関: cadherin、N-cadherin、P-cadherin、uvomorulin

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the 5th letter of the Roman alphabet (同)e
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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2014/06/03 21:12:38」(JST)

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Cadherin-1 also known as CAM 120/80 or epithelial cadherin (E-cadherin) or uvomorulin is a protein that in humans is encoded by the CDH1 gene.^[1] CDH1 has also been designated as CD324 (cluster of differentiation 324). It is a tumor suppressor gene.^[2]^[3]

Function

Cadherin-1 is a classical member of the cadherin superfamily. The encoded protein is a calcium-dependent cell-cell adhesion glycoprotein composed of five extracellular cadherin repeats, a transmembrane region, and a highly conserved cytoplasmic tail. Mutations in this gene are correlated with gastric, breast, colorectal, thyroid, and ovarian cancers. Loss of function is thought to contribute to progression in cancer by increasing proliferation, invasion, and/or metastasis. The ectodomain of this protein mediates bacterial adhesion to mammalian cells, and the cytoplasmic domain is required for internalization. Identified transcript variants arise from mutation at consensus splice sites.^[4]

E-cadherin (epithelial) is the most well-studied member of the cadherin family. It consists of 5 cadherin repeats (EC1 ~ EC5) in the extracellular domain, one transmembrane domain, and an intracellular domain that binds p120-catenin and beta-catenin. The intracellular domain contains a highly-phosphorylated region vital to beta-catenin binding and, therefore, to E-cadherin function.^{[citation needed]} Beta-catenin can also bind to alpha-catenin. Alpha-catenin participates in regulation of actin-containing cytoskeletal filaments. In epithelial cells, E-cadherin-containing cell-to-cell junctions are often adjacent to actin-containing filaments of the cytoskeleton.

E-cadherin is first expressed in the 2-cell stage of mammalian development, and becomes phosphorylated by the 8-cell stage, where it causes compaction.^{[citation needed]} In adult tissues, E-cadherin is expressed in epithelial tissues, where it is constantly regenerated with a 5-hour half-life on the cell surface.^{[citation needed]} Cell-cell interactions mediated by E-cadherin are crucial to blastula formation in many animals.^[5]

Clinical significance

Loss of E-cadherin function or expression has been implicated in cancer progression and metastasis.^[6] E-cadherin downregulation decreases the strength of cellular adhesion within a tissue, resulting in an increase in cellular motility. This in turn may allow cancer cells to cross the basement membrane and invade surrounding tissues.^[6] E-cadherin is also used by pathologists to diagnose different kinds of breast cancer. When compared with invasive ductal carcinoma, E-cadherin expression is markedly reduced or absent in the great majority of invasive lobular carcinomas when studied by immunohistochemistry.^[7]

Interactions

CDH1 (gene) has been shown to interact with

CBLL1,^[8]
CDC27,^[9]
CDON,^[10]
CDH3,^[11]
C-Met,^[12]^[13]^[14]^[15]^[16]^[17]^[18]^[19]
CTNNB1,^[10]^[14]^[15]^[17]^[18]^[20]^[21]^[22]^[23]^[24]^[25]^[26]^[27]^[28]^[29]^[30]^[31]^[32]^[33]^[34]^[35]^[36]^[37]
CTNNA1^[14]^[29]^[30]^[31]^[36]
FOXM1,^[38]
HDAC1,^[39]
HDAC2,^[39]
IQGAP1,^[40]
FYN,^[17]
NEDD9,^[41]
Plakoglobin,^[14]^[15]^[42]^[43]^[44]
Vinculin,^[15]^[23]

PTPmu(PTPRM)^[45]^[46]
PTPrho(PTPRT)^[47]

Cadherin-1 and cancer

Cadherin-1 in metastasis

Transitions between epithelial and mesenchymal states play important roles in embryonic development and cancer metastasis. E-cadherin level changes in EMT (epithelial-mesenchymal transition) and MET (mesenchymal-epithelial transition). E-cadherin acts as an invasion suppressor and a classical tumor suppressor gene in pre-invasive lobular breast carcinoma.^[48]

1. E-cadherin in EMT:

E-cadherin is a crucial type of cell-cell adhesion to hold the epithelial cells tight together. E-cadherin can sequester β-catenin on the cell membrane by the cytoplasmic tail of E-cadherin. Loss of E-cadherin expression results in releasing β-catenin into the cytoplasm. Liberated β-catenin molecules may migrate into the nucleus and trigger the expression of EMT-inducing transcription factors. Together with other mechanisms, such as constitutive RTK activation, E-cadherin loss can lead cancer cells to the mesenchymal state and undergo metastasis. E-cadherin is an important switch in EMT.^[48]

2. E-cadherin in MET:

The mesenchymal state cancer cells migrate to new sites and may undergo METs in certain favorable microenvironment. For example, the cancer cells can recognize differentiated epithelial cell features in the new sites and upregulate E-cadherin expression. Those cancer cells can form cell-cell adhesions again and return to an epithelial state.^[48]

Cancer examples

Inactivation of CDH1 (accompany with loss of the wild-type allele) in 56% of lobular breast carcinomas.^[49]^[50]

Inactivation of CDH1 in 50% of diffuse gastric carcinomas.^[51]

Complete loss of E-cadherin protein expression in 84% of lobular breast carcinomas.^[52]

Genetic and epigenetic control of CDH1

Several proteins such as SNAI1/SNAIL,^[53]^[54] ZFHX1B/SIP1,^[55] SNAI2/SLUG,^[56]^[57] TWIST1^[58] and DeltaEF1^[59] have been found to downregulate E-cadherin expression. When expression of those transcription factors is altered, transcriptional repressors of E-cadherin were overexpressed in tumor cells.^[53]^[54]^[55]^[56]^[58]^[59] Another group of genes, such as AML1, p300 and HNF3,^[60] can upregulate the expression of E-cadherin.^[61]

In order to study the epigenetic regulation of E-cadherin, M Lombaerts et al. performed a genome wide expression study on 27 human mammary cell lines. Their results revealed two main clusters that have the fibroblastic or epithelial phenotype, respectively. In close examination, the clusters showing fibroblast phenotypes only have either partial or complete CDH1 promoter methylation, while the clusters with epithelial phenotypes have both wild-type cell lines and cell lines with mutant CDH1 status. The authors also found that EMT can happen in breast cancer cell lines with hypermethylation of CDH1 promoter, but in breast cancer cell lines with a CDH1 mutational inactivation EMT cannot happen. It contradicts the hypothesis that E-cadherin loss is the initial or primary cause for EMT. In conclusion, the results suggest that “E-cadherin transcriptional inactivation is an epi-phenomenon and part of an entire program, with much more severe effects than loss of E-cadherin expression alone”.^[61]

Other studies also show that epigenetic regulation of E-cadherin expression occurs during metastasis. The methylation patterns of the E-cadherin 5’ CpG island are not stable. During metastatic progression of many cases of epithelial tumors, a transient loss of E-cadherin is seen and the heterogeneous loss of E-cadherin expression results from a heterogeneous pattern of promoter region methylation of E-cadherin.^[62]

References

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External links

CDH1 protein, human at the US National Library of Medicine Medical Subject Headings (MeSH)
GeneReviews/NCBI/NIH/UW entry on Hereditary Diffuse Gastric Cancer

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

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日本産科婦人科學會雜誌 64(10), 2167-2179, 2012-10-01
… Most of the known actions of estrogen are mediated by estrogen receptor α(ERα) and ERβ, both of which bind 17β-Estradiol (E_2) and modulate transcription of E_2-responsive genes, and functional analysis of ER is crucial for the appropriate use of HRT. …
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日本臨床 70(10), 1660-1665, 2012-10
NAID 40019438272

Related Pictures

★リンクテーブル★

リンク元	「E-カドヘリン」「P-cadherin」「uvomorulin」「N-cadherin」「Eカドヘリン」
拡張検索	「VE-cadherin」
関連記事	「Es」「E」

「E-カドヘリン」

Cadherin 1, type 1, E-cadherin (epithelial)
	; PDB rendering based on 1i7w.
Available structures
PDB	Ortholog search: PDBe, RCSB
List of PDB id codes
	1O6S, 2O72, 2OMT, 2OMU, 2OMV, 2OMX, 2OMY, 2OMZ, 3FF7, 3FF8, 3L6X, 3L6Y
Identifiers
Symbols	CDH1 ; Arc-1; CD324; CDHE; ECAD; LCAM; UVO
External IDs	OMIM: 192090 MGI: 88354 HomoloGene: 20917 GeneCards: CDH1 Gene
Gene ontology
Molecular function	• calcium ion binding; • protein binding; • beta-catenin binding; • protein phosphatase binding; • protein domain specific binding; • ankyrin binding; • GTPase activating protein binding; • gamma-catenin binding; • cell adhesion molecule binding;
Cellular component	• cytoplasm; • endosome; • Golgi apparatus; • trans-Golgi network; • plasma membrane; • cell-cell adherens junction; • focal adhesion; • internal side of plasma membrane; • cell surface; • actin cytoskeleton; • integral to membrane; • aggresome; • basolateral plasma membrane; • lateral plasma membrane; • catenin complex; • cell junction; • node of Ranvier; • lateral loop; • Schmidt-Lanterman incisure; • apical junction complex; • axon terminus; • apical part of cell; • perinuclear region of cytoplasm;
Biological process	• trophectodermal cell differentiation; • apoptotic process; • cellular component disassembly involved in execution phase of apoptosis; • homophilic cell adhesion; • synapse assembly; • sensory perception of sound; • response to toxic substance; • cell-cell adhesion; • protein metabolic process; • pituitary gland development; • negative regulation of cell-cell adhesion; • neuron projection development; • regulation of water loss via skin; • cell junction assembly; • adherens junction organization; • response to drug; • positive regulation of transcription factor import into nucleus; • regulation of cysteine-type endopeptidase activity involved in apoptotic process; • cell-cell junction organization; • positive regulation of transcription, DNA-dependent; • regulation of immune response; • protein homooligomerization; • salivary gland cavitation; • regulation of branching involved in salivary gland morphogenesis; • tight junction assembly; • cellular response to amino acid stimulus; • cellular response to lithium ion; • cellular response to indole-3-methanol; • protein localization to plasma membrane; • cochlea development; • regulation of protein localization to cell surface;
	Sources: Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs
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