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Cadherin 5, type 2 (vascular endothelium)
Symbols CDH5 ; 7B4; CD144
External IDs OMIM601120 MGI105057 HomoloGene1359 GeneCards: CDH5 Gene
RNA expression pattern
PBB GE CDH5 204677 at tn.png
More reference expression data
Species Human Mouse
Entrez 1003 12562
Ensembl ENSG00000179776 ENSMUSG00000031871
UniProt P33151 P55284
RefSeq (mRNA) NM_001114117 NM_009868
RefSeq (protein) NP_001786 NP_033998
Location (UCSC) Chr 16:
66.4 – 66.44 Mb
Chr 8:
104.1 – 104.14 Mb
PubMed search [1] [2]

Cadherin 5, type 2 or VE-cadherin (vascular endothelial) also known as CD144 (Cluster of Differentiation 144), is a type of cadherin. It is encoded by the human gene CDH5.[1]


VE-cadherin is a classical cadherin from the cadherin superfamily and the 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. 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. Functioning as a classic cadherin by imparting to cells the ability to adhere in a homophilic manner, the protein may play an important role in endothelial cell biology through control of the cohesion and organization of the intercellular junctions.[2]

Integrity of intercellular junctions is a major determinant of permeability of the endothelium, and the VE-cadherin-based adherens junction is thought to be particularly important. VE-cadherin is known to be required for maintaining a restrictive endothelial barrier – early studies using blocking antibodies to VE-cadherin increased monolayer permeability in cultured cells[3] and resulted in interstitial edema and hemorrhage in vivo.[4]

VE-cadherin is indispensable for proper vascular development – there have been two transgenic mouse models of VE-cadherin deficiency, both embryonic lethal due to vascular defects.[5][6] Further studies using one of these models revealed that although vasculogenesis occurred, nascent vessels collapsed or disassembled in the absence of VE-cadherin.[7] Therefore it was concluded that VE-cadherin serves the purpose of maintaining newly formed vessels.


VE-cadherin has been shown to interact with:

See also[edit]


  1. ^ Suzuki S, Sano K, Tanihara H (April 1991). "Diversity of the cadherin family: evidence for eight new cadherins in nervous tissue". Cell Regul. 2 (4): 261–70. doi:10.1091/mbc.2.4.261. PMC 361775. PMID 2059658. 
  2. ^ "Entrez Gene: CDH5 cadherin 5, type 2, VE-cadherin (vascular epithelium)". 
  3. ^ Corada M, Liao F, Lindgren M, Lampugnani M, Breviario F, Frank R et al. (March 2001). "Monoclonal antibodies directed to different regions of vascular endothelial cadherin extracellular domain affect adhesion and clustering of the protein and modulate endothelial permeability". Blood 97 (6): 1679–84. doi:10.1182/blood.V97.6.1679. PMID 11238107. 
  4. ^ Corada M, Zanetta L, Orsenigo F, Breviario F, Lampugnani M, Bernasconi S et al. (August 2002). "A monoclonal antibody to vascular endothelial-cadherin inhibits tumor angiogenesis without side effects on endothelial permeability". Blood 100 (3): 905–11. doi:10.1182/blood.V100.3.905. PMID 12130501. 
  5. ^ Carmeliet P, Lampugnani M, Moons L, Breviario F, Compernolle V, Bono F et al. (July 1999). "Targeted deficiency or cytosolic truncation of the VE-cadherin gene in mice impairs VEGF-mediated endothelial survival and angiogenesis". Cell 98 (2): 147–57. doi:10.1016/S0092-8674(00)81010-7. PMID 10428027. 
  6. ^ Gory-Fauré S, Prandini M, Pointu H, Roullot V, Pignot-Paintrand I, Vernet M et al. (May 1999). "Role of vascular endothelial-cadherin in vascular morphogenesis". Development 126 (10): 2093–102. PMID 10207135. 
  7. ^ Crosby C, Fleming P, Argraves W, Corada M, Zanetta L, Dejana E et al. (April 2005). "VE-cadherin is not required for the formation of nascent blood vessels but acts to prevent their disassembly". Blood 105 (7): 2771–6. doi:10.1182/blood-2004-06-2244. PMID 15604224. 
  8. ^ a b c Lewalle J, Bajou K, Desreux J, Mareel M, Dejana E, Noël A et al. (Dec 1997). "Alteration of interendothelial adherens junctions following tumor cell-endothelial cell interaction in vitro". Exp. Cell Res. 237 (2): 347–56. doi:10.1006/excr.1997.3799. PMID 9434630. 
  9. ^ a b c Shasby D, Ries D, Shasby S, Winter M (Jun 2002). "Histamine stimulates phosphorylation of adherens junction proteins and alters their link to vimentin". Am. J. Physiol. Lung Cell Mol. Physiol. 282 (6): L1330–8. doi:10.1152/ajplung.00329.2001 (inactive 2015-01-01). PMID 12003790. 
  10. ^ Nawroth R, Poell G, Ranft A, Kloep S, Samulowitz U, Fachinger G et al. (Sep 2002). "VE-PTP and VE-cadherin ectodomains interact to facilitate regulation of phosphorylation and cell contacts". EMBO J. 21 (18): 4885–95. doi:10.1093/emboj/cdf497. PMC 126293. PMID 12234928. 
  11. ^ Ferber A, Yaen C, Sarmiento E, Martinez J (Mar 2002). "An octapeptide in the juxtamembrane domain of VE-cadherin is important for p120ctn binding and cell proliferation". Exp. Cell Res. 274 (1): 35–44. doi:10.1006/excr.2001.5436. PMID 11855855. 
  12. ^ Lampugnani M, Corada M, Andriopoulou P, Esser S, Risau W, Dejana E (Sep 1997). "Cell confluence regulates tyrosine phosphorylation of adherens junction components in endothelial cells". J. Cell. Sci. 110 (17): 2065–77. PMID 9378757. 
  13. ^ Sui X, Kiser T, Hyun S, Angelini D, Del Vecchio R, Young B et al. (2005). "Receptor protein tyrosine phosphatase micro regulates the paracellular pathway in human lung microvascular endothelia.". Am J Pathol 166 (4): 1247–58. doi:10.1016/s0002-9440(10)62343-7. PMC 1602370. PMID 15793303. 
  14. ^ Besco J, Hooft van Huijsduijnen R, Frostholm A, Rotter A (2006). "Intracellular substrates of brain-enriched receptor protein tyrosine phosphatase rho (RPTPrho/PTPRT).". Brain Res 1116 (1): 50–7. doi:10.1016/j.brainres.2006.07.122. PMID 16973135. 

Further reading[edit]

External links[edit]

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