WordNet

a fibrous band of scar tissue that binds together normally separate anatomical structures
abnormal union of bodily tissues; most common in the abdomen
(physics and chemistry) the simplest structural unit of an element or compound

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粘着,付着
分子《略》『mol』) / (一般に)(…の)微量《+『of』+『名』》

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2013/08/02 17:23:03」(JST)

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Cell Adhesion Molecules (CAMs) are proteins located on the cell surface^[1] involved in binding with other cells or with the extracellular matrix (ECM) in the process called cell adhesion. Essentially, cell adhesion molecules help cells stick to each other and to their surroundings.

These proteins are typically transmembrane receptors and are composed of three domains: an intracellular domain that interacts with the cytoskeleton, a transmembrane domain, and an extracellular domain that interacts either with other CAMs of the same kind (homophilic binding) or with other CAMs or the extracellular matrix (heterophilic binding).

Families of CAMs[edit source | edit]

Most of the CAMs belong to four protein families: Ig (immunoglobulin) superfamily (IgSF CAMs), the integrins, the cadherins, and the selectins.

One classification system involves the distinction between calcium-independent CAMs and calcium-dependent CAMs.^[2]

Calcium-independent[edit source | edit]

IgSF CAMs[edit source | edit]

Main article: IgSF CAM

Immunoglobulin superfamily CAMs (IgSF CAMs) are either homophilic or heterophilic and bind integrins or different IgSF CAMs.

Lymphocyte homing receptors[edit source | edit]

These are also known as addressins. Two well known examples are CD34 and GLYCAM-1.

Calcium-dependent[edit source | edit]

Integrins[edit source | edit]

Main article: Integrin

Integrins are one of the major classes of receptors within the ECM^[3] and mediate cell-ECM interactions with collagen, fibrinogen, fibronectin and vitronectin.^[4] Integrins provide essential links between the extracellular environment and the intracellular signalling pathways which can play roles in cell behaviours such as apoptosis, differentiation, survival and transcription.^[5]

Integrins are heterodimeric; as they consist of an alpha and beta subunit.^[6] There are currently 18 alpha subunits and 8 beta subunits which combine to make up 24 different integrin combinations.^[4] Within each of the alpha and beta subunits there is a large extracellular domain, a transmembrane domain and a short cytoplasmic domain.^[7] The extracellular domain is where the ligand binds through the use of divalent cations. Generally Mn2+
increases affinity, Mg2+
promotes adhesion to cells and Ca2+
decreases cell adhesion.^[5] Integrins regulate their activity within the body by changing conformation. Most exist at rest in a low affinity state which can be altered to high affinity through an external agonist which causes a conformational change within the integrin, increasing their affinity.^[5]

An example of this is the aggregation of platelets;^[5]

Agonists such as thrombin or collagen trigger the integrin into its high affinity state which causes increased fibrinogen binding causing platelet aggregation.

Cadherins[edit source | edit]

Main article: Cadherin

The cadherins are homophilic Ca2+
-dependent glycoproteins.^[8] The classic cadherins (E-, N- and P-) are concentrated at the intermediate cell junctions which link to the actin filament network through specific linking proteins called catenins.^[8]

Each cadherin exhibits a unique pattern of tissue distribution, such as epithelial (E-cadherins), placental (P-cadherins), neural (N-cadherins), retinal (R-cadherins), brain (B-cadherins and T-cadherins) and muscle (M-cadherins).^[8] Many cell types express combinations of cadherin types.

The extracellular domain has major repeats called extracellular cadherin domains (ECD). Sequences involved in Ca2+
binding between the ECDs are necessary for cell adhesion. The cytoplasmic domain has specific regions where catenin proteins bind.^[9]

Selectins[edit source | edit]

Main article: Selectin

The selectins are a family of heterophilic CAMs that bind fucosylated carbohydrates, e.g., mucins. The three family members are E-selectin (endothelial), L-selectin (leukocyte), and P-selectin (platelet). The best-characterized ligand for the three selectins is P-selectin glycoprotein ligand-1 (PSGL-1), which is a mucin-type glycoprotein expressed on all white blood cells.

References[edit source | edit]

^ Cell Adhesion Molecules at the US National Library of Medicine Medical Subject Headings (MeSH)
^ Brackenbury R, Rutishauser U, Edelman GM (January 1981). "Distinct calcium-independent and calcium-dependent adhesion systems of chicken embryo cells". Proc. Natl. Acad. Sci. U.S.A. 78 (1): 387–91. doi:10.1073/pnas.78.1.387. PMC 319058. PMID 6165990.
^ Brown, K; Yamada, K (1995), "The Role of Integrins during Vertebrae Development", Developmental Biology 6: 69–77
^ ^a ^b Humphries JD, Byron A, Humphries MJ (October 2006). "Integrin ligands at a glance". J. Cell. Sci. 119 (Pt 19): 3901–3. doi:10.1242/jcs.03098. PMC 3380273. PMID 16988024.
^ ^a ^b ^c ^d Schnapp, L (2006). Integrin, Adhesion/cell-matrix. Seattle: Elsevier.
^ García AJ (December 2005). "Get a grip: integrins in cell-biomaterial interactions". Biomaterials 26 (36): 7525–9. doi:10.1016/j.biomaterials.2005.05.029. PMID 16002137.
^ Vinatier D (March 1995). "Integrins and reproduction". Eur J Obstet Gynecol Reprod Biol 59 (1): 71–81. doi:10.1016/0028-2243(94)01987-I.
^ ^a ^b ^c Buxton RS, Magee AI (June 1992). "Structure and interactions of desmosomal and other cadherins". Semin. Cell Biol. 3 (3): 157–67. PMID 1623205.
^ Soncin, F.; Ward, M.C. (2011). "The Function of E-Cadherin in Stem Cell Pluripotency and Self-Renewal". Genes 2 (1): 229–259. doi:10.3390/genes2010229.

UpToDate Contents

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Analysis of cell surface antigens by Surface Plasmon Resonance imaging.

Stojanović I, Schasfoort RB, Terstappen LW.SourceMedical Cell Biophysics Group, MIRA institute, Faculty of Science and Technology, University of Twente, PO Box 217, 7500AE Enschede, The Netherlands. Electronic address: i.stojanovic@utwente.nl.
Biosensors & bioelectronics.Biosens Bioelectron.2014 Feb 15;52:36-43. doi: 10.1016/j.bios.2013.08.027. Epub 2013 Aug 27.
Surface Plasmon Resonance (SPR) is most commonly used to measure bio-molecular interactions. SPR is used significantly less frequent for measuring whole cell interactions. Here we introduce a method to measure whole cells label free using the specific binding of cell surface antigens expressed on th
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COUP-TFII inhibits NFkappaB activation in endocrine-resistant breast cancer cells.

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mRNA and miRNA expression patterns associated to pathways linked to metal mixture health effects.

Martínez-Pacheco M, Hidalgo-Miranda A, Romero-Córdoba S, Valverde M, Rojas E.SourceUniversidad Nacional Autónoma de México, Instituto de Investigaciones Biomédicas, Departamento de Medicina Genómica y Toxicología Ambiental, C.U., 04510 México, México.
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Metals are a threat to human health by increasing disease risk. Experimental data have linked altered miRNA expression with exposure to some metals. MiRNAs comprise a large family of non-coding single-stranded molecules that primarily function to negatively regulate gene expression post-transcriptio
PMID 24080485

Japanese Journal

Cyclosporine Nanomicelle Eye Drop : A Novel Medication for Corneal Graft Transplantation Treatment

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NAID 40020471511

The Cell Adhesion Molecule Necl-4/CADM4 Serves as a Novel Regulator for Contact Inhibition of Cell Movement and Proliferation

Yamana Shota,Tokiyama Amina,Mizutani Kiyohito,Hirata Ken-ichi,Takai Yoshimi,Rikitake Yoshiyuki
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Direct Infection of Primary Salivary Gland Epithelial Cells by Human T Lymphotropic Virus Type I in Patients With Sjögren's Syndrome

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Related Pictures

Overexpression of adhesion molecules and barrier molecules is associated with Intercellular Adhesion Molecule-1; Antigens, CD54; CD54 Antigens; ICAM-1 Cellular Adhesion Molecules (CAMs) - CHSAnatomy/Physiology Adhesion molecules in skin seminar (2) Opinions on Cell adhesion

★リンクテーブル★

リンク元	「接着分子」
拡張検索	「cell adhesion molecule」「platelet endothelial cell adhesion molecule-1」「neuron-glia cell adhesion molecule」「intracellular adhesion molecule 1」
関連記事	「adhesion」「molecule」

「接着分子」

　　[★]

英: adhesion molecule
同: 接着因子
関

接着分子のファミリー

インテグリンファミリー
Igスーパーファミリー
セレクチンファミリー
CD44ファミリー
カドヘリンファミリー

白血球の相互作用に関与している接着分子 (IMM.87)

グループ名	機能	名称	別名		組織分布	リガンド
セレクチン	炭化水素鎖に結合。白血球-内皮細胞の反応を開始	P-selectin	PADGEN	CD62P	活性化した内皮細胞、活性化した血小板	PSGL-1, sialyl-Lewisx
セレクチン	炭化水素鎖に結合。白血球-内皮細胞の反応を開始	E-selectin	ELAM-1	CD62E	活性化した内皮細胞	sialyl-Lewisx
インテグリン	CAMや細胞外マトリックスに結合。強い結合	LFA-1	αL:β2	CD11a:CD18	単球、T細胞、マクロファージ、好中球、樹状細胞	ICAMs
		CR3, Mac-1	αM:β2	CD11b:CD18	好中球、単球、マクロファージ	ICAM-1, iC3b, fibrinogen
		CR4, p150.95	αX:β2	CD11c:CD18	樹状細胞、マクロファージ、好中球	iC3b
		VLA-5	α5:β1	CD49d:CD29	単球、マクロファージ	fibronectin
免疫グロブリンスーパーファミリー	細胞結合で様々に働く。インテグリンの基質	ICAM-1		CD54	活性化した内皮細胞	LFA-1, MAC1
		ICAM-2		CD102	非活性化状態の内皮細胞、樹状細胞	LFA-1
		VCAM-1		CD106	活性化した内皮細胞	VLA-4
		PECAM		CD31	活性化した白血球、内皮細胞間の結合	CD31

白血球の相互作用に関与している免疫グロブリンスーパーファミリーの接着分子 (IMM.329)

名称		分布組織	リガンド
CD2	LFA-2	T細胞	LFA-1	CD53
ICAM-1	CD54	活性化した血管、リンパ球、樹状細胞	LFA-1, Mac-1
ICAM-2	CD102	非活性化状態の血管	LFA-1
ICAM-3	CD50	Naive T cells	DC-SIGN, LFA-1
LFA-3	CD58	リンパ球、APC	CD2
VCAM-1	CD106	活性化した内皮細胞	VLA-4