VE-cadherin

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Cadherin 5, type 2 (vascular endothelium)
Identifiers
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
Orthologs
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]

Function[edit]

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.

Interactions[edit]

VE-cadherin has been shown to interact with:

See also[edit]

References[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 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. 
  4. ^ 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. 
  5. ^ 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. 
  6. ^ 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. 
  7. ^ 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. 
  8. ^ a b c Lewalle, J M; Bajou K; Desreux J; Mareel M; Dejana E; Noël A; Foidart J M (Dec 1997). "Alteration of interendothelial adherens junctions following tumor cell-endothelial cell interaction in vitro". Exp. Cell Res. (UNITED STATES) 237 (2): 347–56. doi:10.1006/excr.1997.3799. ISSN 0014-4827. PMID 9434630. 
  9. ^ a b c Shasby, D Michael; Ries Dana R; Shasby Sandra S; Winter Michael C (Jun 2002). "Histamine stimulates phosphorylation of adherens junction proteins and alters their link to vimentin". Am. J. Physiol. Lung Cell Mol. Physiol. (United States) 282 (6): L1330–8. doi:10.1152/ajplung.00329.2001 (inactive 2010-07-26). ISSN 1040-0605. PMID 12003790. 
  10. ^ Nawroth, Roman; Poell Gregor; Ranft Alexander; Kloep Stephan; Samulowitz Ulrike; Fachinger Gregor; Golding Matthew; Shima David T; Deutsch Urban; Vestweber Dietmar (Sep 2002). "VE-PTP and VE-cadherin ectodomains interact to facilitate regulation of phosphorylation and cell contacts". EMBO J. (England) 21 (18): 4885–95. doi:10.1093/emboj/cdf497. ISSN 0261-4189. PMC 126293. PMID 12234928. 
  11. ^ Ferber, Andres; Yaen Christopher; Sarmiento Edna; Martinez Jose (Mar 2002). "An octapeptide in the juxtamembrane domain of VE-cadherin is important for p120ctn binding and cell proliferation". Exp. Cell Res. (United States) 274 (1): 35–44. doi:10.1006/excr.2001.5436. ISSN 0014-4827. PMID 11855855. 
  12. ^ Lampugnani, M G; 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. (ENGLAND) 110 (17): 2065–77. ISSN 0021-9533. PMID 9378757. 
  13. ^ Sui XF, Kiser TD, Hyun SW, Angelini DJ, Del Vecchio RL, Young BA 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 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[edit]

External links[edit]

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