関: P-セレクチン P-Selectin

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2014/01/23 22:34:52」(JST)

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P-selectin is a protein that in humans is encoded by the SELP gene.^[1]

P-selectin functions as a cell adhesion molecule (CAM) on the surfaces of activated endothelial cells, which line the inner surface of blood vessels, and activated platelets. In unactivated endothelial cells, it is stored in granules called Weibel-Palade bodies, and α-granules in unactivated platelets.

Other names for P-selectin include CD62P, Granule Membrane Protein 140 (GMP-140), and Platelet Activation-Dependent Granule to External Membrane Protein (PADGEM). It was first identified in endothelial cells in 1989.^[2]

Gene and regulation[edit]

P-selectin is located on chromosome 1q21-q24, spans > 50 kb and contains 17 exons in human.^[3] P-selectin is constitutively expressed on megakaryocytes (the precursor of platelets) and endothelial cells.^[4] The expression of P-selectin consists of two distinct mechanisms. First, P-selectin is synthesized by megakaryocytes and endothelial cells, where it is sorted into the membranes of secretory granules.^[5] When megakaryocytes and endothelial cells are activated by the action of agonists such as thrombin, P-selectin rapidly translocated to the plasma membrane from granules.^[6] Second, the increased level of mRNA and protein of P-selectin is induced by inflammatory mediators such as tumor necrosis factor-a (TNF-a), LPS, interleukin-4 (IL-4) while TNF-a or LPS is not associated with the increase of P-selectin in human endothelial cells unlike murine.^[7] ^[8] ^[9] The elevated synthesis of P-selectin may play an important role in the delivery of protein to the cell surface.

Structure[edit]

P-selectin is found in endothelial cells and platelets where it is stored in Weibel-Palade bodies and α-granules, respectively. In response to inflammatory cytokines such as IL-4 and IL-13, P-selectin is translocated to the plasma membrane in endothelial cells.^[10] The extracellular region of P-selectin is composed of three different domains like other selectin types; a C-type lectin-like domain in the N-terminus, an EGF-like domain and a complement-binding protein-like domains (same as complement regulatory proteins: CRP) having short consensus repeats (~60 amino acids). The number of CRP repeats is the major feature differentiating the type of selectin in extracellular region. In human, P-selectin has nine repeats while E-selectin contains six and L-selectin has only two. P-selectin is anchored in transmembrane region that is followed by a short cytoplasmic tail region.^[11]

Ligand[edit]

The primary ligand for P-selectin is P-selectin glycoprotein ligand-1 (PSGL-1) which is expressed on almost all leukocytes although P-selectin also binds to heparan sulfate and fucoidan. PSGL-1 is situated on various hematopoietic cells such as neutrophils, eosinophils, lymphocytes, and monocytes, in which it mediates tethering and adhesion of these cells. However, there is no specificity of PSGL-1 for P-selectin since it can function as ligand for other types of selectin.^[12]

Function[edit]

P-selectin plays an essential role in the initial recruitment of leukocytes (white blood cells) to the site of injury during inflammation. When endothelial cells are activated by molecules such as histamine or thrombin during inflammation, P-selectin moves from an internal cell location to the endothelial cell surface.

Thrombin is one trigger which can stimulate endothelial-cell release of P-selectin and recent studies suggest an additional Ca²⁺-independent pathway involved in release of P-selectin.^[13]

Ligands for P-selectin on eosinophils and neutrophils are similar sialylated, protease-sensitive, endo-beta-galactosidase-resistant structures, clearly different than those reported for E-selectin, and suggest disparate roles for P-selectin and E-selectin during recruitment during inflammatory responses.^[14]

P-selectin is also very important in the recruitment and aggregation of platelets at areas of vascular injury. In quiescent platelet, P-selectin is located on the inner wall of α-granules. Platelet activation (through agonists such as thrombin, Type II collagen and ADP) results in "membrane flipping" where the platelet releases α- and dense granules and the inner walls of the granules are exposed on the outside of the cell. The P-selectin then promotes platelet aggregation through platelet-fibrin and platelet-platelet binding.

P-selectin attaches to the actin cytoskeleton through anchor proteins that are still poorly characterized.

Role in cancer[edit]

P-selectin has a functional role in metastasis of tumor similar to E-selectin.^[15] P-selectin is expressed on the surface of both stimulated endothelial cell and activated platelet and helps cancer cells invade into bloodstream for metastasis and provided locally with multiple growth factors respectively.^[16] Moreover, it has been known that platelet facilitates tumor metastasis by forming complexes with tumor cells and leukocytes in the vasculature thus preventing recognition by macrophagge, this is thought to contribute to the seeding of tumor microemboli to distant organs.^[17] In vivo mice experiment showed that reduction in circulating platelets could reduce cancer metastasis.^[18]

The oligosaccharide sialylated Lewis x (sLe(x)) is expressed on the surface of tumor cells and can be recognized by E-selectin and P-selectin, playing on a key role in metastasis of the tumor. However in the 4T1 breast cancer cell line, E-selectin reactivity is sLe(x) dependent while P-selectin reactivity is sLe(x)-independent, suggesting P-selectin binding is Ca²⁺-independent and sulfation-dependent.^[19] One of the sulfated ligands is chondroitin sulfate, a type of glycosaminoglycan (GAG). Its activity in tumor metastasis has been probed by the addition of heparin that functions to blocks tumor metastasis. In addition to GAGs, mucin is of interest in P-selectin mediated tumor metastasis.^[20] Selective removal of mucin results in reduced interaction between P-selectin and platelets in vivo and in vitro.^[17]

Heparin has long been known to represent antiheparanase activity that is to keep an endoglycosidase from degrading heparin sulfate, one of the glycosaminoglycans, and to effectively inhibit P-selectin.^[21] Despite a striking effect of heparin on tumor progression shown in a number of clinical trials,^[22] the use of heparin as anti-cancer agent is limited because of its risk, which might induce adverse bleeding complications. Given those reasons, development of new compounds that target P-selectin is now emerging for cancer therapy. Among them, the inhibitory activity of semisynthetic sulfated tri mannose C-C-linked dimers (STMCs) to P-selectin was shown by the attenuation of tumor metastasis in vivo animal model, indicating the inhibition of interaction between tumor cell and endothelial cell is significant for blocking tumor dissemination.^[23]

References[edit]

^ Ryan US, Worthington RE (February 1992). "Cell-cell contact mechanisms". Curr. Opin. Immunol. 4 (1): 33–7. doi:10.1016/0952-7915(92)90120-4. PMID 1375831. Cite uses deprecated parameters (help)
^ McEver RP, Beckstead JH, Moore KL, Marshall-Carlson L, Bainton DF (July 1989). "GMP-140, a platelet alpha-granule membrane protein, is also synthesized by vascular endothelial cells and is localized in Weibel-Palade bodies". J. Clin. Invest. 84 (1): 92–9. doi:10.1172/JCI114175. PMC 303957. PMID 2472431. Cite uses deprecated parameters (help)
^ Herrmann SM, Ricard S, Nicaud V, Mallet C, Evans A, Ruidavets JB, Arveiler D, Luc G, Cambien F (August 1998). "The P-selectin gene is highly polymorphic: reduced frequency of the Pro715 allele carriers in patients with myocardial infarction". Hum. Mol. Genet. 7 (8): 1277–84. doi:10.1093/hmg/7.8.1277. PMID 9668170. Cite uses deprecated parameters (help)
^ Pan J, Xia L, McEver RP (April 1998). "Comparison of promoters for the murine and human P-selectin genes suggests species-specific and conserved mechanisms for transcriptional regulation in endothelial cells". J. Biol. Chem. 273 (16): 10058–67. doi:10.1074/jbc.273.16.10058. PMID 9545353. Cite uses deprecated parameters (help)
^ Disdier M, Morrissey JH, Fugate RD, Bainton DF, McEver RP (March 1992). "Cytoplasmic domain of P-selectin (CD62) contains the signal for sorting into the regulated secretory pathway". Mol. Biol. Cell 3 (3): 309–21. PMC 275532. PMID 1378326. Cite uses deprecated parameters (help)
^ Hattori R, Hamilton KK, Fugate RD, McEver RP, Sims PJ (May 1989). "Stimulated secretion of endothelial von Willebrand factor is accompanied by rapid redistribution to the cell surface of the intracellular granule membrane protein GMP-140". J. Biol. Chem. 264 (14): 7768–71. PMID 2470733. Cite uses deprecated parameters (help)
^ Hahne M, Jäger U, Isenmann S, Hallmann R, Vestweber D (May 1993). "Five tumor necrosis factor-inducible cell adhesion mechanisms on the surface of mouse endothelioma cells mediate the binding of leukocytes". J. Cell Biol. 121 (3): 655–64. doi:10.1083/jcb.121.3.655. PMC 2119562. PMID 7683689. Cite uses deprecated parameters (help)
^ Liu et al., J. Exp. Med. Vol. 207 No. 13 2975-2987 www.jem.org/cgi/doi/10.1084/jem.20101545
^ Panes et al., Br J Pharmacol. 1999 February; 126(3): 537–550. at page 538 doi: 10.1038/sj.bjp.0702328
^ Woltmann G, McNulty CA, Dewson G, Symon FA, Wardlaw AJ (May 2000). "Interleukin-13 induces PSGL-1/P-selectin-dependent adhesion of eosinophils, but not neutrophils, to human umbilical vein endothelial cells under flow". Blood 95 (10): 3146–52. PMID 10807781. Cite uses deprecated parameters (help)
^ Vestweber D, Blanks JE (January 1999). "Mechanisms that regulate the function of the selectins and their ligands". Physiol. Rev. 79 (1): 181–213. PMID 9922371. Cite uses deprecated parameters (help)
^ Lorenzon P, Vecile E, Nardon E, Ferrero E, Harlan JM, Tedesco F, Dobrina A (September 1998). "Endothelial cell E- and P-selectin and vascular cell adhesion molecule-1 function as signaling receptors". J. Cell Biol. 142 (5): 1381–91. doi:10.1083/jcb.142.5.1381. PMC 2149355. PMID 9732297. Cite uses deprecated parameters (help)
^ Cleator JH, Zhu WQ, Vaughan DE, Hamm HE (April 2006). "Differential regulation of endothelial exocytosis of P-selectin and von Willebrand factor by protease-activated receptors and cAMP". Blood 107 (7): 2736–44. doi:10.1182/blood-2004-07-2698. PMC 1895372. PMID 16332977. Cite uses deprecated parameters (help)
^ Wein M, Sterbinsky SA, Bickel CA, Schleimer RP, Bochner BS (March 1995). "Comparison of human eosinophil and neutrophil ligands for P-selectin: ligands for P-selectin differ from those for E-selectin". Am. J. Respir. Cell Mol. Biol. 12 (3): 315–9. PMID 7532979. Cite uses deprecated parameters (help)
^ Köhler S, Ullrich S, Richter U, Schumacher U (February 2010). "E-/P-selectins and colon carcinoma metastasis: first in vivo evidence for their crucial role in a clinically relevant model of spontaneous metastasis formation in the lung". Br. J. Cancer 102 (3): 602–9. doi:10.1038/sj.bjc.6605492. PMC 2822933. PMID 20010946. Cite uses deprecated parameters (help)
^ Chen M, Geng JG (2006). "P-selectin mediates adhesion of leukocytes, platelets, and cancer cells in inflammation, thrombosis, and cancer growth and metastasis". Arch. Immunol. Ther. Exp. (Warsz.) 54 (2): 75–84. doi:10.1007/s00005-006-0010-6. PMID 16648968.
^ ^a ^b Borsig L, Wong R, Feramisco J, Nadeau DR, Varki NM, Varki A (March 2001). "Heparin and cancer revisited: mechanistic connections involving platelets, P-selectin, carcinoma mucins, and tumor metastasis". Proc. Natl. Acad. Sci. U.S.A. 98 (6): 3352–7. doi:10.1073/pnas.061615598. PMC 30657. PMID 11248082. Cite uses deprecated parameters (help)
^ Gasic GJ (1984). "Role of plasma, platelets, and endothelial cells in tumor metastasis". Cancer Metastasis Rev. 3 (2): 99–114. doi:10.1007/BF00047657. PMID 6386144.
^ Monzavi-Karbassi B, Stanley JS, Hennings L, Jousheghany F, Artaud C, Shaaf S, Kieber-Emmons T (March 2007). "Chondroitin sulfate glycosaminoglycans as major P-selectin ligands on metastatic breast cancer cell lines". Int. J. Cancer 120 (6): 1179–91. doi:10.1002/ijc.22424. PMID 17154173. Cite uses deprecated parameters (help)
^ Garcia J, Callewaert N, Borsig L (February 2007). "P-selectin mediates metastatic progression through binding to sulfatides on tumor cells". Glycobiology 17 (2): 185–96. doi:10.1093/glycob/cwl059. PMID 17043066. Cite uses deprecated parameters (help)
^ Bar-Ner M, Eldor A, Wasserman L, Matzner Y, Cohen IR, Fuks Z, Vlodavsky I (August 1987). "Inhibition of heparanase-mediated degradation of extracellular matrix heparan sulfate by non-anticoagulant heparin species". Blood 70 (2): 551–7. PMID 2955820. Cite uses deprecated parameters (help)
^ Lazo-Langner A, Goss GD, Spaans JN, Rodger MA (April 2007). "The effect of low-molecular-weight heparin on cancer survival. A systematic review and meta-analysis of randomized trials". J. Thromb. Haemost. 5 (4): 729–37. doi:10.1111/j.1538-7836.2007.02427.x. PMID 17408406. Cite uses deprecated parameters (help)
^ Borsig L, Vlodavsky I, Ishai-Michaeli R, Torri G, Vismara E (May 2011). "Sulfated hexasaccharides attenuate metastasis by inhibition of P-selectin and heparanase". Neoplasia 13 (5): 445–52. PMC 3084621. PMID 21532885. Cite uses deprecated parameters (help)

External links[edit]

P-Selectin at the US National Library of Medicine Medical Subject Headings (MeSH)

UpToDate Contents

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1. 炎症の病因における白血球内皮細胞接着 leukocyte endothelial adhesion in the pathogenesis of inflammation
2. A群レンサ球菌：病原性因子および発症機序 group a streptococcus virulence factors and pathogenic mechanisms
3. 末期腎不全における他の腎代替療法 alternative renal replacement therapies in end stage renal disease
4. 血小板機能検査 platelet function testing

English Journal

Role of peroxisome proliferator‑activated receptor α in atherosclerosis.

Cao H, Wen G, Li H.Author information Department of Cardiology, Shanghai First People's Hospital, College of Medicine, Shanghai Jiaotong University, Shanghai 200080, P.R. China.AbstractAtherosclerosis is an inﬂammatory disease involving the immune response. In addition to lowering the cholesterol level, the peroxisome proliferator-activated receptor α (PPAR-α) can prevent atherosclerosis via its pleiotropic anti-inflammatory effects. However, the role of PPAR-α in modulating inflammatory progression of atherosclerosis has rarely been studied. Thus, we aimed to investigate the role of PPAR-α in atherosclerosis by evaluating the expression of inflammatory cytokines induced by PPAR-α in an in vivo rabbit model. New Zealand White rabbits were randomly divided into 5 groups: control, high-fat diet + balloon injury, high-fat diet + balloon injury + placebo, high-fat diet + balloon injury + fenofibrate, and high-fat diet + balloon injury + WY-14643. The femoral arteries of rabbits were balloon-injured after initiation of the high-fat diet and before administration of fenofibrate, WY-14643 or placebo solution. Atherosclerosis was induced by high-fat diet and balloon angioplasty, and the vessel wall lumen occlusion was determined by measuring the stenosis rate. PPAR-α gene expression was examined by quantitative polymerase chain reaction analysis. The cellular localization and distribution of PPAR-α was observed by immunohistochemistry, and its protein level was assessed by western blot analysis. The production of interleukin-10 (IL-10), tumor necrosis factor-α (TNF-α) and P-selectin, which are major inflammatory factors involved in atherosclerosis, was monitored by an enzyme-linked immunosorbent assay (ELISA). Treatment with PPAR-α agonists (fenofibrate or WY-14643) reduced the vascular occlusion rate, as compared to the high‑fat diet + balloon injury and the placebo groups. Furthermore, the expression of PPAR-α at both the protein and the mRNA level was increased in the fenofibrate and WY-14643 groups. According to the results, the TNF-α and P-selectin levels were reduced in the fenofibrate and WY-14643 groups. These results suggest that PPAR-α activation can attenuate the effects of atherosclerosis by inhibiting the expression of major inflammatory factors in a rabbit atherosclerosis model.
Molecular medicine reports.Mol Med Rep.2014 May;9(5):1755-60. doi: 10.3892/mmr.2014.2020. Epub 2014 Mar 6.
Atherosclerosis is an inﬂammatory disease involving the immune response. In addition to lowering the cholesterol level, the peroxisome proliferator-activated receptor α (PPAR-α) can prevent atherosclerosis via its pleiotropic anti-inflammatory effects. However, the role of PPAR-α in modulating
PMID 24604149

Platelet Activation in Essential Hypertension During Exercise: Pre- and Post-Treatment Changes With an Angiotensin II Receptor Blocker.

Gkaliagkousi E1, Gavriilaki E, Yiannaki E, Markala D, Papadopoulos N, Triantafyllou A, Anyfanti P, Petidis K, Garypidou V, Doumas M, Ferro A, Douma S.Author information 12nd Propedeutic Department of Internal Medicine, Aristotle University of Thessaloniki, Thessaloniki, Greece.AbstractBACKGROUND: Acute exercise may exert deleterious effects on the cardiovascular system through a variety of pathophysiological mechanisms, including increased platelet activation. However, the degree of exercise-induced platelet activation in untreated hypertensive (UH) individuals as compared with normotensive (NT) individuals has yet to be established. Furthermore, the effect of antihypertensive treatment on exercise-induced platelet activation in essential hypertension (EH) remains unknown.
American journal of hypertension.Am J Hypertens.2014 Apr;27(4):571-8. doi: 10.1093/ajh/hpt153. Epub 2013 Aug 23.
BACKGROUND: Acute exercise may exert deleterious effects on the cardiovascular system through a variety of pathophysiological mechanisms, including increased platelet activation. However, the degree of exercise-induced platelet activation in untreated hypertensive (UH) individuals as compared with n
PMID 23975222

The role of fucosylation in the promotion of endothelial progenitor cells in neovascularization and bone repair.

Sun S1, Liu Z2, Zhou H3, Li G3, Liu M2, Yao J4, Zhou T2, An G5, Wu Q6, Dong N7.Author information 1The Cyrus Tang Hematology Center, Soochow University, Suzhou 215123, China; The Second Affiliated Hospital, Soochow University, Suzhou 215004, China.2The Cyrus Tang Hematology Center, Soochow University, Suzhou 215123, China.3The Second Affiliated Hospital, Soochow University, Suzhou 215004, China.4Department of Oncology, Chao-Yang Hospital, Capital Medical University, Beijing 100020, China.5Department of Oncology, Chao-Yang Hospital, Capital Medical University, Beijing 100020, China. Electronic address: anguangyu@hotmail.com.6The Cyrus Tang Hematology Center, Soochow University, Suzhou 215123, China; Molecular Cardiology, Cleveland Clinic, Cleveland, OH 44195, USA. Electronic address: wuq@ccf.org.7The Cyrus Tang Hematology Center, Soochow University, Suzhou 215123, China; The MOH Key Laboratory of Thrombosis and Hemostasis, Jiangsu Institute of Hematology, the First Affiliated Hospital of Soochow University, Suzhou 215006, China. Electronic address: ningzhengdong@suda.edu.cn.AbstractBone marrow-derived endothelial progenitor cells (EPCs) are being tested as a therapy to treat a variety of ischemic diseases. Poor homing to targeted tissues is one of the major factors limiting the therapeutic efficacy of EPCs. Here, we show that human cord blood-derived EPCs expressed little sialyl Lewis X (sLe(x)) antigen that is necessary for selectin-mediated cell-cell interactions. Expression of α1,3-fucosyltransferase VI (FucT VI) in the EPCs enhanced sLe(x) synthesis, E- and P-selectin-binding, and EPC adhesion to tumor necrosis factor-α-stimulated human umbilical vein endothelial cells in culture. In a mouse model of hind limb ischemia, in which EPCs were injected intravenously, FucT VI expression increased EPC homing, neovascularization, and blood flow in ischemic muscles. In another mouse model of femoral fracture, FucT VI-expressing EPCs were more efficient than control EPCs in targeting to peri-fracture tissues to enhance angiogenesis, blood flow and bone repair. These results indicate that fucosylated EPCs may be used to as an improved cellular source to treat ischemic diseases.
Biomaterials.Biomaterials.2014 Apr;35(12):3777-85. doi: 10.1016/j.biomaterials.2014.01.025. Epub 2014 Jan 30.
Bone marrow-derived endothelial progenitor cells (EPCs) are being tested as a therapy to treat a variety of ischemic diseases. Poor homing to targeted tissues is one of the major factors limiting the therapeutic efficacy of EPCs. Here, we show that human cord blood-derived EPCs expressed little sial
PMID 24485794

Japanese Journal

Gene Expression Analysis during Platelet-Like Particle Production in Phorbol Myristate Acetate-Treated MEG-01 Cells

Isakari Yoshimasa,Sogo Shinji,Ishida Tatsuhiro [他],Kawakami Takuma,Ono Toshihide,Taki Takao,Kiwada Hiroshi
Biological & pharmaceutical bulletin 32(3), 354-358, 2009-03-01
… On the other hand, RT-PCR analysis detected increased expression of β1-tubulin, CD62P, gpIbα and gpIII, which are related to PLT function and megakaryocyte differentiation, following PMA treatment for 24h. …
NAID 110007122743

Time Course of Platelet Activation and von Willebrand Factor in Patients With Non-Valvular Atrial Fibrillation After Ischemic Stroke : Evaluation of Prognostic Determinants

Yip Hon-Kan,Lai Shung-Lon,Lan Min-Yu,Chang Wen-Neng,Liu Josef S.,Kao Yi-Fen,Chang Yung-Yee,Lu Cheng-Hsien,Chen Wei-Hsi,Lin Hung-Hseng,Liou Chia-Wei
Circulation journal : official journal of the Japanese Circulation Society 71(3), 321-326, 2007-02-20
… Background The present study investigated serial changes in platelet activation(expressed by CD62p) and von Willebrand factor(VWF), and the correlation between increased CD62p expression, VWF and brain infarct volume(BIV: measured by magnetic resonance imaging), and prognostic determinants in non-valvular atrial fibrillation(NVAF) patients after acute ischemic stroke(IS). …
NAID 110006224197

Platelet Activation in Patients With Chronic Nonvalvular Atrial Fibrillation

Yip Hon-Kan,Chang Li-Teh,Sun Cheuk-Kwan,Yang Cheng-Hsu,Hung Wei-Chin,Hang Chi-Ling,Wu Chiung-Jen,Chua Sarah,Yeh Kuo-Ho,Chang Hsueh-Wen
International Heart Journal 47(3), 371-379, 2006
… This study investigated platelet reactivity (expressed by CD62p) in patients with chronic nonvalvular (NV) AF. … Expression of CD62p was measured by flow cytometry in 62 consecutive patients with chronic NVAF (defined as sustained AF > … The CD62p expression was also evaluated in 20 healthy subjects. … Expression of CD62p was not different between AF patients and healthy subjects (P = 0.970). …
NAID 130000068706

Related Pictures

★リンクテーブル★

リンク元	「接着分子」「p-selectin」

「接着分子」

Selectin P (granule membrane protein 140kDa, antigen CD62)
	; PDB rendering based on pdb 1G1S.
Available structures
PDB	Ortholog search: PDBe, RCSB
List of PDB id codes
	1FSB, 1G1Q, 1G1R, 1G1S, 1HES
Identifiers
Symbols	SELP; CD62; CD62P; GMP140; GRMP; LECAM3; PADGEM; PSEL
External IDs	OMIM: 173610 MGI: 98280 HomoloGene: 2260 ChEMBL: 5378 GeneCards: SELP Gene
Gene Ontology
Molecular function	• lipopolysaccharide binding; • glycoprotein binding; • protein binding; • heparin binding; • sialic acid binding; • fucose binding; • glycosphingolipid binding; • calcium-dependent protein binding; • oligosaccharide binding;
Cellular component	• extracellular space; • nucleus; • nucleolus; • cytoplasm; • plasma membrane; • integral to plasma membrane; • external side of plasma membrane; • platelet dense granule membrane; • platelet alpha granule membrane;
Biological process	• platelet degranulation; • positive regulation of leukocyte migration; • inflammatory response; • cell adhesion; • heterophilic cell-cell adhesion; • leukocyte cell-cell adhesion; • blood coagulation; • positive regulation of platelet activation; • positive regulation of phosphatidylinositol 3-kinase cascade; • platelet activation; • response to lipopolysaccharide; • regulation of integrin activation; • defense response to Gram-negative bacterium; • leukocyte migration; • leukocyte tethering or rolling;
	Sources: Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs
	This box: view; talk; edit;

　　[★]

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

-接着分子

-細胞接着分子

-カドヘリン

「p-selectin」

　　[★]

同: CD62P

同: CD62P

[pmid1375831-1] Ryan US, Worthington RE (February 1992). "Cell-cell contact mechanisms". Curr. Opin. Immunol. 4 (1): 33–7. doi:10.1016/0952-7915(92)90120-4. PMID 1375831. Cite uses deprecated parameters (help)

[pmid2472431-2] McEver RP, Beckstead JH, Moore KL, Marshall-Carlson L, Bainton DF (July 1989). "GMP-140, a platelet alpha-granule membrane protein, is also synthesized by vascular endothelial cells and is localized in Weibel-Palade bodies". J. Clin. Invest. 84 (1): 92–9. doi:10.1172/JCI114175. PMC 303957. PMID 2472431. Cite uses deprecated parameters (help)

[pmid9668170-3] Herrmann SM, Ricard S, Nicaud V, Mallet C, Evans A, Ruidavets JB, Arveiler D, Luc G, Cambien F (August 1998). "The P-selectin gene is highly polymorphic: reduced frequency of the Pro715 allele carriers in patients with myocardial infarction". Hum. Mol. Genet. 7 (8): 1277–84. doi:10.1093/hmg/7.8.1277. PMID 9668170. Cite uses deprecated parameters (help)

[pmid9545353-4] Pan J, Xia L, McEver RP (April 1998). "Comparison of promoters for the murine and human P-selectin genes suggests species-specific and conserved mechanisms for transcriptional regulation in endothelial cells". J. Biol. Chem. 273 (16): 10058–67. doi:10.1074/jbc.273.16.10058. PMID 9545353. Cite uses deprecated parameters (help)

[pmid1378326-5] Disdier M, Morrissey JH, Fugate RD, Bainton DF, McEver RP (March 1992). "Cytoplasmic domain of P-selectin (CD62) contains the signal for sorting into the regulated secretory pathway". Mol. Biol. Cell 3 (3): 309–21. PMC 275532. PMID 1378326. Cite uses deprecated parameters (help)

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CD62P