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词条 CDH2
释义

  1. Structure

  2. Function

      Role in development    Role in cardiac muscle    Role in neurons    Role in cancer metastasis  

  3. Clinical significance

  4. Interactions

  5. See also

  6. References

  7. Further reading

  8. External links

{{Use dmy dates|date=June 2016}}{{Infobox_gene}}

N-cadherin, also known as Cadherin-2 (CDH2) or neural cadherin (NCAD) is a protein that in humans is encoded by the CDH2 gene.[1][2] CDH2 has also been designated as CD325 (cluster of differentiation 325). N-cadherin is a transmembrane protein expressed in multiple tissues and functions to mediate cell–cell adhesion. In cardiac muscle, N-cadherin is an integral component in adherens junctions residing at intercalated discs, which function to mechanically and electrically couple adjacent cardiomyocytes. While mutations in CDH2 have not thus far been associated with human disease, alterations in expression and integrity of N-cadherin protein has been observed in various forms of disease, including human dilated cardiomyopathy.

Structure

N-cadherin is a protein with molecular weight of 99.7 kDa, and 906 amino acids in length.[3] N-cadherin, a classical cadherin from the cadherin superfamily, is composed of five extracellular cadherin repeats, a transmembrane region and a highly conserved cytoplasmic tail. N-cadherin, as well as other cadherins, interact with N-cadherin on an adjacent cell in an anti-parallel conformation, thus creating a linear, adhesive "zipper" between cells.[4]

Function

N-cadherin, originally named for its role in neural tissue, plays a role in neurons and later was found to also play a role in cardiac muscle and in cancer metastasis. N-cadherin is a transmembrane, homophilic glycoprotein belonging to the calcium-dependent cell adhesion molecule family. These proteins have extracellular domains that mediate homophilic interactions between adjacent cells, and C-terminal, cytoplasmic tails that mediate binding to catenins, which in turn interact with

the actin cytoskeleton.[5][6][7]

Role in development

N-cadherin plays a role in development as a calcium dependent cell–cell adhesion glycoprotein that functions during gastrulation and is required for establishment of left-right asymmetry.[8]

N-cadherin is widely expressed in the embryo post-implantation, showing high levels in the mesoderm with sustained expression through adulthood.[9] N-cadherin mutation during development has the most significant effect on cell adhesion in the primitive heart; dissociated myocytes and abnormal heart tube development occur.[10] N-cadherin plays a role in the development of the vertebrate heart at the transition of epithelial cells to trabecular and compact myocardial cell layer formation.[11] An additional study showed that myocytes expressing a dominant negative N-cadherin mutant showed significant abnormalities in myocyte distribution and migration towards the endocardium, resulting in defects in trabecular formation within the myocardium.[12][13]

Role in cardiac muscle

In cardiac muscle, N-cadherin is found at intercalated disc structures which provide end-on cell–cell connections that facilitate mechanical and electrical coupling between adjacent cardiomyocytes. Within intercalated discs are three types of junctions: adherens junctions, desmosomes and gap junctions;[14] N-cadherin is an essential component in adherens junctions, which enables cell–cell adhesion and force transmission across the sarcolemma.[15] N-cadherin complexed to catenins has been described as a master regulator of intercalated disc function.[16] N-cadherin appears at cell–cell junctions prior to gap junction formation,[17][18] and is critical for normal myofibrillogenesis.[19] Expression of a mutant form of N-cadherin harboring a large deletion in the extracellular domain inhibited the function of endogenous N-cadherin in adult ventricular cardiomyocytes, and neighboring cardiomyocytes lost cell–cell contact and gap junction plaques as well.[20]

Mouse models employing transgenesis have highlighted the function of N-cadherin in cardiac muscle. Mice with altered expression of N-cadherin and/or E-cadherin showed a dilated cardiomyopathy phenotype, likely due to malfunction of intercalated discs.[21] In agreement with this, mice with ablation of N-cadherin in adult hearts via a cardiac-specific tamoxifen-inducible Cre N-cadherin transgene showed disrupted assembly of intercalated discs, dilated cardiomyopathy, impaired cardiac function, decreased sarcomere length, increased Z-line thickness, decreases in connexin 43, and a loss in muscular tension. Mice died within two months of transgene expression, mainly due to spontaneous ventricular tachycardia.[22] Further analysis of N-cadherin knockout mice revealed that the arrhythmias were likely due to ion channel remodeling and aberrant Kv1.5 channel function. These animals showed a prolonged action potential duration, reduced density of inward rectifier potassium channel and decreased expression of Kv1.5, KCNE2 and cortactin combined with disrupted actin cytoskeleton at the sarcolemma.[23]

Role in neurons

In neural cells, at certain central nervous system synapses, presynaptic to postsynaptic adhesion is mediated at least in part by N-cadherin.[24] N-cadherins interact with catenins to play an important role in learning and memory (For full article see Cadherin-catenin complex in learning and memory).

Role in cancer metastasis

N-Cadherin is commonly found in cancer cells and provides a mechanism for transendothelial migration. When a cancer cell adheres to the endothelial cells of a blood vessel it up-regulates the src kinase pathway, which phosphorylates beta-catenins attached to both N-cadherin (this protein) and E-cadherins. This causes the intercellular connection between two adjacent endothelial cells to fail and allows the cancer cell to slip through.[25]

Clinical significance

Mutations in CDH2 have not been conclusively linked to any human disorders. One study investigating genetic underpinnings of obsessive-compulsive disorder and Tourette disorder found that while CDH2 variants are likely not disease-causing as single entities, they may confer risk when examined as part of a panel of related cell–cell adhesion genes.[26] Further studies in larger cohorts will be required to unequivocally determine this.

In human dilated cardiomyopathy, it was shown that N-cadherin expression was enhanced and arranged in a disarrayed fashion, suggesting that disorganization of N-cadherin protein in heart disease may be a component of remodeling.[27]

Interactions

CDH2 has been shown to interact with:

{{div col|colwidth=20em}}
  • Beta-catenin,[28][29]
  • CDH11,[28]
  • type IIb RPTPs including PTPmu (CTNND1),[28][29]
  • CTNNA1,[28][29]
  • LRRC7,[30]
  • PTPRM)[31][32]
  • PTPrho (PTPRT),[33] and
  • Plakoglobin.[28][34]
  • XIRP1[35]
  • SCARB2[36]
{{Div col end}}

See also

  • ADH-1

References

1. ^{{cite journal | vauthors = Walsh FS, Barton CH, Putt W, Moore SE, Kelsell D, Spurr N, Goodfellow PN | title = N-cadherin gene maps to human chromosome 18 and is not linked to the E-cadherin gene | journal = J. Neurochem. | volume = 55 | issue = 3 | pages = 805–12 | date = September 1990 | pmid = 2384753 | doi = 10.1111/j.1471-4159.1990.tb04563.x | url = }}
2. ^{{cite journal | vauthors = Reid RA, Hemperly JJ | title = Human N-cadherin: nucleotide and deduced amino acid sequence | journal = Nucleic Acids Res. | volume = 18 | issue = 19 | pages = 5896 | date = October 1990 | pmid = 2216790 | pmc = 332345 | doi = 10.1093/nar/18.19.5896 | url = }}
3. ^{{cite web|title=Protein sequence of human CDH2 (Uniprot ID: P19022)|url=http://www.heartproteome.org/copa/ProteinInfo.aspx?QType=Protein%20ID&QValue=P19022|website=Cardiac Organellar Protein Atlas Knowledgebase (COPaKB)|accessdate=20 July 2015|archive-url=https://web.archive.org/web/20150924025519/http://www.heartproteome.org/copa/ProteinInfo.aspx?QType=Protein%20ID&QValue=P19022#|archive-date=24 September 2015|dead-url=yes|df=dmy-all}}
4. ^{{cite journal | vauthors = Shapiro L, Fannon AM, Kwong PD, Thompson A, Lehmann MS, Grübel G, Legrand JF, Als-Nielsen J, Colman DR, Hendrickson WA | title = Structural basis of cell–cell adhesion by cadherins | journal = Nature | volume = 374 | issue = 6520 | pages = 327–37 | date = March 1995 | pmid = 7885471 | doi = 10.1038/374327a0 | url = http://orbit.dtu.dk/en/publications/structural-basis-of-cellcell-adhesion-by-cadherins(ec8eb34d-6db6-4bfb-8d7c-a5de4245c383).html }}
5. ^{{cite journal | vauthors = Buxton RS, Magee AI | title = Structure and interactions of desmosomal and other cadherins | journal = Seminars in Cell Biology | volume = 3 | issue = 3 | pages = 157–67 | date = June 1992 | pmid = 1623205 | doi=10.1016/s1043-4682(10)80012-1}}
6. ^{{cite journal | vauthors = Takeichi M | title = Cadherins: a molecular family important in selective cell–cell adhesion | journal = Annual Review of Biochemistry | volume = 59 | pages = 237–52 | date = 1990 | pmid = 2197976 | doi = 10.1146/annurev.bi.59.070190.001321 }}
7. ^{{cite journal | vauthors = Ozawa M, Baribault H, Kemler R | title = The cytoplasmic domain of the cell adhesion molecule uvomorulin associates with three independent proteins structurally related in different species | journal = The EMBO Journal | volume = 8 | issue = 6 | pages = 1711–7 | date = June 1989 | pmid = 2788574 | pmc=401013| doi = 10.1002/j.1460-2075.1989.tb03563.x }}
8. ^{{cite journal | vauthors = García-Castro MI, Vielmetter E, Bronner-Fraser M | title = N-Cadherin, a cell adhesion molecule involved in establishment of embryonic left-right asymmetry | journal = Science | volume = 288 | issue = 5468 | pages = 1047–51 | date = May 2000 | pmid = 10807574 | doi=10.1126/science.288.5468.1047}}
9. ^{{cite journal | vauthors = Angst BD, Khan LU, Severs NJ, Whitely K, Rothery S, Thompson RP, Magee AI, Gourdie RG | title = Dissociated spatial patterning of gap junctions and cell adhesion junctions during postnatal differentiation of ventricular myocardium | journal = Circulation Research | volume = 80 | issue = 1 | pages = 88–94 | date = January 1997 | pmid = 8978327 | doi=10.1161/01.res.80.1.88}}
10. ^{{cite journal | vauthors = Radice GL, Rayburn H, Matsunami H, Knudsen KA, Takeichi M, Hynes RO | title = Developmental defects in mouse embryos lacking N-cadherin | journal = Developmental Biology | volume = 181 | issue = 1 | pages = 64–78 | date = January 1997 | pmid = 9015265 | doi = 10.1006/dbio.1996.8443 }}
11. ^{{cite journal | vauthors = Kostetskii I, Moore R, Kemler R, Radice GL | title = Differential adhesion leads to segregation and exclusion of N-cadherin-deficient cells in chimeric embryos | journal = Developmental Biology | volume = 234 | issue = 1 | pages = 72–9 | date = June 2001 | pmid = 11356020 | doi = 10.1006/dbio.2001.0250 }}
12. ^{{cite journal | vauthors = Linask KK, Knudsen KA, Gui YH | title = N-cadherin-catenin interaction: necessary component of cardiac cell compartmentalization during early vertebrate heart development | journal = Developmental Biology | volume = 185 | issue = 2 | pages = 148–64 | date = May 1997 | pmid = 9187080 | doi = 10.1006/dbio.1997.8570 }}
13. ^{{cite journal | vauthors = Ong LL, Kim N, Mima T, Cohen-Gould L, Mikawa T | title = Trabecular myocytes of the embryonic heart require N-cadherin for migratory unit identity | journal = Developmental Biology | volume = 193 | issue = 1 | pages = 1–9 | date = January 1998 | pmid = 9466883 | doi = 10.1006/dbio.1997.8775 }}
14. ^{{cite journal | vauthors = Peters NS, Severs NJ, Rothery SM, Lincoln C, Yacoub MH, Green CR | title = Spatiotemporal relation between gap junctions and fascia adherens junctions during postnatal development of human ventricular myocardium | journal = Circulation | volume = 90 | issue = 2 | pages = 713–25 | date = August 1994 | pmid = 8044940 | doi=10.1161/01.cir.90.2.713}}
15. ^{{cite journal | vauthors = Forbes MS, Sperelakis N | title = Intercalated discs of mammalian heart: a review of structure and function | journal = Tissue & Cell | volume = 17 | issue = 5 | pages = 605–48 | date = 1985 | pmid = 3904080 | doi=10.1016/0040-8166(85)90001-1}}
16. ^{{cite journal|last1=Vite|first1=A|last2=Radice|first2=GL|title=N-cadherin/catenin complex as a master regulator of intercalated disc function.|journal=Cell Communication & Adhesion|date=June 2014|volume=21|issue=3|pages=169–79|pmid=24766605|pmc=6054126|doi=10.3109/15419061.2014.908853}}
17. ^{{cite journal | vauthors = Zuppinger C, Schaub MC, Eppenberger HM | title = Dynamics of early contact formation in cultured adult rat cardiomyocytes studied by N-cadherin fused to green fluorescent protein | journal = Journal of Molecular and Cellular Cardiology | volume = 32 | issue = 4 | pages = 539–55 | date = April 2000 | pmid = 10756112 | doi = 10.1006/jmcc.1999.1086 }}
18. ^{{cite journal|last1=Dou|first1=JP|last2=Jiao|first2=B|last3=Sheng|first3=JJ|last4=Yu|first4=ZB|title=[Dynamic assembly of intercalated disc during postnatal development in the rat myocardium].|journal=Sheng li xue bao : [Acta Physiologica Sinica]|date=25 October 2014|volume=66|issue=5|pages=569–74|pmid=25332002}}
19. ^{{cite journal | vauthors = Goncharova EJ, Kam Z, Geiger B | title = The involvement of adherens junction components in myofibrillogenesis in cultured cardiac myocytes | journal = Development | volume = 114 | issue = 1 | pages = 173–83 | date = January 1992 | pmid = 1576958 }}
20. ^{{cite journal | vauthors = Hertig CM, Eppenberger-Eberhardt M, Koch S, Eppenberger HM | title = N-cadherin in adult rat cardiomyocytes in culture. I. Functional role of N-cadherin and impairment of cell–cell contact by a truncated N-cadherin mutant | journal = Journal of Cell Science | volume = 109 | pages = 1–10 | date = January 1996 | pmid = 8834785 | issue=1}}
21. ^{{cite journal | vauthors = Ferreira-Cornwell MC, Luo Y, Narula N, Lenox JM, Lieberman M, Radice GL | title = Remodeling the intercalated disc leads to cardiomyopathy in mice misexpressing cadherins in the heart | journal = Journal of Cell Science | volume = 115 | issue = Pt 8 | pages = 1623–34 | date = April 2002 | pmid = 11950881 }}
22. ^{{cite journal | vauthors = Kostetskii I, Li J, Xiong Y, Zhou R, Ferrari VA, Patel VV, Molkentin JD, Radice GL | title = Induced deletion of the N-cadherin gene in the heart leads to dissolution of the intercalated disc structure | journal = Circulation Research | volume = 96 | issue = 3 | pages = 346–54 | date = February 2005 | pmid = 15662031 | doi = 10.1161/01.RES.0000156274.72390.2c }}
23. ^{{cite journal|last1=Cheng|first1=L|last2=Yung|first2=A|last3=Covarrubias|first3=M|last4=Radice|first4=GL|title=Cortactin is required for N-cadherin regulation of Kv1.5 channel function.|journal=The Journal of Biological Chemistry|date=10 June 2011|volume=286|issue=23|pages=20478–89|pmid=21507952|doi=10.1074/jbc.m111.218560|pmc=3121477}}
24. ^{{cite web | title = Entrez Gene: CDH2 cadherin 2, type 1, N-cadherin (neuronal)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1000| accessdate = }}
25. ^{{cite journal | vauthors = Ramis-Conde I, Chaplain MA, Anderson AR, Drasdo D | title = Multi-scale modelling of cancer cell intravasation: the role of cadherins in metastasis | journal = Phys Biol | volume = 6 | issue = 1 | pages = 016008 | year = 2009 | pmid = 19321920 | doi = 10.1088/1478-3975/6/1/016008 | url = | issn = }}
26. ^{{cite journal|last1=Moya|first1=PR|last2=Dodman|first2=NH|last3=Timpano|first3=KR|last4=Rubenstein|first4=LM|last5=Rana|first5=Z|last6=Fried|first6=RL|last7=Reichardt|first7=LF|last8=Heiman|first8=GA|last9=Tischfield|first9=JA|last10=King|first10=RA|last11=Galdzicka|first11=M|last12=Ginns|first12=EI|last13=Wendland|first13=JR|title=Rare missense neuronal cadherin gene (CDH2) variants in specific obsessive-compulsive disorder and Tourette disorder phenotypes.|journal=European Journal of Human Genetics|date=August 2013|volume=21|issue=8|pages=850–4|pmid=23321619|doi=10.1038/ejhg.2012.245|pmc=3722668}}
27. ^{{cite journal|last1=Tsipis|first1=A|last2=Athanassiadou|first2=AM|last3=Athanassiadou|first3=P|last4=Kavantzas|first4=N|last5=Agrogiannis|first5=G|last6=Patsouris|first6=E|title=Apoptosis-related factors p53, bcl-2 and the defects of force transmission in dilated cardiomyopathy.|journal=Pathology, Research and Practice|date=15 September 2010|volume=206|issue=9|pages=625–30|pmid=20591580|doi=10.1016/j.prp.2010.05.007}}
28. ^1 2 3 4 {{cite journal | vauthors = Straub BK, Boda J, Kuhn C, Schnoelzer M, Korf U, Kempf T, Spring H, Hatzfeld M, Franke WW | title = A novel cell–cell junction system: the cortex adhaerens mosaic of lens fiber cells | journal = J. Cell Sci. | volume = 116 | issue = Pt 24 | pages = 4985–95 | date = December 2003 | pmid = 14625392 | doi = 10.1242/jcs.00815 }}
29. ^1 2 {{cite journal | vauthors = Wahl JK, Kim YJ, Cullen JM, Johnson KR, Wheelock MJ | title = N-cadherin-catenin complexes form prior to cleavage of the proregion and transport to the plasma membrane | journal = J. Biol. Chem. | volume = 278 | issue = 19 | pages = 17269–76 | date = May 2003 | pmid = 12604612 | doi = 10.1074/jbc.M211452200 }}
30. ^{{cite journal | vauthors = Izawa I, Nishizawa M, Ohtakara K, Inagaki M | title = Densin-180 interacts with delta-catenin/neural plakophilin-related armadillo repeat protein at synapses | journal = J. Biol. Chem. | volume = 277 | issue = 7 | pages = 5345–50 | date = February 2002 | pmid = 11729199 | doi = 10.1074/jbc.M110052200 }}
31. ^{{cite journal | vauthors = Brady-Kalnay SM, Rimm DL, Tonks NK | title = Receptor protein tyrosine phosphatase PTPmu associates with cadherins and catenins in vivo | journal = J. Cell Biol. | volume = 130 | issue = 4 | pages = 977–86 | pmid = 7642713 | pmc = 2199947 | doi = 10.1083/jcb.130.4.977| year = 1995 }}
32. ^{{cite journal | vauthors = Brady-Kalnay SM, Mourton T, Nixon JP, Pietz GE, Kinch M, Chen H, Brackenbury R, Rimm DL, Del Vecchio RL, Tonks NK | title = Dynamic interaction of PTPmu with multiple cadherins in vivo | journal = J. Cell Biol. | volume = 141 | issue = 1 | pages = 287–96 | pmid = 9531566 | pmc = 2132733 | doi = 10.1083/jcb.141.1.287| year = 1998 }}
33. ^{{cite journal | vauthors = Besco JA, Hooft van Huijsduijnen R, Frostholm A, Rotter A | title = Intracellular substrates of brain-enriched receptor protein tyrosine phosphatase rho (RPTPrho/PTPRT) | journal = Brain Res. | volume = 1116 | issue = 1 | pages = 50–7 | pmid = 16973135 | doi = 10.1016/j.brainres.2006.07.122 | date=October 2006}}
34. ^{{cite journal | vauthors = Sacco PA, McGranahan TM, Wheelock MJ, Johnson KR | title = Identification of plakoglobin domains required for association with N-cadherin and alpha-catenin | journal = J. Biol. Chem. | volume = 270 | issue = 34 | pages = 20201–6 | date = August 1995 | pmid = 7650039 | doi = 10.1074/jbc.270.34.20201}}
35. ^{{cite journal | vauthors = Sinn HW, Balsamo J, Lilien J, Lin JJ | title = Localization of the novel Xin protein to the adherens junction complex in cardiac and skeletal muscle during development | journal = Developmental Dynamics | volume = 225 | issue = 1 | pages = 1–13 | date = September 2002 | pmid = 12203715 | doi = 10.1002/dvdy.10131 }}
36. ^{{cite journal | vauthors = Schroen B, Leenders JJ, van Erk A, Bertrand AT, van Loon M, van Leeuwen RE, Kubben N, Duisters RF, Schellings MW, Janssen BJ, Debets JJ, Schwake M, Høydal MA, Heymans S, Saftig P, Pinto YM | title = Lysosomal integral membrane protein 2 is a novel component of the cardiac intercalated disc and vital for load-induced cardiac myocyte hypertrophy | journal = The Journal of Experimental Medicine | volume = 204 | issue = 5 | pages = 1227–35 | date = May 2007 | pmid = 17485520 | doi = 10.1084/jem.20070145 | pmc=2118572}}

Further reading

{{refbegin|33em}}
  • {{cite journal | vauthors = Doherty P, Smith P, Walsh FS | title = Shared cell adhesion molecule (CAM) homology domains point to CAMs signalling via FGF receptors | journal = Perspectives on Developmental Neurobiology | volume = 4 | issue = 2–3 | pages = 157–68 | year = 1997 | pmid = 9168198 | doi = }}
  • {{cite journal | vauthors = Makrigiannakis A, Coukos G, Blaschuk O, Coutifaris C | title = Follicular atresia and luteolysis. Evidence of a role for N-cadherin | journal = Ann. N. Y. Acad. Sci. | volume = 900 | issue = | pages = 46–55 | year = 2000 | pmid = 10818391 | doi = 10.1111/j.1749-6632.2000.tb06215.x }}
  • {{cite journal | vauthors = Hazan RB, Qiao R, Keren R, Badano I, Suyama K | title = Cadherin switch in tumor progression | journal = Ann. N. Y. Acad. Sci. | volume = 1014 | issue = | pages = 155–63 | year = 2004 | pmid = 15153430 | doi = 10.1196/annals.1294.016 }}
  • {{cite journal | vauthors = Cavallaro U | title = N-cadherin as an invasion promoter: a novel target for antitumor therapy? | journal = Current Opinion in Investigational Drugs | volume = 5 | issue = 12 | pages = 1274–8 | year = 2005 | pmid = 15648948 | doi = }}
  • {{cite journal | vauthors = Salomon D, Ayalon O, Patel-King R, Hynes RO, Geiger B | title = Extrajunctional distribution of N-cadherin in cultured human endothelial cells | journal = J. Cell Sci. | volume = 102 | issue = 1| pages = 7–17 | year = 1992 | pmid = 1500442 | doi = }}
  • {{cite journal | vauthors = Knudsen KA, Wheelock MJ | title = Plakoglobin, or an 83-kD homologue distinct from beta-catenin, interacts with E-cadherin and N-cadherin | journal = J. Cell Biol. | volume = 118 | issue = 3 | pages = 671–9 | year = 1992 | pmid = 1639850 | pmc = 2289540 | doi = 10.1083/jcb.118.3.671 }}
  • {{cite journal | vauthors = Reid RA, Hemperly JJ | title = Human N-cadherin: nucleotide and deduced amino acid sequence | journal = Nucleic Acids Res. | volume = 18 | issue = 19 | pages = 5896 | year = 1990 | pmid = 2216790 | pmc = 332345 | doi = 10.1093/nar/18.19.5896 }}
  • {{cite journal | vauthors = Walsh FS, Barton CH, Putt W, Moore SE, Kelsell D, Spurr N, Goodfellow PN | title = N-cadherin gene maps to human chromosome 18 and is not linked to the E-cadherin gene | journal = J. Neurochem. | volume = 55 | issue = 3 | pages = 805–12 | year = 1990 | pmid = 2384753 | doi = 10.1111/j.1471-4159.1990.tb04563.x }}
  • {{cite journal | vauthors = Selig S, Bruno S, Scharf JM, Wang CH, Vitale E, Gilliam TC, Kunkel LM | title = Expressed cadherin pseudogenes are localized to the critical region of the spinal muscular atrophy gene | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 92 | issue = 9 | pages = 3702–6 | year = 1995 | pmid = 7731968 | pmc = 42029 | doi = 10.1073/pnas.92.9.3702 }}
  • {{cite journal | vauthors = Wallis J, Fox MF, Walsh FS | title = Structure of the human N-cadherin gene: YAC analysis and fine chromosomal mapping to 18q11.2 | journal = Genomics | volume = 22 | issue = 1 | pages = 172–9 | year = 1994 | pmid = 7959764 | doi = 10.1006/geno.1994.1358 }}
  • {{cite journal | vauthors = Andersson AM, Edvardsen K, Skakkebaek NE | title = Expression and localization of N- and E-cadherin in the human testis and epididymis | journal = Int. J. Androl. | volume = 17 | issue = 4 | pages = 174–80 | year = 1995 | pmid = 7995652 | doi = 10.1111/j.1365-2605.1994.tb01239.x }}
  • {{cite journal | vauthors = Matsuyoshi N, Imamura S | title = Multiple cadherins are expressed in human fibroblasts | journal = Biochem. Biophys. Res. Commun. | volume = 235 | issue = 2 | pages = 355–8 | year = 1997 | pmid = 9199196 | doi = 10.1006/bbrc.1997.6707 }}
  • {{cite journal | vauthors = Navarro P, Ruco L, Dejana E | title = Differential localization of VE- and N-cadherins in human endothelial cells: VE-cadherin competes with N-cadherin for junctional localization | journal = J. Cell Biol. | volume = 140 | issue = 6 | pages = 1475–84 | year = 1998 | pmid = 9508779 | pmc = 2132661 | doi = 10.1083/jcb.140.6.1475 }}
  • {{cite journal | vauthors = Gaidar YA, Lepekhin EA, Sheichetova GA, Witt M | title = Distribution of N-cadherin and NCAM in neurons and endocrine cells of the human embryonic and fetal gastroenteropancreatic system | journal = Acta Histochem. | volume = 100 | issue = 1 | pages = 83–97 | year = 1998 | pmid = 9542583 | doi = 10.1016/s0065-1281(98)80008-1}}
  • {{cite journal | vauthors = Kremmidiotis G, Baker E, Crawford J, Eyre HJ, Nahmias J, Callen DF | title = Localization of human cadherin genes to chromosome regions exhibiting cancer-related loss of heterozygosity | journal = Genomics | volume = 49 | issue = 3 | pages = 467–71 | year = 1998 | pmid = 9615235 | doi = 10.1006/geno.1998.5281 }}
  • {{cite journal | vauthors = Lu Q, Paredes M, Medina M, Zhou J, Cavallo R, Peifer M, Orecchio L, Kosik KS | title = delta-catenin, an adhesive junction-associated protein that promotes cell scattering | journal = J. Cell Biol. | volume = 144 | issue = 3 | pages = 519–32 | year = 1999 | pmid = 9971746 | pmc = 2132907 | doi = 10.1083/jcb.144.3.519 }}
  • {{cite journal | vauthors = Shan WS, Tanaka H, Phillips GR, Arndt K, Yoshida M, Colman DR, Shapiro L | title = Functional cis-heterodimers of N- and R-cadherins | journal = J. Cell Biol. | volume = 148 | issue = 3 | pages = 579–90 | year = 2000 | pmid = 10662782 | pmc = 2174798 | doi = 10.1083/jcb.148.3.579 }}
  • {{cite journal | vauthors = Husi H, Ward MA, Choudhary JS, Blackstock WP, Grant SG | title = Proteomic analysis of NMDA receptor-adhesion protein signaling complexes | journal = Nat. Neurosci. | volume = 3 | issue = 7 | pages = 661–9 | year = 2000 | pmid = 10862698 | doi = 10.1038/76615 }}
{{refend}}

External links

  • {{MeshName|CDH2+protein,+human}}
  • {{UCSC genome browser|CDH2}}
  • {{UCSC gene details|CDH2}}
{{NLM content}}{{PDB Gallery|geneid=1000}}{{Clusters of differentiation}}{{Cell adhesion molecules}}

1 : Clusters of differentiation
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