Open Access Articles- Top Results for CDH2


SymbolsCDH2 ; CD325; CDHN; CDw325; NCAD
External IDsOMIM114020 MGI88355 HomoloGene20424 ChEMBL: 1697669 GeneCards: CDH2 Gene
RNA expression pattern
File:PBB GE CDH2 203440 at tn.png
File:PBB GE CDH2 203441 s at tn.png
More reference expression data
RefSeq (mRNA)NM_001792NM_007664
RefSeq (protein)NP_001783NP_031690
Location (UCSC)Chr 18:
25.53 – 25.76 Mb
Chr 18:
16.59 – 16.81 Mb
PubMed search[1][2]

Cadherin-2 (CDH2), also known as 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).


Cadherin 2 a classical cadherin from the cadherin superfamily. Cadherin 2 is a calcium dependent cell-cell adhesion glycoprotein comprising five extracellular cadherin repeats, a transmembrane region and a highly conserved cytoplasmic tail. The protein functions during gastrulation and is required for establishment of left-right asymmetry. At certain central nervous system synapses, presynaptic to postsynaptic adhesion is mediated at least in part by this gene product.[3]

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.[4]


CDH2 has been shown to interact with:


  1. ^ Walsh FS, Barton CH, Putt W, Moore SE, Kelsell D, Spurr N et al. (September 1990). "N-cadherin gene maps to human chromosome 18 and is not linked to the E-cadherin gene". J. Neurochem. 55 (3): 805–12. PMID 2384753. doi:10.1111/j.1471-4159.1990.tb04563.x. 
  2. ^ Reid RA, Hemperly JJ (October 1990). "Human N-cadherin: nucleotide and deduced amino acid sequence". Nucleic Acids Res. 18 (19): 5896–5896. PMC 332345. PMID 2216790. doi:10.1093/nar/18.19.5896. 
  3. ^ "Entrez Gene: CDH2 cadherin 2, type 1, N-cadherin (neuronal)". 
  4. ^ Ramis-Conde I, Chaplain MA, Anderson AR, Drasdo D (2009). "Multi-scale modelling of cancer cell intravasation: the role of cadherins in metastasis". Phys Biol 6 (1): 016008. PMID 19321920. doi:10.1088/1478-3975/6/1/016008. 
  5. ^ a b c d e Straub BK, Boda J, Kuhn C, Schnoelzer M, Korf U, Kempf T et al. (Dec 2003). "A novel cell-cell junction system: the cortex adhaerens mosaic of lens fiber cells". J. Cell. Sci. 116 (Pt 24): 4985–95. PMID 14625392. doi:10.1242/jcs.00815. 
  6. ^ a b c Wahl JK, Kim YJ, Cullen JM, Johnson KR, Wheelock MJ (May 2003). "N-cadherin-catenin complexes form prior to cleavage of the proregion and transport to the plasma membrane". J. Biol. Chem. 278 (19): 17269–76. PMID 12604612. doi:10.1074/jbc.M211452200. 
  7. ^ Izawa I, Nishizawa M, Ohtakara K, Inagaki M (Feb 2002). "Densin-180 interacts with delta-catenin/neural plakophilin-related armadillo repeat protein at synapses". J. Biol. Chem. 277 (7): 5345–50. PMID 11729199. doi:10.1074/jbc.M110052200. 
  8. ^ Brady-Kalnay SM, Rimm DL, Tonks NK. "Receptor protein tyrosine phosphatase PTPmu associates with cadherins and catenins in vivo". J. Cell Biol. 130 (4): 977–86. PMC 2199947. PMID 7642713. doi:10.1083/jcb.130.4.977. 
  9. ^ Brady-Kalnay SM, Mourton T, Nixon JP, Pietz GE, Kinch M, Chen H et al. "Dynamic interaction of PTPmu with multiple cadherins in vivo". J. Cell Biol. 141 (1): 287–96. PMC 2132733. PMID 9531566. doi:10.1083/jcb.141.1.287. 
  10. ^ Besco JA, Hooft van Huijsduijnen R, Frostholm A, Rotter A. "Intracellular substrates of brain-enriched receptor protein tyrosine phosphatase rho (RPTPrho/PTPRT)". Brain Res. 1116 (1): 50–7. PMID 16973135. doi:10.1016/j.brainres.2006.07.122. 
  11. ^ Sacco PA, McGranahan TM, Wheelock MJ, Johnson KR (Aug 1995). "Identification of plakoglobin domains required for association with N-cadherin and alpha-catenin". J. Biol. Chem. 270 (34): 20201–6. PMID 7650039. doi:10.1074/jbc.270.34.20201. 

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