同: Fas antigen, APO-1. Tumor necrosis factor receptor family, member 6
関: Fas、Fas抗原

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2013/08/07 15:23:54」(JST)

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The FAS receptor (FasR), also known as apoptosis antigen 1 (APO-1 or APT), cluster of differentiation 95 (CD95) or tumor necrosis factor receptor superfamily member 6 (TNFRSF6) is a protein that in humans is encoded by the TNFRSF6 gene.^[1]^[2]

The Fas receptor is a death receptor on the surface of cells that leads to programmed cell death (apoptosis). It is one of two apoptosis pathways, the other being the mitochondrial pathway.^[3] FasR is located on chromosome 10 in humans and 19 in mice. Similar sequences related by evolution (orthologs)^[4] are found in most mammals.

Gene[edit source | edit]

FAS receptor is located on the long arm of chromosome 10 (10q24.1) in humans and on chromosome 19 in mice. The gene lies on the plus (Watson strand) and is 25,255 bases in length organised into 9 protein encoding exons.

Protein[edit source | edit]

Previous reports have identified as many as eight splice variants, which are translated into seven isoforms of the protein. Apoptosis-inducing Fas receptor is dubbed isoform 1 and is a type 1 transmembrane protein. Many of the other isoforms are rare haplotypes that are usually associated with a state of disease. However, two isoforms, the apoptosis-inducing membrane-bound form and the soluble form, are normal products whose production via alternative splicing is regulated by the cytotoxic protein TIA1.^[5]

The mature Fas protein has 319 amino acids, has a predicted molecular weight of 48 kiloDaltons and is divided into 3 domains: an extracellular domain, a transmembrane domain, and a cytoplasmic domain. The extracellular domain has 157 amino acids and is rich in cysteine residues. The transmembrane and cytoplasmic domains have 17 and 145 amino acids respectively. Exons 1 through 5 encode the extracelluar region. Exon 6 encodes the transmembrane region. Exons 7-9 encode the intracellular region.

Function[edit source | edit]

Fas forms the death-inducing signaling complex (DISC) upon ligand binding. Membrane-anchored Fas ligand trimer on the surface of an adjacent cell causes oligomerization of Fas. Recent studies which suggested the trimerization of Fas could not be validated. Other models suggested the oligomerization up to 5-7 Fas molecules in the DISC.^[6] This event is also mimicked by binding of an agonistic Fas antibody, though some evidence suggests that the apoptotic signal induced by the antibody is unreliable in the study of Fas signaling. To this end, several clever ways of trimerizing the antibody for in vitro research have been employed.

Upon ensuing death domain (DD) aggregation, the receptor complex is internalized via the cellular endosomal machinery. This allows the adaptor molecule FADD to bind the death domain of Fas through its own death domain.^[7]

FADD also contains a death effector domain (DED) near its amino terminus,^[8] which facilitates binding to the DED of FADD-like interleukin-1 beta-converting enzyme (FLICE), more commonly referred to as caspase-8. FLICE can then self-activate through proteolytic cleavage into p10 and p18 subunits, two each of which form the active heterotetramer enzyme. Active caspase-8 is then released from the DISC into the cytosol, where it cleaves other effector caspases, eventually leading to DNA degradation, membrane blebbing, and other hallmarks of apoptosis.

Recently, Fas has also been shown to promote tumor growth, since during tumor progression, it is frequently downregulated or cells are rendered apoptosis resistant. Cancer cells in general, regardless of their Fas apoptosis sensitivity, depend on constitutive activity of Fas. This is stimulated by cancer-produced Fas ligand for optimal growth.^[9]

Although Fas has been shown to promote tumor growth in the above mouse models, analysis of the human cancer genomics database revealed that FAS is not significantly focally amplified across a dataset of 3131 tumors (FAS is not an oncogene), but is significantly focally deleted across the entire dataset of these 3131 tumors,^[10] suggesting that FAS functions as a tumor suppressor in humans.

In cultured cells, FasL induces various types of cancer cell apoptosis through the Fas receptor. In AOM-DSS-induced colon carcinoma and MCA-induced sarcoma mouse models, it has been shown that Fas acts as a tumor suppressor.^[11] Furthermore, the Fas receptor also mediates tumor-specific cytotoxic T lymphocyte (CTL) anti-tumor cytotoxicity.^[12]

Role in apoptosis[edit source | edit]

Some reports have suggested that the extrinsic Fas pathway is sufficient to induce complete apoptosis in certain cell types through DISC assembly and subsequent caspase-8 activation.

These cells are dubbed Type 1 cells and are characterized by the inability of anti-apoptotic members of the Bcl-2 family (namely Bcl-2 and Bcl-xL) to protect from Fas-mediated apoptosis.

Characterized Type 1 cells include H9, CH1, SKW6.4 and SW480, all of which are lymphocyte lineages except the latter, which is a colon adenocarcinoma lineage.

However, evidence for crosstalk between the extrinsic and intrinsic pathways exists in the Fas signal cascade.

In most cell types, caspase-8 catalyzes the cleavage of the pro-apoptotic BH3-only protein Bid into its truncated form, tBid. BH-3 only members of the Bcl-2 family exclusively engage anti-apoptotic members of the family (Bcl-2, Bcl-xL), allowing Bak and Bax to translocate to the outer mitochondrial membrane, thus permeabilizing it and facilitating release of pro-apoptotic proteins such as cytochrome c and Smac/DIABLO, an antagonist of inhibitors of apoptosis proteins (IAPs).

Overview of signal transduction pathways involved in apoptosis.

Interactions[edit source | edit]

Fas receptor has been shown to interact with:

Caspase 8,^[13]^[14]^[15]
Caspase 10,^[16]
CFLAR,^[14]^[15]
FADD,^[13]^[14]^[17]^[18]^[19]^[20]
Fas ligand,^[13]^[21]^[22]^[23]
PDCD6,^[24] and
Small ubiquitin-related modifier 1.^[25]^[26]

References[edit source | edit]

^ Lichter P, Walczak H, Weitz S, Behrmann I, Krammer PH (September 1992). "The human APO-1 (APT) antigen maps to 10q23, a region that is syntenic with mouse chromosome 19". Genomics 14 (1): 179–80. doi:10.1016/S0888-7543(05)80302-7. PMID 1385299.
^ Inazawa J, Itoh N, Abe T, Nagata S (November 1992). "Assignment of the human Fas antigen gene (Fas) to 10q24.1". Genomics 14 (3): 821–2. doi:10.1016/S0888-7543(05)80200-9. PMID 1385309.
^ Wajant H (2002). "The Fas signaling pathway: more than a paradigm.". Science 296 (5573): 1635–6. doi:10.1126/science.1071553. PMID 12040174.
^ "OrthoMaM phylogenetic marker: FAS coding sequence".
^ Izquierdo JM, Majós N, Bonnal S, Martínez C, Castelo R, Guigó R, Bilbao D, Valcárcel J (August 2005). "Regulation of Fas alternative splicing by antagonistic effects of TIA-1 and PTB on exon definition". Mol. Cell 19 (4): 475–84. doi:10.1016/j.molcel.2005.06.015. PMID 16109372.
^ Wang et al. (2010). "The Fas–FADD death domain complex structure reveals the basis of DISC assembly and disease mutations". Nat Struct Mol Biol 17: 1324–29. doi:10.1038/nsmb.1920. PMID 20935634.
^ Huang B, et al. (1996). "NMR structure and mutagenesis of the Fas (APO-1/CD95) death domain". Nature 384 (6610): 638–41. doi:10.1038/384638a0. PMID 8967952.
^ Eberstadt M, et al. (1998). "NMR structure and mutagenesis of the FADD (Mort1) death-effector domain". Nature 392 (6679): 941–5. doi:10.1038/31972. PMID 9582077.
^ Chen L, Park SM, Tumanov AV, Hau A, Sawada K, Feig C, Turner JR, Fu YX, Romero IL, Lengyel E, Peter ME (May 2010). "CD95 promotes tumour growth". Nature 465 (7297): 492–6. doi:10.1038/nature09075. PMC 2879093. PMID 20505730.
^ "Tumorscape". The Broad Institute.
^ Liu F, Bardhan K, Yang D, Thangaraju M, Ganapathy V, Liles G, Lee J, Liu K (June 2012). "NF-κB directly regulates Fas transcription to modulate Fas-mediated apoptosis and tumor suppression". J Biol Chem. doi:10.1074/jbc.M112.356279. PMID 22669972.
^ Yang D, Torres CM, Bardhan K, Zimmerman M, McGaha TL, Liu K (May 2012). "Decitabine and vorinostat cooperate to sensitize colon carcinoma cells to Fas ligand-induced apoptosis in vitro and tumor suppression in vivo". J. Immunol. 188 (9): 4441–9. doi:10.4049/jimmunol.1103035. PMID 22461695.
^ ^a ^b ^c Gajate C, Mollinedo F (March 2005). "Cytoskeleton-mediated death receptor and ligand concentration in lipid rafts forms apoptosis-promoting clusters in cancer chemotherapy". J. Biol. Chem. 280 (12): 11641–7. doi:10.1074/jbc.M411781200. PMID 15659383.
^ ^a ^b ^c MacFarlane M, Ahmad M, Srinivasula SM, Fernandes-Alnemri T, Cohen GM, Alnemri ES (October 1997). "Identification and molecular cloning of two novel receptors for the cytotoxic ligand TRAIL". J. Biol. Chem. 272 (41): 25417–20. doi:10.1074/jbc.272.41.25417. PMID 9325248.
^ ^a ^b Shu HB, Halpin DR, Goeddel DV (June 1997). "Casper is a FADD- and caspase-related inducer of apoptosis". Immunity 6 (6): 751–63. doi:10.1016/S1074-7613(00)80450-1. PMID 9208847.
^ Vincenz C, Dixit VM (March 1997). "Fas-associated death domain protein interleukin-1beta-converting enzyme 2 (FLICE2), an ICE/Ced-3 homologue, is proximally involved in CD95- and p55-mediated death signaling". J. Biol. Chem. 272 (10): 6578–83. doi:10.1074/jbc.272.10.6578. PMID 9045686.
^ Pan G, O'Rourke K, Chinnaiyan AM, Gentz R, Ebner R, Ni J, Dixit VM (April 1997). "The receptor for the cytotoxic ligand TRAIL". Science 276 (5309): 111–3. doi:10.1126/science.276.5309.111. PMID 9082980.
^ Huang B, Eberstadt M, Olejniczak ET, Meadows RP, Fesik SW (1996). "NMR structure and mutagenesis of the Fas (APO-1/CD95) death domain". Nature 384 (6610): 638–41. doi:10.1038/384638a0. PMID 8967952.
^ Chinnaiyan AM, O'Rourke K, Tewari M, Dixit VM (May 1995). "FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis". Cell 81 (4): 505–12. doi:10.1016/0092-8674(95)90071-3. PMID 7538907.
^ Thomas LR, Stillman DJ, Thorburn A (September 2002). "Regulation of Fas-associated death domain interactions by the death effector domain identified by a modified reverse two-hybrid screen". J. Biol. Chem. 277 (37): 34343–8. doi:10.1074/jbc.M204169200. PMID 12107169.
^ Micheau O, Tschopp J (July 2003). "Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes". Cell 114 (2): 181–90. doi:10.1016/S0092-8674(03)00521-X. PMID 12887920.
^ Starling GC, Bajorath J, Emswiler J, Ledbetter JA, Aruffo A, Kiener PA (April 1997). "Identification of amino acid residues important for ligand binding to Fas". J. Exp. Med. 185 (8): 1487–92. doi:10.1084/jem.185.8.1487. PMC 2196280. PMID 9126929.
^ Schneider P, Bodmer JL, Holler N, Mattmann C, Scuderi P, Terskikh A, Peitsch MC, Tschopp J (July 1997). "Characterization of Fas (Apo-1, CD95)-Fas ligand interaction". J. Biol. Chem. 272 (30): 18827–33. doi:10.1074/jbc.272.30.18827. PMID 9228058.
^ Jung YS, Kim KS, Kim KD, Lim JS, Kim JW, Kim E (October 2001). "Apoptosis-linked gene 2 binds to the death domain of Fas and dissociates from Fas during Fas-mediated apoptosis in Jurkat cells". Biochem. Biophys. Res. Commun. 288 (2): 420–6. doi:10.1006/bbrc.2001.5769. PMID 11606059.
^ Okura T, Gong L, Kamitani T, Wada T, Okura I, Wei CF, Chang HM, Yeh ET (November 1996). "Protection against Fas/APO-1- and tumor necrosis factor-mediated cell death by a novel protein, sentrin". J. Immunol. 157 (10): 4277–81. PMID 8906799.
^ Ryu SW, Chae SK, Kim E (December 2000). "Interaction of Daxx, a Fas binding protein, with sentrin and Ubc9". Biochem. Biophys. Res. Commun. 279 (1): 6–10. doi:10.1006/bbrc.2000.3882. PMID 11112409.

External links[edit source | edit]

FAS Receptor at the US National Library of Medicine Medical Subject Headings (MeSH)

UpToDate Contents

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5. 自己免疫性リンパ増殖症候群(ALPS)：管理および予後 autoimmune lymphoproliferative syndrome alps management and prognosis

English Journal

Regulation of T lymphocyte apoptotic markers is associated to cell activation during the acute phase of dengue.

Torrentes-Carvalho A1, Marinho CF2, de Oliveira-Pinto LM2, de Oliveira DB2, Damasco PV3, Cunha RV4, de Souza LJ5, de Azeredo EL2, Kubelka CF6.Author information 1Laboratório de Imunologia Viral, Instituto Oswaldo Cruz/FIOCRUZ, RJ, Brazil. Electronic address: torrentes@ioc.fiocruz.br.2Laboratório de Imunologia Viral, Instituto Oswaldo Cruz/FIOCRUZ, RJ, Brazil.3Hospital Universitário Pedro Ernesto, UERJ and Hospital Universitário Gafreé-Guinle, UNIRIO, RJ, Brazil.4Departamento de Clínica Médica, FM, Universidade Federal do Mato Grosso do Sul, Campo Grande, MS, Brazil.5Centro de Referência em Dengue e Faculdade de Medicina, Campos de Goytacazes, RJ, Brazil.6Laboratório de Imunologia Viral, Instituto Oswaldo Cruz/FIOCRUZ, RJ, Brazil. Electronic address: claire@ioc.fiocruz.br.AbstractDengue fever, a public health problem in Brazil, may present severe clinical manifestations as result of an increased vascular permeability and coagulation disorders. T cell activation is a critical event for an effective immune response against infection, including the production of cytokines. We aim to reveal mechanisms that modulate the virus-cell interaction, with an emphasis on cell death. Apoptosis is involved in lymphocyte homeostasis, contributes to the clearance of virus-infected cells but also may play a role in the pathogenesis. Phosphatidylserine exposure on CD8T lymphocytes from dengue patients support early apoptotic processes and loss of genomic integrity, observed by DNA fragmentation in T lymphocytes and indicating late apoptosis. These T cells express activation and cytotoxic phenotypes as revealed by CD29 and CD107a upregulation. Higher frequencies of CD95 were detected in T lymphocytes mainly in those with the cytotoxic profile (CD107a(+)) and lower levels of anti-apoptotic molecule Bcl-2, suggesting that both CD4(+) and CD8(+) T cell subsets are more susceptible to apoptosis during acute dengue. The analysis of apoptosis-related protein expression profile showed that not only molecules with pro- but also those with anti-apoptotic functions are overexpressed, indicating that survival mechanisms could be possibly protecting cells against apoptosis caused by viral, immune, oxidative and/or genotoxic stresses. These observations led us to propose that in dengue patients there is an association between T cell susceptibility to apoptosis and the activation state. The mechanisms for understanding the immunopathogenesis during dengue infection are discussed.
Immunobiology.Immunobiology.2014 May;219(5):329-40. doi: 10.1016/j.imbio.2013.11.002. Epub 2014 Jan 9.
Dengue fever, a public health problem in Brazil, may present severe clinical manifestations as result of an increased vascular permeability and coagulation disorders. T cell activation is a critical event for an effective immune response against infection, including the production of cytokines. We a
PMID 24508270

Constitutive expression of murine c-FLIPR causes autoimmunity in aged mice.

Ewald F1, Annemann M1, Pils MC2, Plaza-Sirvent C1, Neff F3, Erck C4, Reinhold D5, Schmitz I1.Author information 11] Institute of Molecular and Clinical Immunology, Otto-von-Guericke-University Magdeburg, Leipziger Str. 44, Magdeburg, Germany [2] Research Group of Systems-Oriented Immunology and Inflammation Research, Department of Immune Control, Helmholtz Centre for Infection Research, Inhoffenstr. 7, Braunschweig, Germany.2Mouse Pathology, Animal Experimental Unit, Helmholtz Centre for Infection Research, Inhoffenstr. 7, Braunschweig, Germany.3Institute of Pathology, Helmholtz Centre Munich, Ingolstaedter Landstr. 1, Neuherberg, Germany.4Cellular Proteome Research, Department of Structure and Function of Proteins, Helmholtz Centre for Infection Research, Inhoffenstr. 7, Braunschweig, Germany.5Institute of Molecular and Clinical Immunology, Otto-von-Guericke-University Magdeburg, Leipziger Str. 44, Magdeburg, Germany.AbstractDeath receptor-mediated apoptosis is a key mechanism for the control of immune responses and dysregulation of this pathway may lead to autoimmunity. Cellular FLICE-inhibitory proteins (c-FLIPs) are known as inhibitors of death receptor-mediated apoptosis. The only short murine c-FLIP splice variant is c-FLIPRaji (c-FLIPR). To investigate the functional role of c-FLIPR in the immune system, we used the vavFLIPR mouse model constitutively expressing murine c-FLIPR in all hematopoietic compartments. Lymphocytes from these mice are protected against CD95-mediated apoptosis and activation-induced cell death. Young vavFLIPR mice display normal lymphocyte compartments, but the lymphocyte populations alter with age. We identified reduced levels of T cells and slightly higher levels of B cells in 1-year-old vavFLIPR mice compared with wild-type (WT) littermates. Moreover, both B and T cells from aged vavFLIPR animals show activated phenotypes. Sera from 1-year-old WT and transgenic animals were analysed for anti-nuclear antibodies. Notably, elevated titres of these autoantibodies were detected in vavFLIPR sera. Furthermore, tissue damage in kidneys and lungs from aged vavFLIPR animals was observed, indicating that vavFLIPR mice develop a systemic lupus erythematosus-like phenotype with age. Taken together, these data suggest that c-FLIPR is an important modulator of apoptosis and enforced expression leads to autoimmunity.
Cell death & disease.Cell Death Dis.2014 Apr 10;5:e1168. doi: 10.1038/cddis.2014.138.
Death receptor-mediated apoptosis is a key mechanism for the control of immune responses and dysregulation of this pathway may lead to autoimmunity. Cellular FLICE-inhibitory proteins (c-FLIPs) are known as inhibitors of death receptor-mediated apoptosis. The only short murine c-FLIP splice variant
PMID 24722293

Death Induced by CD95 or CD95 Ligand Elimination.

Hadji A1, Ceppi P1, Murmann AE1, Brockway S1, Pattanayak A1, Bhinder B2, Hau A1, De Chant S1, Parimi V3, Kolesza P3, Richards J4, Chandel N5, Djaballah H2, Peter ME6.Author information 1Division of Hematology/Oncology, Northwestern University, Feinberg School of Medicine, Chicago, IL 60611, USA.2HTS Core Facility, Memorial Sloan-Kettering Cancer Center, New York, NY 10065, USA.3Department of Pathology, Northwestern University, Feinberg School of Medicine, Chicago, IL 60611, USA.4Department of Molecular and Cellular Biology, Baylor College of Medicine, Houston, TX 77030, USA.5Division of Pulmonary and Cell and Molecular Biology, Northwestern University, Feinberg School of Medicine, Chicago, IL 60611, USA.6Division of Hematology/Oncology, Northwestern University, Feinberg School of Medicine, Chicago, IL 60611, USA. Electronic address: m-peter@northwestern.edu.AbstractCD95 (Fas/APO-1), when bound by its cognate ligand CD95L, induces cells to die by apoptosis. We now show that elimination of CD95 or CD95L results in a form of cell death that is independent of caspase-8, RIPK1/MLKL, and p53, is not inhibited by Bcl-xL expression, and preferentially affects cancer cells. All tumors that formed in mouse models of low-grade serous ovarian cancer or chemically induced liver cancer with tissue-specific deletion of CD95 still expressed CD95, suggesting that cancer cannot form in the absence of CD95. Death induced by CD95R/L elimination (DICE) is characterized by an increase in cell size, production of mitochondrial ROS, and DNA damage. It resembles a necrotic form of mitotic catastrophe. No single drug was found to completely block this form of cell death, and it could also not be blocked by the knockdown of a single gene, making it a promising way to kill cancer cells.
Cell reports.Cell Rep.2014 Apr 10;7(1):208-22. doi: 10.1016/j.celrep.2014.02.035. Epub 2014 Mar 20.
CD95 (Fas/APO-1), when bound by its cognate ligand CD95L, induces cells to die by apoptosis. We now show that elimination of CD95 or CD95L results in a form of cell death that is independent of caspase-8, RIPK1/MLKL, and p53, is not inhibited by Bcl-xL expression, and preferentially affects cancer c
PMID 24656822

Japanese Journal

B細胞の成熟過程でのアポトーシス抑制と腫瘍化 (特集細胞死と造血器腫瘍)

錦織桃子
血液内科 62(2), 166-171, 2011-02
NAID 40019064502

CD95による腫瘍の増殖促進

高橋強志
血液内科 62(6), 746-749, 2011-06
NAID 40019064253

Peripheral regulatory T cells from silicosis patients are susceptible to CD95-mediated apoptosis

HAYASHI Hiroaki
川崎医学会誌 36(1), 13-21, 2010
NAID 110007527339

Related Pictures

★リンクテーブル★

リンク元	「表面抗原分類」「FAS」「Fas抗原」
拡張検索	「CD95 ligand」「CD95リガンド」「CD95抗原」「CD95 antigen」
関連記事	「CD」

「表面抗原分類」

Fas (TNF receptor superfamily, member 6)
	; PDB rendering based on 1ddf.
Available structures
PDB	Ortholog search: PDBe, RCSB
List of PDB id codes
	1DDF, 3EWT, 3EZQ, 3THM, 3TJE
Identifiers
Symbols	FAS; ALPS1A; APO-1; APT1; CD95; FAS1; FASTM; TNFRSF6
External IDs	OMIM: 134637 MGI: 95484 HomoloGene: 27 GeneCards: FAS Gene
Gene Ontology
Molecular function	• signal transducer activity; • receptor activity; • transmembrane signaling receptor activity; • protein binding; • kinase binding; • identical protein binding;
Cellular component	• extracellular region; • nucleus; • cytoplasm; • cytosol; • plasma membrane; • external side of plasma membrane; • integral to membrane; • death-inducing signaling complex; • CD95 death-inducing signaling complex; • membrane raft;
Biological process	• immunoglobulin production; • renal system process; • protein complex assembly; • apoptotic process; • induction of apoptosis; • activation of cysteine-type endopeptidase activity involved in apoptotic process; • activation-induced cell death of T cells; • inflammatory cell apoptotic process; • transformed cell apoptotic process; • signal transduction; • extrinsic apoptotic signaling pathway via death domain receptors; • response to toxic substance; • gene expression; • positive regulation of necrotic cell death; • B cell mediated immunity; • positive regulation of protein homooligomerization; • regulation of apoptotic process; • positive regulation of apoptotic process; • negative regulation of apoptotic process; • negative thymic T cell selection; • regulation of lymphocyte differentiation; • regulation of myeloid cell differentiation; • spleen development; • negative regulation of B cell activation; • protein homooligomerization; • response to glucocorticoid stimulus; • neuron apoptotic process; • cellular response to mechanical stimulus; • cellular response to lithium ion; • cellular response to hyperoxia; • apoptotic signaling pathway;
	Sources: Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs
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　　[★]

英: cluster of differentiation, CD

細胞の表面抗原を認識する抗体を整理した分類

Bリンパ球 CD10,CD19,CD20

Tリンパ球 CD2,CD3,CD5,CD7

幹細胞 CD34

顆粒球 CD13,CD33

単球 CD14：LPSをリガンドとし、Toll-like receptorと共役して細胞内シグナルを伝達する分子。

巨核球 CD41(GpIIb),CD42(GpIb)

NK細胞：CD16(IgGのFc部に対する受容体)、CD56(NCAM-I)

CD1	CD21	CD41	CD61	CD81
CD2	CD22	CD42	CD62	CD82
CD3	CD23	CD43	CD63	CD83
CD4	CD24	CD44	CD64	CD84
CD5	CD25	CD45	CD65	CD85
CD6	CD26	CD46	CD66	CD86
CD7	CD27	CD47	CD67	CD87
CD8	CD28	CD48	CD68	CD88
CD9	CD29	CD49	CD69	CD89
CD10	CD30	CD50	CD70	CD90
CD11	CD31	CD51	CD71	CD91
CD12	CD32	CD52	CD72	CD92
CD13	CD33	CD53	CD73	CD93
CD14	CD34	CD54	CD74	CD94
CD15	CD35	CD55	CD75	CD95
CD16	CD36	CD56	CD76	CD96
CD17	CD37	CD57	CD77	CD97
CD18	CD38	CD58	CD78	CD98
CD19	CD39	CD59	CD79	CD99
CD20	CD40	CD60	CD80	CD100