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CDH1 (gene): Wikis


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Cadherin 1, type 1, E-cadherin (epithelial)

PDB rendering based on 1i7w.
Available structures
1i7w, 1i7x, 1o6s, 2omv, 2omy
Symbols CDH1; Arc-1; CD324; CDHE; ECAD; LCAM; UVO
External IDs OMIM192090 MGI88354 HomoloGene20917 GeneCards: CDH1 Gene
RNA expression pattern
PBB GE CDH1 201131 s at tn.png
PBB GE CDH1 201130 s at tn.png
More reference expression data
Species Human Mouse
Entrez 999 12550
Ensembl ENSG00000039068 ENSMUSG00000000303
UniProt P12830 Q4KML8
RefSeq (mRNA) NM_004360 NM_009864
RefSeq (protein) NP_004351 NP_033994
Location (UCSC) Chr 16:
67.33 - 67.43 Mb
Chr 8:
109.49 - 109.56 Mb
PubMed search [1] [2]

Cadherin-1 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]

This gene is a classical cadherin from 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 cancer. 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]



CDH1 (gene) has been shown to interact with Beta-catenin,[5][6][7][8][9][10][11][12][13][14][15][16][17][18][19][20][21][22][23][24][25][26][27] C-Met,[5] HDAC1,[28] Histone deacetylase 2,[28] FOXM1,[29] CTNND1,[30][31][9][11][32][16][23][33] CDH3,[34] IQGAP1,[35] CDC27,[36] FYN,[16] Plakoglobin,[9][11][37][38][39] CDON,[17] Vinculin,[8][11] Catenin (cadherin-associated protein), alpha 1[9][18][19][20][26] and NEDD9.[40]

See also


  1. ^ Huntsman DG, Caldas C (Mar 1999). "Assignment1 of the E-cadherin gene (CDH1) to chromosome 16q22.1 by radiation hybrid mapping". Cytogenet Cell Genet 83 (1-2): 82–3. PMID 9925936. 
  2. ^ Semb H, Christofori G (December 1998). "The tumor-suppressor function of E-cadherin". Am. J. Hum. Genet. 63 (6): 1588–93. doi:10.1086/302173. PMID 9837810.& PMC 1377629. 
  3. ^ Wong AS, Gumbiner BM (June 2003). "Adhesion-independent mechanism for suppression of tumor cell invasion by E-cadherin". J. Cell Biol. 161 (6): 1191–203. doi:10.1083/jcb.200212033. PMID 12810698.& PMC 2173007. 
  4. ^ "Entrez Gene: CDH1 cadherin 1, type 1, E-cadherin (epithelial)". 
  5. ^ a b Davies, G; Jiang W G, Mason M D (Apr. 2001). "HGF/SF modifies the interaction between its receptor c-Met, and the E-cadherin/catenin complex in prostate cancer cells". Int. J. Mol. Med. (Greece) 7 (4): 385–8. ISSN 1107-3756. PMID 11254878. 
  6. ^ Kucerová, D; Sloncová E, Tuhácková Z, Vojtechová M, Sovová V (Dec. 2001). "Expression and interaction of different catenins in colorectal carcinoma cells". Int. J. Mol. Med. (Greece) 8 (6): 695–8. ISSN 1107-3756. PMID 11712088. 
  7. ^ Oyama, T; Kanai Y, Ochiai A, Akimoto S, Oda T, Yanagihara K, Nagafuchi A, Tsukita S, Shibamoto S, Ito F (Dec. 1994). "A truncated beta-catenin disrupts the interaction between E-cadherin and alpha-catenin: a cause of loss of intercellular adhesiveness in human cancer cell lines". Cancer Res. (UNITED STATES) 54 (23): 6282–7. ISSN 0008-5472. PMID 7954478. 
  8. ^ a b Hazan, R B; Kang L, Roe S, Borgen P I, Rimm D L (Dec. 1997). "Vinculin is associated with the E-cadherin adhesion complex". J. Biol. Chem. (UNITED STATES) 272 (51): 32448–53. ISSN 0021-9258. PMID 9405455. 
  9. ^ a b c d Kinch, M S; Clark G J, Der C J, Burridge K (Jul. 1995). "Tyrosine phosphorylation regulates the adhesions of ras-transformed breast epithelia". J. Cell Biol. (UNITED STATES) 130 (2): 461–71. ISSN 0021-9525. PMID 7542250. 
  10. ^ Jiang, Ming-Chung; Liao Ching-Fong, Tai Chia-Chen (Jun. 2002). "CAS/CSE 1 stimulates E-cadhrin-dependent cell polarity in HT-29 human colon epithelial cells". Biochem. Biophys. Res. Commun. (United States) 294 (4): 900–5. doi:10.1016/S0006-291X(02)00551-X. ISSN 0006-291X. PMID 12061792. 
  11. ^ a b c d Hazan, R B; Norton L (Apr. 1998). "The epidermal growth factor receptor modulates the interaction of E-cadherin with the actin cytoskeleton". J. Biol. Chem. (UNITED STATES) 273 (15): 9078–84. ISSN 0021-9258. PMID 9535896. 
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  13. ^ Li, Y; Bharti A, Chen D, Gong J, Kufe D (Dec. 1998). "Interaction of glycogen synthase kinase 3beta with the DF3/MUC1 carcinoma-associated antigen and beta-catenin". Mol. Cell. Biol. (UNITED STATES) 18 (12): 7216–24. ISSN 0270-7306. PMID 9819408. 
  14. ^ Wendeler, M W; Praus M, Jung R, Hecking M, Metzig C, Gessner R (Apr. 2004). "Ksp-cadherin is a functional cell-cell adhesion molecule related to LI-cadherin". Exp. Cell Res. (United States) 294 (2): 345–55. doi:10.1016/j.yexcr.2003.11.022. ISSN 0014-4827. PMID 15023525. 
  15. ^ Shibata, Tatsuhiro; Chuma Makoto, Kokubu Akiko, Sakamoto Michiie, Hirohashi Setsuo (Jul. 2003). "EBP50, a beta-catenin-associating protein, enhances Wnt signaling and is over-expressed in hepatocellular carcinoma". Hepatology (United States) 38 (1): 178–86. doi:10.1053/jhep.2003.50270. ISSN 0270-9139. PMID 12830000. 
  16. ^ a b c Piedra, Jose; Miravet Susana, Castaño Julio, Pálmer Héctor G, Heisterkamp Nora, García de Herreros Antonio, Duñach Mireia (Apr. 2003). "p120 Catenin-associated Fer and Fyn tyrosine kinases regulate beta-catenin Tyr-142 phosphorylation and beta-catenin-alpha-catenin Interaction". Mol. Cell. Biol. (United States) 23 (7): 2287–97. ISSN 0270-7306. PMID 12640114. 
  17. ^ a b Kang, Jong-Sun; Feinleib Jessica L, Knox Sarah, Ketteringham Michael A, Krauss Robert S (Apr. 2003). "Promyogenic members of the Ig and cadherin families associate to positively regulate differentiation". Proc. Natl. Acad. Sci. U.S.A. (United States) 100 (7): 3989–94. doi:10.1073/pnas.0736565100. ISSN 0027-8424. PMID 12634428. 
  18. ^ a b Oneyama, Chitose; Nakano Hirofumi, Sharma Sreenath V (Mar. 2002). "UCS15A, a novel small molecule, SH3 domain-mediated protein-protein interaction blocking drug". Oncogene (England) 21 (13): 2037–50. doi:10.1038/sj.onc.1205271. ISSN 0950-9232. PMID 11960376. 
  19. ^ a b Navarro, P; Lozano E, Cano A (Aug. 1993). "Expression of E- or P-cadherin is not sufficient to modify the morphology and the tumorigenic behavior of murine spindle carcinoma cells. Possible involvement of plakoglobin". J. Cell. Sci. (ENGLAND) 105 ( Pt 4): 923–34. ISSN 0021-9533. PMID 8227214. 
  20. ^ a b Takahashi, K; Suzuki K, Tsukatani Y (Jul. 1997). "Induction of tyrosine phosphorylation and association of beta-catenin with EGF receptor upon tryptic digestion of quiescent cells at confluence". Oncogene (ENGLAND) 15 (1): 71–8. doi:10.1038/sj.onc.1201160. ISSN 0950-9232. PMID 9233779. 
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  22. ^ Geng, L; Burrow C R, Li H P, Wilson P D (Dec. 2000). "Modification of the composition of polycystin-1 multiprotein complexes by calcium and tyrosine phosphorylation". Biochim. Biophys. Acta (NETHERLANDS) 1535 (1): 21–35. ISSN 0006-3002. PMID 11113628. 
  23. ^ a b Shibamoto, S; Hayakawa M, Takeuchi K, Hori T, Miyazawa K, Kitamura N, Johnson K R, Wheelock M J, Matsuyoshi N, Takeichi M (Mar. 1995). "Association of p120, a tyrosine kinase substrate, with E-cadherin/catenin complexes". J. Cell Biol. (UNITED STATES) 128 (5): 949–57. ISSN 0021-9525. PMID 7876318. 
  24. ^ Rao, Radhakrishna K; Basuroy Shyamali, Rao Vijay U, Karnaky Jr Karl J, Gupta Akshay (Dec. 2002). "Tyrosine phosphorylation and dissociation of occludin-ZO-1 and E-cadherin-beta-catenin complexes from the cytoskeleton by oxidative stress". Biochem. J. (England) 368 (Pt 2): 471–81. doi:10.1042/BJ20011804. ISSN 0264-6021. PMID 12169098. 
  25. ^ Huber, A H; Weis W I (May. 2001). "The structure of the beta-catenin/E-cadherin complex and the molecular basis of diverse ligand recognition by beta-catenin". Cell (United States) 105 (3): 391–402. ISSN 0092-8674. PMID 11348595. 
  26. ^ a b Schmeiser, K; Grand R J (Apr. 1999). "The fate of E- and P-cadherin during the early stages of apoptosis". Cell Death Differ. (ENGLAND) 6 (4): 377–86. doi:10.1038/sj.cdd.4400504. ISSN 1350-9047. PMID 10381631. 
  27. ^ Pai, Rama; Dunlap Debra, Qing Jing, Mohtashemi Iman, Hotzel Kathy, French Dorothy M (Jul. 2008). "Inhibition of fibroblast growth factor 19 reduces tumor growth by modulating beta-catenin signaling". Cancer Res. (United States) 68 (13): 5086–95. doi:10.1158/0008-5472.CAN-07-2325. PMID 18593907. 
  28. ^ a b Yoon, Young-Mee; Baek Kwan-Hyuck, Jeong Sook-Jung, Shin Hyun-Jin, Ha Geun-Hyoung, Jeon Ae-Hwa, Hwang Sang-Gu, Chun Jang-Soo, Lee Chang-Woo (Sep. 2004). "WD repeat-containing mitotic checkpoint proteins act as transcriptional repressors during interphase". FEBS Lett. (Netherlands) 575 (1-3): 23–9. doi:10.1016/j.febslet.2004.07.089. ISSN 0014-5793. PMID 15388328. 
  29. ^ Laoukili, Jamila; Alvarez-Fernandez Monica, Stahl Marie, Medema René H (Sep. 2008). "FoxM1 is degraded at mitotic exit in a Cdh1-dependent manner". Cell Cycle (United States) 7 (17): 2720–6. PMID 18758239. 
  30. ^ Daniel, J M; Reynolds A B (Sep. 1995). "The tyrosine kinase substrate p120cas binds directly to E-cadherin but not to the adenomatous polyposis coli protein or alpha-catenin". Mol. Cell. Biol. (UNITED STATES) 15 (9): 4819–24. ISSN 0270-7306. PMID 7651399. 
  31. ^ Ireton, Renee C; Davis Michael A, van Hengel Jolanda, Mariner Deborah J, Barnes Kirk, Thoreson Molly A, Anastasiadis Panos Z, Matrisian Linsey, Bundy Linda M, Sealy Linda, Gilbert Barbara, van Roy Frans, Reynolds Albert B (Nov. 2002). "A novel role for p120 catenin in E-cadherin function". J. Cell Biol. (United States) 159 (3): 465–76. doi:10.1083/jcb.200205115. ISSN 0021-9525. PMID 12427869. 
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Further reading

  • Berx G, Becker KF, Höfler H, van Roy F (1998). "Mutations of the human E-cadherin (CDH1) gene.". Hum. Mutat. 12 (4): 226–37. doi:10.1002/(SICI)1098-1004(1998)12:4<226::AID-HUMU2>3.0.CO;2-D. PMID 9744472. 
  • Wijnhoven BP, Dinjens WN, Pignatelli M (2000). "E-cadherin-catenin cell-cell adhesion complex and human cancer.". The British journal of surgery 87 (8): 992–1005. doi:10.1046/j.1365-2168.2000.01513.x. PMID 10931041. 
  • Beavon IR (2000). "The E-cadherin-catenin complex in tumour metastasis: structure, function and regulation.". Eur. J. Cancer 36 (13 Spec No): 1607–20. doi:10.1016/S0959-8049(00)00158-1. PMID 10959047. 
  • Wilson PD (2001). "Polycystin: new aspects of structure, function, and regulation.". J. Am. Soc. Nephrol. 12 (4): 834–45. PMID 11274246. 
  • Chun YS, Lindor NM, Smyrk TC, et al. (2001). "Germline E-cadherin gene mutations: is prophylactic total gastrectomy indicated?". Cancer 92 (1): 181–7. PMID 11443625. 
  • Hazan RB, Qiao R, Keren R, et al. (2004). "Cadherin switch in tumor progression.". Ann. N. Y. Acad. Sci. 1014: 155–63. doi:10.1196/annals.1294.016. PMID 15153430. 
  • Bryant DM, Stow JL (2005). "The ins and outs of E-cadherin trafficking.". Trends Cell Biol. 14 (8): 427–34. doi:10.1016/j.tcb.2004.07.007. PMID 15308209. 
  • Wang HD, Ren J, Zhang L (2004). "CDH1 germline mutation in hereditary gastric carcinoma.". World J. Gastroenterol. 10 (21): 3088–93. PMID 15457549. 
  • Reynolds AB, Carnahan RH (2005). "Regulation of cadherin stability and turnover by p120ctn: implications in disease and cancer.". Semin. Cell Dev. Biol. 15 (6): 657–63. doi:10.1016/j.semcdb.2004.09.003. PMID 15561585. 
  • Moran CJ, Joyce M, McAnena OJ (2005). "CDH1 associated gastric cancer: a report of a family and review of the literature.". Eur J Surg Oncol 31 (3): 259–64. doi:10.1016/j.ejso.2004.12.010. PMID 15780560. 
  • Georgolios A, Batistatou A, Manolopoulos L, Charalabopoulos K (2006). "Role and expression patterns of E-cadherin in head and neck squamous cell carcinoma (HNSCC).". J. Exp. Clin. Cancer Res. 25 (1): 5–14. PMID 16761612. 
  • Renaud-Young M, Gallin WJ (2002). "In the first extracellular domain of E-cadherin, heterophilic interactions, but not the conserved His-Ala-Val motif, are required for adhesion". Journal of Biological Chemistry 277 (42): 39609–39616. PMID 12154084. 

External links

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



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