VE-cadherin

CDH5
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
Aliases CDH5, 7B4, CD144, VE-cadherin, cadherin 5
External IDs MGI: 105057 HomoloGene: 1359 GeneCards: CDH5
RNA expression pattern
More reference expression data
Orthologs
Species Human Mouse
Entrez

1003

12562

Ensembl

ENSG00000179776

ENSMUSG00000031871

UniProt

P33151

P55284

RefSeq (mRNA)

NM_001114117
NM_001795

NM_009868

RefSeq (protein)

NP_001786.2

NP_033998.2

Location (UCSC) Chr 16: 66.37 – 66.4 Mb Chr 8: 104.1 – 104.14 Mb
PubMed search [1] [2]
Wikidata
View/Edit HumanView/Edit Mouse

Cadherin 5, type 2 or VE-cadherin (vascular endothelial cadherin) also known as CD144 (Cluster of Differentiation 144), is a type of cadherin. It is encoded by the human gene CDH5.[3]

Function

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.[4]

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[5] and resulted in interstitial edema and hemorrhage in vivo.[6]

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.[7][8] Further studies using one of these models revealed that although vasculogenesis occurred, nascent vessels collapsed or disassembled in the absence of VE-cadherin.[9] Therefore, it was concluded that VE-cadherin serves the purpose of maintaining newly formed vessels.

Interactions

VE-cadherin has been shown to interact with:

See also

References

  1. ↑ "Human PubMed Reference:".
  2. ↑ "Mouse PubMed Reference:".
  3. ↑ 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 361775Freely accessible. PMID 2059658.
  4. ↑ "Entrez Gene: CDH5 cadherin 5, type 2, VE-cadherin (vascular epithelium)".
  5. ↑ Corada M, Liao F, Lindgren M, Lampugnani MG, Breviario F, Frank R, Muller WA, Hicklin DJ, Bohlen P, Dejana E (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.
  6. ↑ Corada M, Zanetta L, Orsenigo F, Breviario F, Lampugnani MG, Bernasconi S, Liao F, Hicklin DJ, Bohlen P, Dejana E (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.
  7. ↑ Carmeliet P, Lampugnani MG, Moons L, Breviario F, Compernolle V, Bono F, Balconi G, Spagnuolo R, Oosthuyse B, Dewerchin M, Zanetti A, Angellilo A, Mattot V, Nuyens D, Lutgens E, Clotman F, de Ruiter MC, Gittenberger-de Groot A, Poelmann R, Lupu F, Herbert JM, Collen D, Dejana E (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.
  8. ↑ Gory-Fauré S, Prandini MH, Pointu H, Roullot V, Pignot-Paintrand I, Vernet M, Huber P (May 1999). "Role of vascular endothelial-cadherin in vascular morphogenesis". Development. 126 (10): 2093–102. PMID 10207135.
  9. ↑ Crosby CV, Fleming PA, Argraves WS, Corada M, Zanetta L, Dejana E, Drake CJ (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.
  10. 1 2 3 Lewalle JM, Bajou K, Desreux J, Mareel M, Dejana E, Noël A, Foidart JM (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.
  11. 1 2 3 Shasby DM, Ries DR, Shasby SS, Winter MC (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.
  12. ↑ Nawroth R, Poell G, Ranft A, Kloep S, Samulowitz U, Fachinger G, Golding M, Shima DT, Deutsch U, Vestweber D (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 126293Freely accessible. PMID 12234928.
  13. ↑ 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.
  14. ↑ Lampugnani MG, 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.
  15. ↑ Sui XF, Kiser TD, Hyun SW, Angelini DJ, Del Vecchio RL, Young BA, Hasday JD, Romer LH, Passaniti A, Tonks NK, Goldblum SE (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 1602370Freely accessible. PMID 15793303.
  16. ↑ Besco JA, 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

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

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