CDH1 (gene)
From Wikipedia, the free encyclopedia
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Cadherin 1, type 1, E-cadherin (epithelial)
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| PDB rendering based on 1i7w. | ||||||||||||||
| Available structures: 1i7w, 1i7x, 1o6s, 2omv, 2omy | ||||||||||||||
| Identifiers | ||||||||||||||
| Symbol(s) | CDH1; Arc-1; CD324; CDHE; ECAD; LCAM; UVO | |||||||||||||
| External IDs | OMIM: 192090 MGI: 88354 HomoloGene: 20917 | |||||||||||||
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| RNA expression pattern | ||||||||||||||
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| Orthologs | ||||||||||||||
| Human | Mouse | |||||||||||||
| Entrez | 999 | 12550 | ||||||||||||
| Ensembl | ENSG00000039068 | ENSMUSG00000000303 | ||||||||||||
| Uniprot | P12830 | Q4KML8 | ||||||||||||
| Refseq | NM_004360 (mRNA) NP_004351 (protein) |
NM_009864 (mRNA) NP_033994 (protein) |
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| Location | Chr 16: 67.33 - 67.43 Mb | Chr 8: 109.49 - 109.56 Mb | ||||||||||||
| Pubmed search | [1] | [2] | ||||||||||||
Cadherin 1, type 1, E-cadherin (epithelial), also known as CDH1, is a human gene. CDH1 has also been designated as CD324 (cluster of differentiation 324).
This gene is a classical cadherin from the cadherin superfamily. The encoded protein is a calcium dependent cell-cell adhesion glycoprotein comprised 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.[1]
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[edit] See also
[edit] References
[edit] 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:. 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:. 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. 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. PMID 15153430.
- Bryant DM, Stow JL (2005). "The ins and outs of E-cadherin trafficking.". Trends Cell Biol. 14 (8): 427–34. doi:. 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:. 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:. 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.
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This article incorporates text from the United States National Library of Medicine, which is in the public domain.
