VE-カドヘリン、VEカドヘリン
WordNet
- the 22nd letter of the Roman alphabet (同)v
PrepTutorEJDIC
- vanadium の化学記号
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2015/03/24 23:51:12」(JST)
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Cadherin 5, type 2 (vascular endothelium) |
Identifiers |
Symbols |
CDH5 ; 7B4; CD144 |
External IDs |
OMIM: 601120 MGI: 105057 HomoloGene: 1359 GeneCards: CDH5 Gene |
Gene ontology |
Molecular function |
• receptor binding
• calcium ion binding
• protein binding
• beta-catenin binding
• protein phosphatase binding
• ion channel binding
|
Cellular component |
• plasma membrane
• cell-cell junction
• tight junction
• membrane
• integral component of membrane
• cell junction
|
Biological process |
• blood vessel maturation
• homophilic cell adhesion
• negative regulation of cell proliferation
• cell junction assembly
• adherens junction organization
• cell-cell junction organization
• regulation of establishment of cell polarity
|
Sources: Amigo / QuickGO |
|
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_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]
Contents
- 1 Function
- 2 Interactions
- 3 See also
- 4 References
- 5 Further reading
- 6 External links
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.[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
VE-cadherin has been shown to interact with:
- Beta-catenin[8][9]
- Plakoglobin[8][9]
- PTPRB[10]
- Catenin (cadherin-associated protein), alpha 1[8][9]
- CTNND1[11][12]
- PTPmu (PTPRM)[13]
- PTPrho (PTPRT)[14]
See also
- Cluster of differentiation
- Endothelium
References
- ^ 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.
- ^ "Entrez Gene: CDH5 cadherin 5, type 2, VE-cadherin (vascular epithelium)".
- ^ Corada M, Liao F, Lindgren M, Lampugnani MG, 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.
- ^ Corada M, Zanetta L, Orsenigo F, Breviario F, Lampugnani MG, 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.
- ^ Carmeliet P, Lampugnani MG, 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.
- ^ Gory-Fauré S, Prandini MH, 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.
- ^ Crosby CV, Fleming PA, Argraves WS, 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.
- ^ a b c Lewalle JM, 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.
- ^ a b c 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.
- ^ 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.
- ^ 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.
- ^ 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.
- ^ 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.
- ^ 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
- Lampugnani MG, Resnati M, Raiteri M, Pigott R, Pisacane A, Houen G et al. (1992). "A novel endothelial-specific membrane protein is a marker of cell-cell contacts". J. Cell Biol. 118 (6): 1511–22. doi:10.1083/jcb.118.6.1511. PMC 2289607. PMID 1522121.
- Suzuki S, Sano K, Tanihara H (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.
- Breviario F, Caveda L, Corada M, Martin-Padura I, Navarro P, Golay J et al. (1995). "Functional properties of human vascular endothelial cadherin (7B4/cadherin-5), an endothelium-specific cadherin". Arterioscler. Thromb. Vasc. Biol. 15 (8): 1229–39. doi:10.1161/01.ATV.15.8.1229. PMID 7627717.
- Ali J, Liao F, Martens E, Muller WA (1997). "Vascular endothelial cadherin (VE-cadherin): cloning and role in endothelial cell-cell adhesion". Microcirculation (New York, N.Y. : 1994) 4 (2): 267–77. doi:10.3109/10739689709146790. PMID 9219219.
- Lampugnani MG, Corada M, Andriopoulou P, Esser S, Risau W, Dejana E (1997). "Cell confluence regulates tyrosine phosphorylation of adherens junction components in endothelial cells". J. Cell. Sci. 110 (17): 2065–77. PMID 9378757.
- Lewalle JM, Bajou K, Desreux J, Mareel M, Dejana E, Noël A et al. (1998). "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.
- Kremmidiotis G, Baker E, Crawford J, Eyre HJ, Nahmias J, Callen DF (1998). "Localization of human cadherin genes to chromosome regions exhibiting cancer-related loss of heterozygosity". Genomics 49 (3): 467–71. doi:10.1006/geno.1998.5281. PMID 9615235.
- Kowalczyk AP, Navarro P, Dejana E, Bornslaeger EA, Green KJ, Kopp DS et al. (1998). "VE-cadherin and desmoplakin are assembled into dermal microvascular endothelial intercellular junctions: a pivotal role for plakoglobin in the recruitment of desmoplakin to intercellular junctions". J. Cell. Sci. 111 (20): 3045–57. PMID 9739078.
- Kawashima M, Kitagawa M (1999). "An immunohistochemical study of cadherin 5 (VE-cadherin) in vascular endothelial cells in placentas with gestosis". J. Obstet. Gynaecol. Res. 24 (6): 375–84. doi:10.1111/j.1447-0756.1998.tb00112.x. PMID 10063232.
- Carmeliet P, Lampugnani MG, Moons L, Breviario F, Compernolle V, Bono F et al. (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.
- Ukropec JA, Hollinger MK, Salva SM, Woolkalis MJ (2000). "SHP2 association with VE-cadherin complexes in human endothelial cells is regulated by thrombin". J. Biol. Chem. 275 (8): 5983–6. doi:10.1074/jbc.275.8.5983. PMID 10681592.
- Shimoyama Y, Tsujimoto G, Kitajima M, Natori M (2001). "Identification of three human type-II classic cadherins and frequent heterophilic interactions between different subclasses of type-II classic cadherins". Biochem. J. 349 (Pt 1): 159–67. doi:10.1042/0264-6021:3490159. PMC 1221133. PMID 10861224.
- Shaw SK, Bamba PS, Perkins BN, Luscinskas FW (2001). "Real-time imaging of vascular endothelial-cadherin during leukocyte transmigration across endothelium". J. Immunol. 167 (4): 2323–30. doi:10.4049/jimmunol.167.4.2323. PMID 11490021.
- van Buul JD, Voermans C, van den Berg V, Anthony EC, Mul FP, van Wetering S et al. (2002). "Migration of human hematopoietic progenitor cells across bone marrow endothelium is regulated by vascular endothelial cadherin". J. Immunol. 168 (2): 588–96. doi:10.4049/jimmunol.168.2.588. PMID 11777950.
- Ferber A, Yaen C, Sarmiento E, Martinez J (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.
- Gorlatov S, Medved L (2002). "Interaction of fibrin(ogen) with the endothelial cell receptor VE-cadherin: mapping of the receptor-binding site in the NH2-terminal portions of the fibrin beta chains". Biochemistry 41 (12): 4107–16. doi:10.1021/bi0160314. PMID 11900554.
- Di Simone N, Castellani R, Caliandro D, Caruso A (2003). "Antiphospholid antibodies regulate the expression of trophoblast cell adhesion molecules". Fertil. Steril. 77 (4): 805–11. doi:10.1016/S0015-0282(01)03258-7. PMID 11937138.
- Zanetti A, Lampugnani MG, Balconi G, Breviario F, Corada M, Lanfrancone L et al. (2002). "Vascular endothelial growth factor induces SHC association with vascular endothelial cadherin: a potential feedback mechanism to control vascular endothelial growth factor receptor-2 signaling". Arterioscler. Thromb. Vasc. Biol. 22 (4): 617–22. doi:10.1161/01.ATV.0000012268.84961.AD. PMID 11950700.
- Lampugnani MG, Zanetti A, Breviario F, Balconi G, Orsenigo F, Corada M et al. (2002). "VE-cadherin regulates endothelial actin activating Rac and increasing membrane association of Tiam". Mol. Biol. Cell 13 (4): 1175–89. doi:10.1091/mbc.01-07-0368. PMC 102260. PMID 11950930.
- Vincent PA, Xiao K, Buckley KM, Kowalczyk AP (2004). "VE-cadherin: adhesion at arm's length". Am J Physiol Cell Physiol. 286 (5): C987–97. doi:10.1152/ajpcell.00522.2003. PMID 15075197.
External links
- VE-cadherin protein, human at the US National Library of Medicine Medical Subject Headings (MeSH)
- CDH5 human gene location in the UCSC Genome Browser.
- CDH5 human gene details in the UCSC Genome Browser.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
Membrane proteins: cell adhesion molecules
|
|
Calcium-independent |
IgSF CAM |
- N-CAM (Myelin protein zero)
- ICAM (1, 5)
- VCAM-1
- PE-CAM
- L1-CAM
- Nectin (PVRL1, PVRL2, PVRL3)
|
|
Integrins |
- LFA-1 (CD11a+CD18)
- Integrin alphaXbeta2 (CD11c+CD18)
- Macrophage-1 antigen (CD11b+CD18)
- VLA-4 (CD49d+CD29)
- Glycoprotein IIb/IIIa (ITGA2B+ITGB3)
|
|
|
Calcium-dependent |
Cadherins |
Classical |
|
|
Desmosomal |
- Desmoglein (DSG1, DSG2, DSG3, DSG4)
- Desmocollin (DSC1, DSC2, DSC3)
|
|
Protocadherin |
|
|
Unconventional/ungrouped |
- T-cadherin
- CDH4
- CDH5
- CDH6
- CDH8
- CDH11
- CDH12
- CDH15
- CDH16
- CDH17
- CDH9
- CDH10
|
|
|
Selectins |
- E-selectin
- L-selectin
- P-selectin
|
|
|
Other |
- Lymphocyte homing receptor: CD44
- L-selectin
- integrin (VLA-4, LFA-1)
- Carcinoembryonic antigen
- CD22
- CD24
- CD44
- CD146
- CD164
|
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- See also
- cell membrane protein disorders
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Description |
- Cell membranes
- Cell adhesion
- Membrane transport
- ion channels
- vesicular transport
- solute carrier
- ABC transporters
- ATPase
- oxidoreduction-driven
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Disease |
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UpToDate Contents
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English Journal
- Systems biological analyses reveal the HCV-specific regulation of hematopoietic development.
- Velazquez VM1, Uebelhoer LS, Thapa M, Ibegbu C, Courtney C, Bosinger SE, Magliocca JF, Adams AB, Kirk AD, Knechtle SJ, Kalman D, Suthar M, Grakoui A.
- Hepatology (Baltimore, Md.).Hepatology.2014 Oct 21. doi: 10.1002/hep.27575. [Epub ahead of print]
- Chronic liver disease is characterized by the liver enrichment of myeloid DCs. To assess the role of disease on myelopoiesis, we utilized a systems biology approach to study development in liver-resident cells expressing stem cell marker CD34. In patients with end-stage liver disease, liver CD34+ ce
- PMID 25331524
- An RGD motif present in cadherin 17 induces integrin activation and tumor growth.
- Bartolome R1, Pelaez-Garcia A1, Gomez I2, Torrres S1, Fernandez-Acenero MJ3, Escudero-Paniagua B1, Imbaud JI2, Casal JI4.
- The Journal of biological chemistry.J Biol Chem.2014 Oct 21. pii: jbc.M114.600502. [Epub ahead of print]
- Little is known about the mechanism of integrin activation by cadherin 17 (CDH17). Here, we observed the presence of a tripeptide motif RGD in the domain 6 of the human CDH17 sequence and other cadherins such as cadherin 5 and cadherin 6. The use of CDH17 RAD mutants demonstrated a considerable decr
- PMID 25336636
- SHP2 and FAK Protein Interactions Regulate Pulmonary Endothelium Barrier Function.
- Chichger H1, Braza J, Duong H, Harrington EO.
- American journal of respiratory cell and molecular biology.Am J Respir Cell Mol Biol.2014 Oct 15. [Epub ahead of print]
- Enhanced protein tyrosine phosphorylation (PTP) is associated with changes in vascular permeability through formation and dissolution of adherens junctions and regulation of stress fiber formation. Inhibition of the PTP, SHP2, increases tyrosine phosphorylation of VE-cadherin and β-catenin, resulti
- PMID 25317600
Japanese Journal
- Endothelial PI3K-C2α, a class II PI3K, has an essential role in angiogenesis and vascular barrier function
- Yoshioka Kazuaki,Yoshida Kotaro,Cui Hong,Wakayama Tomohiko,Takuwa Noriko,Okamoto Yasuo,Du Wa,Qi Xun,Asanuma Ken,Sugihara Kazushi,Aki Sho,Miyazawa Hidekazu,Biswas Kuntal,Nagakura Chisa,Ueno Masaya,Iseki Shoichi,Schwartz Robert J.,Okamoto Hiroshi,Sasaki Takehiko,Matsui Osamu,Asano Masahide,Adams Ralf H.,Takakura Nobuyuki,Takuwa Yoh
- Nature Medicine 18(10), 1560-1569, 2012-10
- … PI3K-C2α knockdown in endothelial cells resulted in a decrease in the number of PI3-phosphate-enriched endosomes, impaired endosomal trafficking, defective delivery of VE-cadherin to endothelial cell junctions and defective junction assembly. …
- NAID 120004966617
- VE-Cadherin^<low> α-Smooth Muscle Actin^+ Component of Vascular Progenitor Cells Correlates With the Coronary Artery Gensini Score
- WANG Chao-Hung,HSIEH I-Chang,CHEN Shih-Jen,WANG Jong-Shyan,CHERNG Wen-Jin,CHEN Chun-Chi,LAM Iii-Jan,LIN Shing-Jong
- Circulation journal : official journal of the Japanese Circulation Society 76(2), 477-484, 2012-01-25
- … A subpopulation of VPCs expressed both endothelial (VE-cadherin [VE-Cad]) and smooth-muscle phenotypes (α-smooth muscle actin [α-SMA]). … Correlations of the VE-Cadlowα-SMA+ VPC level and adhesion molecule expression by VPCs with the Gensini score were investigated. …
- NAID 10030036076
- SAM-based cell transfer to photopatterned hydrogels for microengineering vascular-like structures
- Sadr Nasser,Zhu Mojun,Osaki Tatsuya,Kakegawa Takahiro,Yang Yunzhi,Moretti Matteo,Fukuda Junji,Khademhosseini Ali,福田 淳二
- Biomaterials 32(30), 7479-7490, 2011-10
- … The latter, prompted by additional potential application, preserved cell morphology and maintained high transfer efficiency of VE-cadherin positive monolayers over longer culture periods. …
- NAID 80021956594
Related Links
- CD144抗原は、カドヘリン5またはVE-カドヘリンとも呼ばれる分子量140kDaのタンパクで、カドヘリンファミリーに属する接着分子です。内皮細胞に特異的で、内皮組織の接着部位の細胞間隙にみられます。カドヘリン5分子は、血管内皮の ...
- 系統情報 資源番号 nbio132 系統名 VE-cadherin-Cre 正式名称 略称・別名 VE-cad-Creマウス 系統分類 mutant バックグラウンド系統 由来 国立循環器病センター 樹立者 望月 直樹 先生 寄託者 望月 直樹 先生 分譲条件 利用者は研究成果 ...
Related Pictures
★リンクテーブル★
[★]
- 英
- VE-cadherin
- 関
- VE-カドヘリン
[★]
- 英
- VE-cadherin
- 関
- VEカドヘリン
[★]