接着結合
- 関
- zonula adherens
WordNet
- follow through or carry out a plan without deviation; "They adhered to their plan"
- stick to firmly; "Will this wallpaper adhere to the wall?" (同)hold fast, bond, bind, stick, stick_to
- be a devoted follower or supporter; "The residents of this village adhered to Catholicism"; "She sticks to her principles" (同)stick
- be compatible or in accordance with; "You must adhere to the rules"
- the state of being joined together (同)conjunction, conjugation, colligation
- an act of joining or adjoining things (同)adjunction
- something that joins or connects (同)conjunction
- the place where two or more things come together
PrepTutorEJDIC
- 〈物が〉(…に)『くっつく』,付着する,粘着する《+『to』+『名』》 / 〈人が〉(決心・主義などに)執着する,固守する《+『to』+『名』》
- 〈U〉〈C〉連結すること(された状態),『結合』,連合,合体 / 〈C〉『結合点』,連結(接合,合流)点 / 〈C〉(鉄道の)『連絡駅』,接続駅
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2016/01/29 20:53:37」(JST)
[Wiki en表示]
Principal interactions of structural proteins at cadherin-based adherens junction. Actin filaments are associated with adherens junctions in addition to several other actin-binding proteins such as vinculin. The head domain of vinculin associates to E-cadherin via α-, β - and γ -catenins. The tail domain of vinculin binds to membrane lipids and to actin filaments.
Adherens junction |
Details |
Latin |
junctio adhaesionis |
Identifiers |
TH |
H1.00.01.1.02002 |
FMA |
67400 |
Anatomical terminology
[edit on Wikidata]
|
Adherens junctions (or zonula adherens, intermediate junction, or "belt desmosome"[1]) are protein complexes that occur at cell–cell junctions in epithelial and endothelial tissues,[2] usually more basal than tight junctions. An adherens junction is defined as a cell junction whose cytoplasmic face is linked to the actin cytoskeleton. They can appear as bands encircling the cell (zonula adherens) or as spots of attachment to the extracellular matrix (adhesion plaques).
A similar cell junction in non-epithelial, non-endothelial cells is the fascia adherens. It is structurally the same, but appears in ribbonlike patterns that do not completely encircle the cells. One example is in cardiomyocytes.
Contents
- 1 Proteins
- 2 Models
- 3 References
- 4 External links
Proteins
Adherens junctions are composed of the following proteins:[3]
- cadherins. The cadherins are a family of transmembrane proteins that form homodimers in a calcium-dependent manner with other cadherin molecules on adjacent cells.
- p120 (sometimes called delta catenin) binds the juxtamembrane region of the cadherin.
- γ-catenin or gamma-catenin (plakoglobin) binds the catenin-binding region of the cadherin.
- α-catenin or alpha-catenin binds the cadherin indirectly via β-catenin or plakoglobin and links the actin cytoskeleton with cadherin.
Models
Adherens junctions were, for many years, thought to share the characteristic of anchor cells through their cytoplasmic actin filaments.
The accepted model has been that adherens junctions serve as a bridge connecting the actin cytoskeleton of neighboring cells through direct interaction. However, scientists have not been able to isolate the quaternary complex of cadherin-βcatenin-αcatenin-actin in vitro. Recent data (2005) demonstrate that membrane- associated actin is several fold less stable compared to components of the adherens junctional complex.[4][5]
Additionally, the authors found that monomeric α-catenin preferentially binds to the cadherin junction complex through β-catenin. Dimeric α-catenin preferentially binds to actin and suppresses Arp2/3 complex-mediated actin branching, thus acting as a molecular switch to regulate actin polymerization.
Adherens junctions may serve as a regulatory module to maintain the actin contractile ring with which it is associated in microscopic studies.
References
- ^ Pardo, JV, Craig, SW (1979). "alpha-Actinin localization in the junctional complex of intestinal epithelial cells". J Cell Biol 80: 203–210. doi:10.1083/jcb.80.1.203. Retrieved 15 October 2014.
- ^ Guo, Renyong; Sakamoto, Hiroshi; Sugiura, Shigeki (October 2006). "Endothelial Cell Motility Is Compatible With Junctional Integrity". Journal of Cellular Physiology 211: 327–335. doi:10.1002/jcp.20937.
- ^ Ferreri DM, Vincent PA (2008). "Signaling to and through the Endothelial Adherens Junction". In LaFlamme SE, Kowalczyck AP. Cell Junctions: Adhesion, Development, and Disease. Wiley VCH. ISBN 978-3-527-31882-7.
- ^ Yamada S, Pokutta S, Drees F, Weis W, Nelson W (2005). "Deconstructing the cadherin-catenin-actin complex.". Cell 123 (5): 889–901. doi:10.1016/j.cell.2005.09.020. PMC 3368712. PMID 16325582.
- ^ Drees F, Pokutta S, Yamada S, Nelson W, Weis W (2005). "Alpha-catenin is a molecular switch that binds E-cadherin-beta-catenin and regulates actin-filament assembly.". Cell 123 (5): 903–15. doi:10.1016/j.cell.2005.09.021. PMC 3369825. PMID 16325583.
External links
|
Wikimedia Commons has media related to Adherens junctions. |
- MBInfo - Adherens Junction
- MBInfo - Adherens Junction Assembly
- Adherens Junctions at the US National Library of Medicine Medical Subject Headings (MeSH)
- Histology image: 20502loa – Histology Learning System at Boston University
Histology: Epithelial proteins (TH H1.00.01.1)
|
|
Lateral/cell-cell |
- Cell adhesion molecules: Adherens junction
- Desmosome
- Ion channels: Gap junction/Connexon
- Cytoskeleton: Desmosome
- Desmoplakin
- Plakoglobin
- Tonofibril
- other membrane proteins: Tight junction
- Claudin
- Occludin
- MARVELD2
|
|
Basal/cell-matrix |
- Basal lamina
- Hemidesmosome/Tonofibril
- Focal adhesion
- Costamere
|
|
Apical |
- Cilia/Kinocilium
- Microvilli/Stereocilia (STRC)
|
|
Index of cells
|
|
Description |
- Structure
- Organelles
- peroxisome
- cytoskeleton
- centrosome
- epithelia
- cilia
- mitochondria
- Membranes
- Membrane transport
- ion channels
- vesicular transport
- solute carrier
- ABC transporters
- ATPase
- oxidoreduction-driven
|
|
Disease |
- Structural
- peroxisome
- cytoskeleton
- cilia
- mitochondria
- nucleus
- scleroprotein
- Membrane
- channelopathy
- solute carrier
- ATPase
- ABC transporters
- other
- extracellular ligands
- cell surface receptors
- intracellular signalling
- Vesicular transport
- Pore-forming toxins
|
|
|
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
- Modeling keratinocyte wound healing dynamics: Cell-cell adhesion promotes sustained collective migration.
- Nardini JT1, Chapnick DA2, Liu X3, Bortz DM4.
- Journal of theoretical biology.J Theor Biol.2016 Jul 7;400:103-17. doi: 10.1016/j.jtbi.2016.04.015. Epub 2016 Apr 19.
- The in vitro migration of keratinocyte cell sheets displays behavioral and biochemical similarities to the in vivo wound healing response of keratinocytes in animal model systems. In both cases, ligand-dependent Epidermal Growth Factor Receptor (EGFR) activation is sufficient to elicit collective ce
- PMID 27105673
- Crucial roles of the Arp2/3 complex during mammalian corticogenesis.
- Wang PS1, Chou FS2, Ramachandran S3, Xia S3, Chen HY4, Guo F1, Suraneni P5, Maher B4, Li R6.
- Development (Cambridge, England).Development.2016 Jul 6. pii: dev.130542. [Epub ahead of print]
- The polarity and organization of radial glial cells (RGCs), which serve as both stem cells and scaffolds for neuronal migration, are crucial for cortical development. However, the cytoskeletal mechanisms that drive radial glial outgrowth and maintain RGC polarity remain poorly understood. Here, we s
- PMID 27385014
- Phospholipase C Epsilon Signaling Mediates Endothelial Cell Inflammation and Barrier Disruption in Acute Lung Injury.
- Bijli KM1, Fazal F2, Slavin SA2, Leonard A2, Grose V2, Alexander WB3, Smrcka AV4, Rahman A5.
- American journal of physiology. Lung cellular and molecular physiology.Am J Physiol Lung Cell Mol Physiol.2016 Jul 1:ajplung.00069.2016. doi: 10.1152/ajplung.00069.2016. [Epub ahead of print]
- Phospholipase C epsilon (PLCε) is a unique PLC isoform that can be regulated by multiple signaling inputs from both Ras family GTPases and heterotrimeric G proteins and has primary sites of expression in the heart and lung. While the role of PLCε in cardiac function and pathology has been document
- PMID 27371732
Japanese Journal
- 細胞間接着 : Eカドヘリンとネクチンのバリア機能への関与 (特集 生体バリアと生体防御・免疫系)
- 臨床免疫・アレルギー科 = Clinical immunology & allergology 64(1), 15-19, 2015-07
- NAID 40020540430
- 1P203 アクトミオシン収縮運動の制御機構 : α-カテニンの阻害作用を中心に(12.細胞生物的課題,ポスター,日本生物物理学会年会第51回(2013年度))
- 2SEA-03 AFMを用いた接着結合分子の力学挙動解析(2SEA 新学術領域「細胞シグナリング複合体によるシグナル検知・伝達・応答の構造的基礎」共催,構造細胞生物学の生物物理学的こころ,シンポジウム,日本生物物理学会第51回年会(2013年度))
Related Links
- Principal interactions of structural proteins at cadherin-based adherens junction. Actin filaments are associated with adherens junctions in addition to several other actin-binding proteins such as vinculin. The head domain of vinculin ...
- 米国CST社の日本法人CSTジャパン株式会社【公式サイト】接着接合動態 (Adherens Junction Dynamics)ページ。高品質の研究用試薬、米国本社の開発研究者による技術的サポートをご提供しております。
★リンクテーブル★
[★]
接着帯
- 関
- adherens junction、adhesion belt
[★]
- 関
- accretion、adherence、adherent、adhesion、adhesive、attach、attachment、coalesce、coalescence、coalescent、cohesion、perseveration、stick、symphysial
[★]
- 関
- junctional、junctional region、juncture