- 関
- vascular cell adhesion molecule、VCAM-1
WordNet
- small room in which a monk or nun lives (同)cubicle
- a device that delivers an electric current as the result of a chemical reaction (同)electric cell
- a room where a prisoner is kept (同)jail cell, prison cell
- (biology) the basic structural and functional unit of all organisms; they may exist as independent units of life (as in monads) or may form colonies or tissues as in higher plants and animals
- any small compartment; "the cells of a honeycomb"
- a small unit serving as part of or as the nucleus of a larger political movement (同)cadre
- a fibrous band of scar tissue that binds together normally separate anatomical structures
- abnormal union of bodily tissues; most common in the abdomen
- of or relating to or having vessels that conduct and circulate fluids; "vascular constriction"; "a vascular bundle"
- (physics and chemistry) the simplest structural unit of an element or compound
PrepTutorEJDIC
- (刑務所の)『独房』;(修道院の)小さい独居室 / (ミツバチの)みつ房,巣穴 / 小さい部屋 / 『細胞』 / 電池 / 花粉室 / (共産党などの)細胞
- 粘着,付着
- (血液・樹液などを運ぶ)管の,導管の,血管の
- 分子《略》『mol』) / (一般に)(…の)微量《+『of』+『名』》
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2012/11/15 23:23:12」(JST)
[Wiki en表示]
Vascular cell adhesion molecule 1 |
PDB rendering based on 1ij9. |
Available structures |
PDB |
Ortholog search: PDBe, RCSB |
List of PDB id codes |
1IJ9, 1VCA, 1VSC
|
|
|
Identifiers |
Symbols |
VCAM1; CD106; INCAM-100 |
External IDs |
OMIM: 192225 MGI: 98926 HomoloGene: 838 ChEMBL: 3735 GeneCards: VCAM1 Gene |
Gene Ontology |
Molecular function |
• integrin binding
• cell adhesion molecule binding
|
Cellular component |
• podosome
• extracellular space
• plasma membrane
• microvillus
• external side of plasma membrane
• cell surface
• integral to membrane
• filopodium
• sarcolemma
• apical part of cell
• alpha9-beta1 integrin-vascular cell adhesion molecule-1 complex
|
Biological process |
• response to hypoxia
• acute inflammatory response
• chronic inflammatory response
• cell adhesion
• heterophilic cell-cell adhesion
• leukocyte cell-cell adhesion
• heart development
• aging
• response to nutrient
• response to ionizing radiation
• virus-host interaction
• cytokine-mediated signaling pathway
• membrane to membrane docking
• B cell differentiation
• positive regulation of T cell proliferation
• regulation of immune response
• leukocyte tethering or rolling
• interferon-gamma-mediated signaling pathway
• chorio-allantoic fusion
• cellular response to glucose stimulus
|
Sources: Amigo / QuickGO |
|
RNA expression pattern |
|
More reference expression data |
Orthologs |
Species |
Human |
Mouse |
|
Entrez |
7412 |
22329 |
|
Ensembl |
ENSG00000162692 |
ENSMUSG00000027962 |
|
UniProt |
P19320 |
P29533 |
|
RefSeq (mRNA) |
NM_001078.3 |
NM_011693.3 |
|
RefSeq (protein) |
NP_001069.1 |
NP_035823.3 |
|
Location (UCSC) |
Chr 1:
101.19 – 101.2 Mb |
Chr 3:
116.11 – 116.13 Mb |
|
PubMed search |
[1] |
[2] |
|
|
Vascular cell adhesion protein 1 also known as vascular cell adhesion molecule 1 (VCAM-1) or cluster of differentiation 106 (CD106) is a protein that in humans is encoded by the VCAM1 gene.[1] VCAM-1 functions as a cell adhesion molecule.
Contents
- 1 Structure
- 2 Function
- 3 Pharmacology
- 4 References
- 5 Further reading
- 6 External links
|
Structure
The VCAM-1 gene contains six or seven immunoglobulin domains, and is expressed on both large and small blood vessels only after the endothelial cells are stimulated by cytokines. It is alternatively spliced into two known RNA transcripts that encode different isoforms in humans.[2] The gene product is a cell surface sialoglycoprotein, a type I membrane protein that is a member of the Ig superfamily.
Function
The VCAM-1 protein mediates the adhesion of lymphocytes, monocytes, eosinophils, and basophils to vascular endothelium. It also functions in leukocyte-endothelial cell signal transduction, and it may play a role in the development of atherosclerosis and rheumatoid arthritis.
Upregulation of VCAM-1 in endothelial cells by cytokines occurs as a result of increased gene transcription (e.g., in response to Tumor necrosis factor-alpha (TNF-α) and Interleukin-1 (IL-1)) and through stabilization of Messenger RNA (mRNA) (e.g., Interleukin-4 (IL-4)). The promoter region of the VCAM-1 gene contains functional tandem NF-κB (nuclear factor-kappa B) sites. The sustained expression of VCAM-1 lasts over 24 hours.
Primarily, the VCAM-1 protein is an endothelial ligand for VLA-4 (Very Late Antigen-4 or α4β1) of the β1 subfamily of integrins, and for integrin α4β7. VCAM-1 expression has also been observed in other cell types (e.g., smooth muscle cells). It has also been shown to interact with EZR[3] and Moesin.[3]
Pharmacology
Certain melanoma cells can use VCAM-1 to adhere to the endothelium, and VCAM-1 may participate in monocyte recruitment to atherosclerotic sites. As a result, VCAM-1 is a potential drug target.
References
- ^ Cybulsky M, Fries JW, Williams AJ, Sultan P, Eddy RL, Byers MG, Shows TB, Gimbrone MA Jr, Collins T (1991). "The human VCAM1 gene is assigned to chromosome 1p31-p32". Cytogenet. Cell Genet. 58: 1852. doi:10.1159/000133735.
- ^ "Entrez Gene: VCAM1 vascular cell adhesion molecule 1". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7412.
- ^ a b Barreiro, Olga; Yanez-Mo Maria, Serrador Juan M, Montoya Maria C, Vicente-Manzanares Miguel, Tejedor Reyes, Furthmayr Heinz, Sanchez-Madrid Francisco (Jun. 2002). "Dynamic interaction of VCAM-1 and ICAM-1 with moesin and ezrin in a novel endothelial docking structure for adherent leukocytes". J. Cell Biol. (United States) 157 (7): 1233–45. doi:10.1083/jcb.200112126. ISSN 0021-9525. PMC 2173557. PMID 12082081. //www.ncbi.nlm.nih.gov/pmc/articles/PMC2173557/.
Further reading
- Yonekawa K, Harlan JM (2005). "Targeting leukocyte integrins in human diseases.". J. Leukoc. Biol. 77 (2): 129–40. doi:10.1189/jlb.0804460. PMID 15548573.
- Wu TC (2007). "The role of vascular cell adhesion molecule-1 in tumor immune evasion.". Cancer Res. 67 (13): 6003–6. doi:10.1158/0008-5472.CAN-07-1543. PMID 17616653.
External links
- VCAM-1 at the US National Library of Medicine Medical Subject Headings (MeSH)
PDB gallery
|
|
|
1ij9: Highly Hydrated Human VCAM-1 Fragment
|
|
1vca: CRYSTAL STRUCTURE OF AN INTEGRIN-BINDING FRAGMENT OF VASCULAR CELL ADHESION MOLECULE-1 AT 1.8 ANGSTROMS RESOLUTION
|
|
|
|
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
|
|
- See also
- cell membrane protein disorders
B memb: cead, trns (1A, 1C, 1F, 2A, 3A1, 3A2-3, 3D), othr
|
|
UpToDate Contents
全文を閲覧するには購読必要です。 To read the full text you will need to subscribe.
English Journal
- Resveratrol inhibits Staphylococcus aureus-induced TLR2/MyD88/NF-κB-dependent VCAM-1 expression in human lung epithelial cells.
- Lee IT1, Lin CC2, Hsu CK1, Wu MY1, Cho RL1, Yang CM1.
- Clinical science (London, England : 1979).Clin Sci (Lond).2014 Sep 1;127(6):375-90. doi: 10.1042/CS20130816.
- Staphylococcus aureus is the most commonly found Gram-positive bacterium in patients admitted to intensive-care units, causing septicaemia or pneumonia. S. aureus is considered to play an important role in the induction of cell adhesion molecules. Resveratrol, a compound found in the skins of red fr
- PMID 24617573
- VCAM-1 specific PEGylated SAINT-based lipoplexes deliver siRNA to activated endothelium in vivo but do not attenuate target gene expression.
- Leus NG1, Morselt HW1, Zwiers PJ1, Kowalski PS1, Ruiters MH2, Molema G1, Kamps JA3.
- International journal of pharmaceutics.Int J Pharm.2014 Jul 20;469(1):121-31. doi: 10.1016/j.ijpharm.2014.04.041. Epub 2014 Apr 18.
- In recent years much research in RNA nanotechnology has been directed to develop an efficient and clinically suitable delivery system for short interfering RNA (siRNA). The current study describes the in vivo siRNA delivery using PEGylated antibody-targeted SAINT-based-lipoplexes (referred to as ant
- PMID 24746643
- Parathyroid hormone-related protein (107-111) improves the bone regeneration potential of gelatin-glutaraldehyde biopolymer-coated hydroxyapatite.
- Lozano D1, Sánchez-Salcedo S2, Portal-Núñez S3, Vila M2, López-Herradón A3, Ardura JA3, Mulero F4, Gómez-Barrena E5, Vallet-Regí M6, Esbrit P3.
- Acta biomaterialia.Acta Biomater.2014 Jul;10(7):3307-16. doi: 10.1016/j.actbio.2014.03.025. Epub 2014 Apr 2.
- Biopolymer-coated nanocrystalline hydroxyapatite (HA) made as macroporous foams which are degradable and flexible are promising candidates as orthopaedic implants. The C-terminal (107-111) epitope of parathyroid hormone-related protein (PTHrP) exhibits osteogenic properties. The main aim of this stu
- PMID 24704694
Japanese Journal
- Omega 3 Polyunsaturated Fatty Acids Suppress the Development of Aortic Aneurysms Through the Inhibition of Macrophage-Mediated Inflammation
- Yoshihara Takuma,Shimada Kazunori,Fukao Kosuke,Sai Eiryu,Sato-Okabayashi Yayoi,Matsumori Rie,Shiozawa Tomoyuki,Alshahi Hamad,Miyazaki Tetsuro,Tada Norihiro,Daida Hiroyuki
- Circulation Journal 79(7), 1470-1478, 2015
- … EPA administration and DHA administration significantly decreased the expression of tumor necrosis factor-α, monocyte chemoattractant protein-1, transforming growth factor-β, matrix metalloproteinases (MMP)-2, MMP-9, and vascular cell adhesion molecule-1 in the aortas. …
- NAID 130005083946
- Omega 3 Polyunsaturated Fatty Acids Suppress the Development of Aortic Aneurysms Through the Inhibition of Macrophage-Mediated Inflammation
- Yoshihara Takuma,Shimada Kazunori,Fukao Kosuke,Sai Eiryu,Sato-Okabayashi Yayoi,Matsumori Rie,Shiozawa Tomoyuki,Alshahi Hamad,Miyazaki Tetsuro,Tada Norihiro,Daida Hiroyuki
- Circulation Journal advpub(0), 2015
- … EPA administration and DHA administration significantly decreased the expression of tumor necrosis factor-α, monocyte chemoattractant protein-1, transforming growth factor-β, matrix metalloproteinases (MMP)-2, MMP-9, and vascular cell adhesion molecule-1 in the aortas. …
- NAID 130005068466
- 4 VCAM-1はRANKLが誘導する破骨細胞分化を増強する(第543回大阪歯科学会例会)
- 林 寛,氏井 庸介,合田 征司,松本 尚之
- 歯科医学 77(2), 96, 2014-09-25
- … Vascular cell adhesion molecule-1 (VCAM-1) is bound to very late antigen-4 (VLA-4) which is a kind of α4 β1-integrin. … We focused on how VCAM-1/α4 integrin mediates the differentiation into osteoclasts and found that it was through FAK. … These findings confirmed that VCAM-1 regulates the differentiation of bone into osteoclasts. …
- NAID 110009857559
Related Links
- Data indicate neither serum vascular cell adhesion molecule-1 (VCAM-1) levels nor serum epithelial cell adhesion molecule (EpCAM) levels were identified to have a prognostic role on either progression-free survival (PFS) and ...
- CATALOG NO. PRODUCT NAME APPLICATIONS Proteins RPA547Hu01 Recombinant Vascular Cell Adhesion Molecule 1 (VCAM1) SDS-PAGE; WB; ELISA; IP. Antibodies MAA547Hu22 Monoclonal Antibody to Vascular Cell ...
Related Pictures
★リンクテーブル★
[★]
- 英
- vascular cell adhesion molecule-1、VCAM-1
- 関
- 血管内皮細胞接着因子、血管細胞接着分子1
[★]
- 関
- angio、blood vessel、fibrovascular bundle、vascular bundle、vasculogenic、vein、vessel
[★]
[★]
- 関
- mol、molecular、numerator
[★]
細胞