CDH3 (gene)

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Cadherin 3, type 1, P-cadherin (placental)
Identifiers
Symbols CDH3 ; CDHP; HJMD; PCAD
External IDs OMIM114021 MGI88356 HomoloGene20425 GeneCards: CDH3 Gene
RNA expression pattern
PBB GE CDH3 203256 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 1001 12560
Ensembl ENSG00000062038 ENSMUSG00000061048
UniProt P22223 P10287
RefSeq (mRNA) NM_001793 NM_001037809
RefSeq (protein) NP_001784 NP_001032898
Location (UCSC) Chr 16:
68.67 – 68.76 Mb
Chr 8:
106.51 – 106.56 Mb
PubMed search [1] [2]

Cadherin-3, also known as P-Cadherin, is a protein that in humans is encoded by the CDH3 gene.[1][2]

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. This gene is located in a six-cadherin cluster in a region on the long arm of chromosome 16 that is involved in loss of heterozygosity events in breast and prostate cancer. In addition, aberrant expression of this protein is observed in cervical adenocarcinomas. Mutations in this gene have been associated with congential hypotrichosis with juvenile macular dystrophy.[2]

Interactions[edit]

CDH3 (gene) has been shown to interact with CDH1,[3] Beta-catenin,[3][4] Plakoglobin,[3] Nephrin[5] and Catenin (cadherin-associated protein), alpha 1.[3][4]

See also[edit]

References[edit]

  1. ^ Kaupmann K, Becker-Follmann J, Scherer G, Jockusch H, Starzinski-Powitz A (December 1992). "The gene for the cell adhesion molecule M-cadherin maps to mouse chromosome 8 and human chromosome 16q24.1-qter and is near the E-cadherin (uvomorulin) locus in both species". Genomics 14 (2): 488–90. doi:10.1016/S0888-7543(05)80247-2. PMID 1427864. 
  2. ^ a b "Entrez Gene: CDH3 cadherin 3, type 1, P-cadherin (placental)". 
  3. ^ a b c d Klingelhöfer, J; Troyanovsky R B; Laur O Y; Troyanovsky S (August 2000). "Amino-terminal domain of classic cadherins determines the specificity of the adhesive interactions". J. Cell. Sci. (ENGLAND) 113 (16): 2829–36. ISSN 0021-9533. PMID 10910767. 
  4. ^ a b Schmeiser, K; Grand R J (April 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. 
  5. ^ Lehtonen, Sanna; Lehtonen Eero; Kudlicka Krystyna; Holthöfer Harry; Farquhar Marilyn G (September 2004). "Nephrin forms a complex with adherens junction proteins and CASK in podocytes and in Madin-Darby canine kidney cells expressing nephrin". Am. J. Pathol. (United States) 165 (3): 923–36. doi:10.1016/S0002-9440(10)63354-8. ISSN 0002-9440. PMC 1618613. PMID 15331416. 

Further reading[edit]

  • Bauer K, Gosau M, Reinders J, Oefner P, Reichert TE, Bauer R (2013). "Presenilin 1/γ-secretase modulates P-cadherin processing and influences cell adhesion in oral squamous cell carcinoma cell lines.". Carcinogenesis 5 (11): 2622–8. doi:10.1093/carcin/bgt211. PMID 23740836. 

External links[edit]