosomes are intercellular adhesive junctions that associate with the intermediate filament cytoskeleton. The two major classes of transmembrane desmosomal glycoproteins, desmogleins and desmocollins, are widely considered to function as adhesion molecules. This assumption is based in part on their homology to the cadherin family of calcium-dependent homophilic adhesion molecules. In addition, autoantibodies from pemphigus patients bind directly to desmoglein family members and are thought to cause epidermal blistering by inhibiting the function of these cadherins. To directly test the ability of the desmosomal cadherins to mediate adhesion, desmoglein-1 (Dsg1), desmocollin-2 (Dsc2a) and plakoglobin were expressed in mouse L cell fibroblasts. Similar to catenin:classical cadherin complexes, plakoglobin:Dsc2a complexes exhibited an approximately 1:1 stoichiometry; however, plakoglobin:Dsg1 complexes exhibited a 6:1 stoichiometry. When L cells expressing the desmosomal cadherins were tested for the ability to aggregate in suspension, L cells expressing E-cadherin exhibited extensive aggregation, but L cells expressing Dsg1 or Dsc2a did not aggregate. In addition, L cells co-expressing Dsg1, Dsc2a, and plakoglobin failed to aggregate. The cytoplasmic domain of E-cadherin is thought to play a central role in the adhesive function of E-cadherin by providing a link to the actin cytoskeleton. Therefore, two chimeric cadherins comprising the cytoplasmic domain of E-cadherin and the extracellular domain of either Dsg1 or Dsc2a were expressed in L cells. Both chimeras formed a complex with alpha- and beta-catenin. Nevertheless, neither of these chimeras supported aggregation of L cells when expressed individually or when co-expressed. These data suggest that the extracellular domains of the desmosomal cadherins exhibit functional properties distinct from those of the classical cadherins, such as E-cadherin.
Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 8751959 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
20: Bioessays. 1996 Aug;18(8):609-12.
Adherens junctions in the Drosophila embryo: the role of E-cadherin in their establishment and morphogenetic function.
Knust E, Leptin M.
University of Cologne, Institut für Entwicklungsbiologie, Köln, Germany.
The integrity of epithelia depends largely on specialised adhesive structures, the adherens junctions. Several of the components required for building these structures are highly conserved between vertebrates and insects (e.g. E-cadherin and alpha- and beta-catenin), while others have so far been found only in invertebrates (e.g. crumbs). Two recent papers(1,2) show that the Drosophila E-cadherin is encoded by the gene shotgun. Phenotypic analyses of shotgun as well as armadillo (beta-catenin) and crumbs mutants provide new insights into the mechanisms by which adherens junctions are built and, further, show that the requirement for E-cadherin largely depends on the morphogenetic activity of an epithelium.
Publication Types:
Review
PMID: 8760333 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
21: Pathol Res Pract. 1996 Jul;192(7):694-707.
Regulation of the invasion suppressor function of the cadherin/catenin complex.
Vermeulen S, Van Marck V, Van Hoorde L, Van Roy F, Bracke M, Mareel M.
Laboratory of Experimental Cancerology, University Hospital, Gent, Belgium.
Invasion is the cause of cancer malignancy. Invasion results from the cross-talk between cancer cells and host cells, building molecular invasion-promoter and invasion-suppressor complexes. The E-cadherin/catenin invasion-suppressor complex is regulated multifactorially, at multiple levels and sometimes in a reversible way. Mutations in the E-cadherin gene combined with loss of the wild type allele, causing irreversible downregulation, has been demonstrated only in a minority of human cancers. Posttranslational and reversible downregulation has been ascribed to tyrosine phosphorylation of beta-catenin. Phosphorylation is also implicated in transmembrane receptor signal transduction through the E-cadherin/catenin complex. E-cadherin interacts with E-cadherin on another cell through a dimeric adhesion zipper, involving the histidine-alanine-valine (HAV) sequence of the first extracellular domains. This is the major extracellular like of the E-cadherin/catenin complex, though not the only one. Intracellularly, the list of proteins that bind to or signal through the complex or through one or more of its elements is steadily growing. Extrinsic factors may influence the complex. At least in vitro, insulin-like growth factor-I, retinoic acid, tangeretin and tamoxifen were shown to upregulate the functions of the E-cadherin/catenin complex including inhibition of invasion.
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 8880870 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
22: J Cell Biochem. 1996 Jun 15;61(4):514-23.
Cadherin-catenin complex: protein interactions and their implications for cadherin function.
Aberle H, Schwartz H, Kemler R.
Max-Planck-Institut für Immunbiologie, Freiburg, Germany.
Cadherins comprise a family of calcium-dependent glycoproteins that function in mediating cell-cell adhesion in virtually all solid tissues of multicellular organisms. In epithelial cells, E-cadherin represents a key molecule in the establishment and stabilization of cellular junctions. On the cellular level, E-cadherin is concentrated at the adherens junction and interacts homophilically with E-cadherin molecules of adjacent cells. Significant progress has been made in understanding the extra- and intracellular interactions of E-cadherin. Recent success in solving the three-dimensional structure of an extracellular cadherin domain provides a structural basis for understanding the homophilic interaction mechanism and the calcium requirement of cadherins. According to the crystal structure, individual cadherin molecules cooperate to form a linear cell adhesion zipper. The intracellular anchorage of cadherins is regulated by the dynamic association with cytoplasmic proteins, termed catenins. The cytoplasmic domain of E-cadherin is complexed with either beta-catenin or plakoglobin (gamma-catenin). Beta-catenin and plakoglobin bind directly to alpha-catenin, giving rise to two distinct cadherin-catenin complexes (CCC). Alpha-catenin is thought to link both CCC's to actin filaments. The anchorage of cadherins to the cytoskeleton appears to be regulated by tyrosine phosphorylation. Phosphorylation-induced junctional disassembly targets the catenins, indicating that catenins are components of signal transduction pathways. The unexpected association of catenins with the product of the tumor suppressor gene APC has led to the discovery of a second, cadherin-independent catenin complex. Two separate catenin complexes are therefore involved in the cross-talk between cell adhesion and signal transduction. In this review we focus on protein interactions regulating the molecular architecture and function of the CCC. In the light of a fundamental role of the CCC during mammalian development and tissue morphogenesis, we also discuss the phenotypes of embryos lacking E-cadherin or beta-catenin.
Publication Types:
Review
PMID: 8806074 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
23: Invasion Metastasis. 1994-1995;14(1-6):71-81.
Defective E-cadherin function in urological cancers: clinical implications and molecular mechanisms.
Giroldi LA, Bringuier PP, Schalken JA.
Urological Research Laboratory, University Hospital Nijmegen, The Netherlands.
Decreased E-cadherin expression assessed by immunohistochemistry correlates with poor survival of bladder and prostate cancer patients. The clinical usefulness of this parameter should therefore be evaluated in a large-scale prospective study. E-cadherin is an epithelial cell-cell adhesion molecule and impaired function presumably leads to increased invasive capacity of the cells. It has been shown that defective function can result from several mechanisms: mutation of the gene, alteration of transcription, posttranslational modification or changes in the interaction of E-cadherin with cytoskeleton anchoring proteins--the catenins. A major mechanism leading to decreased E-cadherin expression in tumors lies in decreased transcription of the gene. Hence, a better understanding of the regulation of E-cadherin transcription might open avenues for therapy by restoring normal expression.
Publication Types:
Review
PMID: 7657535 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
24: J Cell Sci Suppl. 1993;17:139-45.
Epithelial cell adhesion and development of cell surface polarity: possible mechanisms for modulation of cadherin function, organization and distribution.
Näthke IS, Hinck LE, Nelson WJ.
Department of Molecular and Cellular Physiology, Stanford University School of Medicine, CA 94305-5426.
Epithelial cell adhesion is principally regulated by calcium-dependent cell adhesion proteins, termed cadherins. Recent studies indicate that cadherin function is modulated by a class of proteins, termed catenins, that bind to the cytoplasmic domain of cadherin. Here we review the evidence that catenins regulate cadherin function in cell-cell adhesion, and discuss their role in initiating cell surface polarity in epithelial cells.
Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 8144690 [PubMed - indexed for MEDLINE]
Beyond the epithelium: cadherin function in fibrous connective tissues.
El Sayegh TY, Kapus A, McCulloch CA.
CIHR Group in Matrix Dynamics, University of Toronto, Room 243, Fitzgerald Building, 150 College Street, Toronto, Ont., Canada M5S 3E2. t.elsayegh@utoronto.ca
In fibrous connective tissues, fibroblasts are organized into syncytia, cellular networks that enable matrix remodeling and that are interconnected by intercellular adherens junctions (AJs). The AJs of fibroblasts are mediated by N-cadherin, a broadly expressed classical cadherin that is critically involved in developmental processes, wound healing and several diseases of mesenchymal tissues. In contrast to E-cadherin-dependent junctions of epithelia, the formation of AJs in fibrous connective tissues is relatively uncharacterized. Work over the last several years has documented an expanding list of molecules which function to regulate N-cadherin mediated junctions such as: Fer, PTP1B, cortactin, calcium, gelsolin, PIP5KIgamma, PIP2, and the Rho family of GTPases. We present an overview on the regulation of N-cadherin-mediated junction formation that highlights recent molecular advances in the field and rationalizes the roles of N-cadherin in connective tissue function.
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 17217950 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
2: Seikagaku. 2006 Jul;78(7):609-14.
[Loss of adhesive function of desmosomal cadherin and skin diseases in humans and animals]
[Article in Japanese]
Nishifuji K, Amagai M.
Department of Dermatology, Keio University School of Medicine, 35 Shinanomachi, Shinjuku-ku, Tokyo 160-8582, Japan.
Publication Types:
Review
PMID: 16910554 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
3: Seikagaku. 2006 Jul;78(7):579-87.
[Structure and function of cadherin-catenin complex]
[Article in Japanese]
Nagafuchi A.
Division of Cellular Interactions, Institute of Molecular Embryology and Genetics, Kumamoto University, Honjo 2-2-1, Kumamoto 860-0811, Japan.
Publication Types:
Review
PMID: 16910550 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
4: Inflammopharmacology. 2005;13(1-3):91-101.
Polyamines regulate expression of E-cadherin and play an important role in control of intestinal epithelial barrier function.
Wang JY.
Surgical Service, Baltimore Veterans Affairs Medical Center, 10 North Greene Street, Baltimore, MD 21201, USA. jwang@smail.umaryland.edu
Epithelial cells line the gastrointestinal mucosa and form an important barrier that protects the subepithelial tissue against a wide array of noxious substances, allergens, viruses and luminal microbial pathogens. Restoration of mucosal integrity following injury and various environmental stresses requires epithelial cell decisions that regulate signaling networks controlling gene expression, survival, migration and proliferation. Recently, it has been shown that polyamines play an important role in the regulation of cell-cell interactions and are critical for maintenance of intestinal epithelial integrity. Both the function of polyamines in expression of adherens junction proteins and their possible mechanisms, especially in implication of intracellular Ca2+ and c-Myc transcription factor, are the subject of this review article.
Publication Types:
Research Support, N.I.H., Extramural
Research Support, U.S. Gov't, Non-P.H.S.
Review
PMID: 16259731 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
5: Heart Fail Rev. 2000 Oct;5(3):251-7.
N-Cadherin: structure, function and importance in the formation of new intercalated disc-like cell contacts in cardiomyocytes.
Zuppinger C, Eppenberger-Eberhardt M, Eppenberger HM.
Dept. of Biology, Institute of Cell Biology, Swiss Federal Institute of Technology ETH, CH-8093, Zurich, Switzerland.
N-Cadherin belongs to a superfamily of calcium-dependent transmembrane adhesion proteins. It mediates adhesion in the intercalated discs at the termini of cardiomyocytes thereby serving as anchor for myofibrils at cell-cell contacts. A large body of data on the molecular structure and function of N-cadherin exists, however, little is known concerning spatial and temporal interactions between the different junctional structures during formation of the intercalated disc and its maturation in postnatal development. The progression of compensated left ventricular hypertrophy to congestive left heart failure is accompanied by intercalated disc remodeling and has been demonstrated in animal models and in patients. The long-term culture of adult rat cardiomyocytes allows to investigate the development of de novo intercalated disc-like structures. In order to analyze the dynamics of the cytoskeletal redifferentiation in living cells, we used the expression of chimeric proteins tagged with the green fluorescent protein reporter. This technique is becoming a routine method in basic research and complements video time-lapse and confocal microscopy. Cultured cardiomyocytes have been used for a variety of studies in cell biology and pharmacology. Their ability to form an electrically coupled beating tissue-like network in culture possibly allows reimplantation of such cells into injured myocardium, where they eventually will form new contacts with the healthy muscle tissue. Several groups have already shown that cardiomyocytes can be grafted successfully into sites of myocardial infarcts or cryoinjuries. Autologous adult cardiomyocyte implantation, might indeed contribute to cardiac repair after infarction, thanks to advances in tissue engineering.
Publication Types:
Comparative Study
Research Support, Non-U.S. Gov't
Review
PMID: 16228908 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
6: Zhong Nan Da Xue Xue Bao Yi Xue Ban. 2004 Jun;29(3):338-42.
[Structure and function of cadherin]
[Article in Chinese]
Huang YL, Song ZX.
Publication Types:
Review
PMID: 16136975 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
7: J Mol Histol. 2004 Mar;35(3):263-75.
Role of subtilisin-like convertases in cadherin processing or the conundrum to stall cadherin function by convertase inhibitors in cancer therapy.
Müller EJ, Caldelari R, Posthaus H.
Institute of Animal Pathology, University of Berne, Bern, Switzerland.
Cadherins are a family of intercellular adhesion receptors. Produced as inactive precursors, they become functional adhesion molecules after proteolytic cleavage by subtilisin-like pro-protein convertases (PCs). Owing to their activation and assembly into multiprotein adhesion complexes at sites of cell contacts, adhesion-competent cadherins are prerequisite for tissue integrity. In recent years evidence has accumulated that intercellular junctions not only provide mechanical linkage, but in addition are potent modulators of signalling cascades. This infers a biological role to intercellular adhesion complexes that is significantly more complex and powerful. Currently, the broad implications of disturbances in somatic tissue adhesion components are only just beginning to emerge. Prominent examples of adhesion defects include autoimmune diseases, or tumour invasion and metastasis and malignant transformation. This review reports on our current knowledge of cadherin function and their maturation by pro-protein convertases, and puts special emphasis on the consequences of pro-protein convertase inhibition for epithelial tissue homeostasis.
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 15339046 [PubMed - indexed for MEDLINE]
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8: Cancer Cell. 2003 Apr;3(4):307-10.
Connecting estrogen receptor function, transcriptional repression, and E-cadherin expression in breast cancer.
Fearon ER.
Division of Molecular Medicine and Genetics and the Cancer Center, Department of Internal Medicine, University of Michigan Medical School, Ann Arbor, MI 48109, USA. fearon@umich.edu
A recent paper in Cell (Fujita et al., 2003) demonstrates that MTA3, a novel component of the Mi-2/NuRD transcriptional repression complex, is an estrogen receptor-regulated inhibitor of the Snail zinc finger transcription factor in breast cancer. Given the important role of Snail in repressing E-cadherin transcription and the function of E-cadherin as a tumor suppressor protein and regulator of epithelial architecture, the findings offer potentially significant new insights into cancer pathogenesis.
Publication Types:
Review
PMID: 12726856 [PubMed - indexed for MEDLINE]
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9: Front Biosci. 2003 Jan 1;8:d306-55.
The cadherin superfamily in neural development: diversity, function and interaction with other molecules.
Hirano S, Suzuki ST, Redies C.
Recognition and Formation PRESTO, Japan Science and Technology Corporation, Saitama 332-0012, Japan. hirano@cdb.riken.go.jp
Cell-cell interactions are crucial steps for the development of the highly complex nervous system. A variety of cell-cell adhesion molecules of the cadherin superfamily have been found to be expressed in the developing nervous system. Recently it was proposed classic cadherins are involved in various aspects of neural development such as regionalization, brain nucleus formation, neurite outgrowth, target recognition and synaptogenesis. Classic cadherins preferentially bind to the same cadherin subtype ("homophilic adhesion"), and this binding specificity can provide an "adhesive code" that can account for various aspects of neural morphogenesis. In addition, novel members of the cadherin superfamily are also involved in various steps of neural development. The function of these cadherins molecules is orchestrated in the cellular context by a complex network of signaling pathways such as the small GTPase pathway. Here, we will review the molecular properties of the cadherin superfamily and their coordinated roles in the formation of the nervous system along with the accumulated knowledge in non-neuronal systems.
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 12456358 [PubMed - indexed for MEDLINE]
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10: Nat Cell Biol. 2002 Oct;4(10):E227-30.
Comment on:
Nat Cell Biol. 2002 Oct;4(10):798-805.
Robo is Abl to block N-Cadherin function.
Emerson MM, Van Vactor D.
Publication Types:
Comment
Review
PMID: 12360300 [PubMed - indexed for MEDLINE]
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11: Curr Biol. 2001 Jul 24;11(14):R569-72.
Cadherin function: breaking the barrier.
Ishii K, Green KJ.
Departments of Pathology and Dermatology, Northwestern University Medical School, 303 E. Chicago Avenue, Chicago, Illinois 60611, USA.
Three desmoglein isoforms collaborate with desmocollins to build the adhesive core of desmosomes. A recent study has shown that altering the ratio of desmoglein isoforms influences epidermal barrier function, suggesting distinct roles for these cadherins that extend beyond adhesion.
Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 11509257 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
12: Tanpakushitsu Kakusan Koso. 2001 Mar;46(3):197-207.
[Beta-catenin: its discovery as a cadherin-associated protein and its function as a transcription activator]
[Article in Japanese]
Ozawa M.
mozawa@m.kufm.kagoshima-u.ac.jp
Publication Types:
Review
PMID: 11244716 [PubMed - indexed for MEDLINE]
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13: J Cell Sci. 2001 Feb;114(Pt 4):629-41.
The cadherin superfamily: diversity in form and function.
Angst BD, Marcozzi C, Magee AI.
Division of Membrane Biology, National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK. bangst@nimr.mrc.ac.uk
Over recent years cadherins have emerged as a growing superfamily of molecules, and a complex picture of their structure and their biological functions is becoming apparent. Variation in their extracellular region leads to the large potential for recognition properties of this superfamily. This is demonstrated strikingly by the recently discovered FYN-binding CNR-protocadherins; these exhibit alternative expression of the extracellular portion, which could lead to distinct cell recognition in different neuronal populations, whereas their cytoplasmic part, and therefore intracellular interactions, is constant. Diversity in the cytoplasmic moiety of the cadherins imparts specificity to their interactions with cytoplasmic components; for example, classical cadherins interact with catenins and the actin filament network, desmosomal cadherins interact with catenins and the intermediate filament system and CNR-cadherins interact with the SRC-family kinase FYN. Recent evidence suggests that CNR-cadherins, 7TM-cadherins and T-cadherin, which is tethered to the membrane by a GPI anchor, all localise to lipid rafts, specialised cell membrane domains rich in signalling molecules. Originally thought of as cell adhesion molecules, cadherin superfamily molecules are now known to be involved in many biological processes, such as cell recognition, cell signalling, cell communication, morphogenesis, angiogenesis and possibly even neurotransmission.
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 11171368 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
14: Eur J Cancer. 2000 Aug;36(13 Spec No):1607-20.
The E-cadherin-catenin complex in tumour metastasis: structure, function and regulation.
Beavon IR.
Department of Anatomical Pathology, School of Pathology, South African Institute for Medical Research and University of the Witwatersrand, Johannesburg, South Africa. nesinsa@global.co.za
E-cadherin and the associated catenin complex have been recognised as performing a key role in cell adhesion. Loss of cell adhesion is seen as a key step in the cascade leading to tumour metastasis. The ability of both extra- and intracellular factors to regulate E-cadherin-mediated cell adhesion in physiological processes has provided insight into both the interactions of the E-cadherin-catenin complex, and possible mechanisms utilised by tumours in the process of metastasis. The interaction of the E-cadherin-catenin complex with various regulating factors, their effect on cell signalling pathways, and the relationship with the metastatic potential of tumours are reviewed.
Publication Types:
Review
PMID: 10959047 [PubMed - indexed for MEDLINE]
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15: Curr Opin Cell Biol. 1999 Oct;11(5):540-8.
Genetic analysis of cadherin function in animal morphogenesis.
Tepass U.
Department of Zoology University of Toronto 25 Harbord Street, Toronto, Ontario, M5S 3G5, Canada. utepass@zoo.utoronto.ca.
Cadherins are a superfamily of Ca(2+)-dependent adhesion molecules found in metazoans. Several classes of cadherins have been defined from which two - classic cadherins and Fat-like cadherins - have been studied by genetic approaches. Recent in vivo studies in Caenorhabditis elegans and Drosophila show that cadherins play an active role in a number of distinct morphogenetic processes. Classic cadherins function in epithelial polarization, epithelial sheet or tube fusion, cell migration, cell sorting, and axonal patterning. Fat-like cadherins are required for epithelial morphogenesis, proliferation control, and epithelial planar polarization.
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 10508657 [PubMed - indexed for MEDLINE]
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16: Am J Hum Genet. 1998 Dec;63(6):1588-93.
The tumor-suppressor function of E-cadherin.
Semb H, Christofori G.
Institute of Medical Biochemistry, Gothenburg University, Sweden. Henrik.Semb@medkem.gu.se
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 9837810 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
17: Bioessays. 1997 Oct;19(10):883-91.
Tyrosine phosphorylation and cadherin/catenin function.
Daniel JM, Reynolds AB.
Dept of Cell Biology, Vanderbilt University School of Medicine, Nashville, TN 37232-2175, USA.
Cadherin-mediated cell-cell adhesion is perturbed in protein tyrosine kinase (PTK)-transformed cells. While cadherins themselves appear to be poor PTK substrates, their cytoplasmic binding partners, the Arm catenins, are excellent PTK substrates and therefore good candidates for mediating PTK-induced changes in cadherin behavior. These proteins, p120ctn, beta-catenin and plakoglobin, bind to the cytoplasmic region of classical cadherins and function to modulate adhesion and/or bridge cadherins to the actin cytoskeleton. In addition, as demonstrated recently for beta-catenin, these proteins also have crucial signaling roles that may or may not be related to their effects on cell-cell adhesion. Tyrosine phosphorylation of cadherin complexes is well documented and widely believed to modulate cell adhesiveness. The data to date, however, is largely correlative and the mechanism of action remains unresolved. In this review, we discuss the current literature and suggest models whereby tyrosine phosphorylation of Arm catenins contribute to regulation or perturbation of cadherin function.
Publication Types:
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 9363682 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
18: Curr Top Dev Biol. 1997;35:161-89.
beta-Catenin is a target for extracellular signals controlling cadherin function: the neurocan-GalNAcPTase connection.
Lilien J, Balsamo J, Hoffman S, Eisenberg C.
Department of Biological Sciences, Wayne State University, Detroit, Michigan 48230, USA.
Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 9292270 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
19: J Invest Dermatol. 1996 Sep;107(3):293-300.
Analysis of desmosomal cadherin-adhesive function and stoichiometry of desmosomal cadherin-plakoglobin complexes.
Kowalczyk AP, Borgwardt JE, Green KJ.
Department of Pathology, Northwestern University Medical School, Chicago, Illinois 60611, USA.
Desmosomes are intercellular adhesive junctions that associate with the intermediate filament cytoskeleton. The two major classes of transmembrane desmosomal glycoproteins, desmogleins and desmocollins, are widely considered to function as adhesion molecules. This assumption is based in part on their homology to the cadherin family of calcium-dependent homophilic adhesion molecules. In addition, autoantibodies from pemphigus patients bind directly to desmoglein family members and are thought to cause epidermal blistering by inhibiting the function of these cadherins. To directly test the ability of the desmosomal cadherins to mediate adhesion, desmoglein-1 (Dsg1), desmocollin-2 (Dsc2a) and plakoglobin were expressed in mouse L cell fibroblasts. Similar to catenin:classical cadherin complexes, plakoglobin:Dsc2a complexes exhibited an approximately 1:1 stoichiometry; however, plakoglobin:Dsg1 complexes exhibited a 6:1 stoichiometry. When L cells expressing the desmosomal cadherins were tested for the ability to aggregate in suspension, L cells expressing E-cadherin exhibited extensive aggregation, but L cells expressing Dsg1 or Dsc2a did not aggregate. In addition, L cells co-expressing Dsg1, Dsc2a, and plakoglobin failed to aggregate. The cytoplasmic domain of E-cadherin is thought to play a central role in the adhesive function of E-cadherin by providing a link to the actin cytoskeleton. Therefore, two chimeric cadherins comprising the cytoplasmic domain of E-cadherin and the extracellular domain of either Dsg1 or Dsc2a were expressed in L cells. Both chimeras formed a complex with alpha- and beta-catenin. Nevertheless, neither of these chimeras supported aggregation of L cells when expressed individually or when co-expressed. These data suggest that the extracellular domains of the desmosomal cadherins exhibit functional properties distinct from those of the classical cadherins, such as E-cadherin.
Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 8751959 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
20: Bioessays. 1996 Aug;18(8):609-12.
Adherens junctions in the Drosophila embryo: the role of E-cadherin in their establishment and morphogenetic function.
Knust E, Leptin M.
University of Cologne, Institut für Entwicklungsbiologie, Köln, Germany.
The integrity of epithelia depends largely on specialised adhesive structures, the adherens junctions. Several of the components required for building these structures are highly conserved between vertebrates and insects (e.g. E-cadherin and alpha- and beta-catenin), while others have so far been found only in invertebrates (e.g. crumbs). Two recent papers(1,2) show that the Drosophila E-cadherin is encoded by the gene shotgun. Phenotypic analyses of shotgun as well as armadillo (beta-catenin) and crumbs mutants provide new insights into the mechanisms by which adherens junctions are built and, further, show that the requirement for E-cadherin largely depends on the morphogenetic activity of an epithelium.
Publication Types:
Review
PMID: 8760333 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
21: Pathol Res Pract. 1996 Jul;192(7):694-707.
Regulation of the invasion suppressor function of the cadherin/catenin complex.
Vermeulen S, Van Marck V, Van Hoorde L, Van Roy F, Bracke M, Mareel M.
Laboratory of Experimental Cancerology, University Hospital, Gent, Belgium.
Invasion is the cause of cancer malignancy. Invasion results from the cross-talk between cancer cells and host cells, building molecular invasion-promoter and invasion-suppressor complexes. The E-cadherin/catenin invasion-suppressor complex is regulated multifactorially, at multiple levels and sometimes in a reversible way. Mutations in the E-cadherin gene combined with loss of the wild type allele, causing irreversible downregulation, has been demonstrated only in a minority of human cancers. Posttranslational and reversible downregulation has been ascribed to tyrosine phosphorylation of beta-catenin. Phosphorylation is also implicated in transmembrane receptor signal transduction through the E-cadherin/catenin complex. E-cadherin interacts with E-cadherin on another cell through a dimeric adhesion zipper, involving the histidine-alanine-valine (HAV) sequence of the first extracellular domains. This is the major extracellular like of the E-cadherin/catenin complex, though not the only one. Intracellularly, the list of proteins that bind to or signal through the complex or through one or more of its elements is steadily growing. Extrinsic factors may influence the complex. At least in vitro, insulin-like growth factor-I, retinoic acid, tangeretin and tamoxifen were shown to upregulate the functions of the E-cadherin/catenin complex including inhibition of invasion.
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 8880870 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
22: J Cell Biochem. 1996 Jun 15;61(4):514-23.
Cadherin-catenin complex: protein interactions and their implications for cadherin function.
Aberle H, Schwartz H, Kemler R.
Max-Planck-Institut für Immunbiologie, Freiburg, Germany.
Cadherins comprise a family of calcium-dependent glycoproteins that function in mediating cell-cell adhesion in virtually all solid tissues of multicellular organisms. In epithelial cells, E-cadherin represents a key molecule in the establishment and stabilization of cellular junctions. On the cellular level, E-cadherin is concentrated at the adherens junction and interacts homophilically with E-cadherin molecules of adjacent cells. Significant progress has been made in understanding the extra- and intracellular interactions of E-cadherin. Recent success in solving the three-dimensional structure of an extracellular cadherin domain provides a structural basis for understanding the homophilic interaction mechanism and the calcium requirement of cadherins. According to the crystal structure, individual cadherin molecules cooperate to form a linear cell adhesion zipper. The intracellular anchorage of cadherins is regulated by the dynamic association with cytoplasmic proteins, termed catenins. The cytoplasmic domain of E-cadherin is complexed with either beta-catenin or plakoglobin (gamma-catenin). Beta-catenin and plakoglobin bind directly to alpha-catenin, giving rise to two distinct cadherin-catenin complexes (CCC). Alpha-catenin is thought to link both CCC's to actin filaments. The anchorage of cadherins to the cytoskeleton appears to be regulated by tyrosine phosphorylation. Phosphorylation-induced junctional disassembly targets the catenins, indicating that catenins are components of signal transduction pathways. The unexpected association of catenins with the product of the tumor suppressor gene APC has led to the discovery of a second, cadherin-independent catenin complex. Two separate catenin complexes are therefore involved in the cross-talk between cell adhesion and signal transduction. In this review we focus on protein interactions regulating the molecular architecture and function of the CCC. In the light of a fundamental role of the CCC during mammalian development and tissue morphogenesis, we also discuss the phenotypes of embryos lacking E-cadherin or beta-catenin.
Publication Types:
Review
PMID: 8806074 [PubMed - indexed for MEDLINE]
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23: Invasion Metastasis. 1994-1995;14(1-6):71-81.
Defective E-cadherin function in urological cancers: clinical implications and molecular mechanisms.
Giroldi LA, Bringuier PP, Schalken JA.
Urological Research Laboratory, University Hospital Nijmegen, The Netherlands.
Decreased E-cadherin expression assessed by immunohistochemistry correlates with poor survival of bladder and prostate cancer patients. The clinical usefulness of this parameter should therefore be evaluated in a large-scale prospective study. E-cadherin is an epithelial cell-cell adhesion molecule and impaired function presumably leads to increased invasive capacity of the cells. It has been shown that defective function can result from several mechanisms: mutation of the gene, alteration of transcription, posttranslational modification or changes in the interaction of E-cadherin with cytoskeleton anchoring proteins--the catenins. A major mechanism leading to decreased E-cadherin expression in tumors lies in decreased transcription of the gene. Hence, a better understanding of the regulation of E-cadherin transcription might open avenues for therapy by restoring normal expression.
Publication Types:
Review
PMID: 7657535 [PubMed - indexed for MEDLINE]
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24: J Cell Sci Suppl. 1993;17:139-45.
Epithelial cell adhesion and development of cell surface polarity: possible mechanisms for modulation of cadherin function, organization and distribution.
Näthke IS, Hinck LE, Nelson WJ.
Department of Molecular and Cellular Physiology, Stanford University School of Medicine, CA 94305-5426.
Epithelial cell adhesion is principally regulated by calcium-dependent cell adhesion proteins, termed cadherins. Recent studies indicate that cadherin function is modulated by a class of proteins, termed catenins, that bind to the cytoplasmic domain of cadherin. Here we review the evidence that catenins regulate cadherin function in cell-cell adhesion, and discuss their role in initiating cell surface polarity in epithelial cells.
Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 8144690 [PubMed - indexed for MEDLINE]
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