CD93

同

Clq receptor for phagocytosis

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1. certificate of deposit / (また『C.D.』)Civil Defense民間防衛

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2012/12/05 06:41:54」(JST)

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CD93 molecule
Identifiers
Symbols	CD93; C1QR1; C1qR(P); C1qRP; CDw93; ECSM3; MXRA4; dJ737E23.1
External IDs	OMIM: 120577 MGI: 106664 HomoloGene: 7823 GeneCards: CD93 Gene
Gene Ontology Molecular function • complement component C1q binding • receptor activity • calcium ion binding • protein binding • carbohydrate binding Cellular component • plasma membrane • cell surface • integral to membrane • cytoplasmic membrane-bounded vesicle Biological process • phagocytosis • cell-cell adhesion • virus-host interaction • macrophage activation Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	22918	17064
Ensembl	ENSG00000125810	ENSMUSG00000027435
UniProt	Q9NPY3	O89103
RefSeq (mRNA)	NM_012072.3	NM_010740.3
RefSeq (protein)	NP_036204.2	NP_034870.1
Location (UCSC)	Chr 20: 23.06 – 23.07 Mb	Chr 2: 148.44 – 148.44 Mb
PubMed search	[1]	[2]

CD93 (Cluster of Differentiation 93) is a protein that in humans is encoded by the CD93 gene. CD93 is a C-type lectin transmembrane receptors which play a role not only in cell–cell adhesion processes but also in host defence.

Family

CD93 belongs to the Group XIV C-Type lectin family, a group containing two other members, endosialin (CD248) and thrombomodulin, a well characterized anticoagulant. All of them contain a C-type lectin domain, a series of epidermal growth factor like domains (EGF), a highly glycosylated mucin-like domain, a unique transmembrane domain and a short cytoplasmic tail. Due to their strong homology and their close proximity on chromosome 20, CD93 has been suggested to have arisen from the thrombomodulin gene through a duplication event

Expression

CD93 was originally identified in mice as an early B cell marker through the use of AA4.1 monoclonal antibody.^{[citation needed]} Then this molecule was shown to be expressed on an early population of hematopoietic stem cells, which give rise to the entire spectrum of mature cells in the blood. Now CD93 is known to be expressed by a wide variety of cells such as platelets, monocytes, microglia and endothelial cells. In the immune system CD93 is also expressed on neutrophils, activated macrophages, B cell precursors until the T2 stage in the spleen, a subset of dendritic cells and of natural killer cells. Molecular characterization of CD93 revealed that this protein is identical with C1qRp, a human protein identified as a putative C1q receptor. C1q belongs to the complement activation proteins and plays a major role in the activation of the classical pathway of the complement, which leads to the formation of the membrane attack complex. C1q is also involved in other immunological processes such as enhancement of bacterial phagocytosis, clearance of apoptotic cells or neutralisation of virus. Strikingly, it has been shown that anti-C1qRp significantly reduced C1q enhanced phagocytosis. A more recent study confirmed that C1qRp is identical to CD93 protein, but failed to demonstrate a direct interaction between CD93 and C1q under physiological conditions. Rencently it has been shown that CD93 is re-expressed during the late B cell differentiation and CD93 can be used in this context as a plasma cell maturation marker.

Function

CD93 was initially thought to be a receptor for C1q, but now is thought to instead be involved in intercellular adhesion and in the clearance of apoptotic cells. The intracellular cytoplasmic tail of this protein contains two highly conserved domains which may be involved in CD93 function. Indeed, the highly charged juxtamembrane domain has been found to interact with moesin, a protein known to play a role in linking transmembrane proteins to the cytoskeleton and in the remodelling of the cytoskeleton. This process appears crucial for both adhesion, migration and phagocytosis, three functions in which CD93 may be involved.

In the context of late B cell differentiation, CD93 has been shown to be important for the maintenance of high antibody titres after immunization and in the survival of long-lived plasma cells in the bone marrow. Indeed, CD93 deficient mice failed to maintain high antibody level upon immunization and present a lower amount of antigen specific plasma cells in the bone marrow.

See also

• Cluster of differentiation
• C-type lectin

References

Further reading

• Chevrier S; Genton, C; Kallies, A; Karnowski, A; Otten, LA; Malissen, B; Malissen, M; Botto, M et al. (2009). "CD93 is required for maintenance of antibody secretion and persistence of plasma cells in the bone marrow niche". PNAS 106 (10): 3895–3900. doi:10.1073/pnas.0809736106. PMC 2656176. PMID 19228948. //www.ncbi.nlm.nih.gov/pmc/articles/PMC2656176/.
• Tenner AJ (1999). "C1q receptors: regulating specific functions of phagocytic cells". Immunobiology 199 (2): 250–64. PMID 9777410.
• Ghebrehiwet B, Peerschke EI, Hong Y et al. (1992). "Short amino acid sequences derived from C1q receptor (C1q-R) show homology with the alpha chains of fibronectin and vitronectin receptors and collagen type IV". J. Leukoc. Biol. 51 (6): 546–56. PMID 1377218.
• Peerschke EI, Ghebrehiwet B (1990). "Platelet C1q receptor interactions with collagen- and C1q-coated surfaces". J. Immunol. 145 (9): 2984–8. PMID 2212670.
• Eggleton P, Lieu TS, Zappi EG et al. (1994). "Calreticulin is released from activated neutrophils and binds to C1q and mannan-binding protein". Clin. Immunol. Immunopathol. 72 (3): 405–9. doi:10.1006/clin.1994.1160. PMID 8062452.
• Joseph K, Ghebrehiwet B, Peerschke EI et al. (1996). "Identification of the zinc-dependent endothelial cell binding protein for high molecular weight kininogen and factor XII: identity with the receptor that binds to the globular "heads" of C1q (gC1q-R)". Proc. Natl. Acad. Sci. U.S.A. 93 (16): 8552–7. doi:10.1073/pnas.93.16.8552. PMC 38710. PMID 8710908. //www.ncbi.nlm.nih.gov/pmc/articles/PMC38710/.
• Cáceres J, Brandan E (1997). "Interaction between Alzheimer's disease beta A4 precursor protein (APP) and the extracellular matrix: evidence for the participation of heparan sulfate proteoglycans". J. Cell. Biochem. 65 (2): 145–58. doi:10.1002/(SICI)1097-4644(199705)65:2<145::AID-JCB2>3.0.CO;2-U. PMID 9136074.
• Nepomuceno RR, Tenner AJ (1998). "C1qRP, the C1q receptor that enhances phagocytosis, is detected specifically in human cells of myeloid lineage, endothelial cells, and platelets". J. Immunol. 160 (4): 1929–35. PMID 9469455.
• Stuart GR, Lynch NJ, Day AJ et al. (1998). "The C1q and collectin binding site within C1q receptor (cell surface calreticulin)". Immunopharmacology 38 (1–2): 73–80. doi:10.1016/S0162-3109(97)00076-3. PMID 9476117.
• Nepomuceno RR, Ruiz S, Park M, Tenner AJ (1999). "C1qRP is a heavily O-glycosylated cell surface protein involved in the regulation of phagocytic activity". J. Immunol. 162 (6): 3583–9. PMID 10092817.
• Norsworthy PJ, Taylor PR, Walport MJ, Botto M (1999). "Cloning of the mouse homolog of the 126-kDa human C1q/MBL/SP-A receptor, C1qR(p)". Mamm. Genome 10 (8): 789–93. doi:10.1007/s003359901093. PMID 10430665.
• Hartley JL, Temple GF, Brasch MA (2001). "DNA Cloning Using In Vitro Site-Specific Recombination". Genome Res. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863. //www.ncbi.nlm.nih.gov/pmc/articles/PMC310948/.
• Kittlesen DJ, Chianese-Bullock KA, Yao ZQ et al. (2001). "Interaction between complement receptor gC1qR and hepatitis C virus core protein inhibits T-lymphocyte proliferation". J. Clin. Invest. 106 (10): 1239–49. doi:10.1172/JCI10323. PMC 381434. PMID 11086025. //www.ncbi.nlm.nih.gov/pmc/articles/PMC381434/.
• Joseph K, Shibayama Y, Ghebrehiwet B, Kaplan AP (2001). "Factor XII-dependent contact activation on endothelial cells and binding proteins gC1qR and cytokeratin 1". Thromb. Haemost. 85 (1): 119–24. PMID 11204562.
• Simpson JC, Wellenreuther R, Poustka A et al. (2001). "Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing". EMBO Rep. 1 (3): 287–92. doi:10.1093/embo-reports/kvd058. PMC 1083732. PMID 11256614. //www.ncbi.nlm.nih.gov/pmc/articles/PMC1083732/.
• Deloukas P, Matthews LH, Ashurst J et al. (2002). "The DNA sequence and comparative analysis of human chromosome 20". Nature 414 (6866): 865–71. doi:10.1038/414865a. PMID 11780052.
• Steinberger P, Szekeres A, Wille S et al. (2002). "Identification of human CD93 as the phagocytic C1q receptor (C1qRp) by expression cloning". J. Leukoc. Biol. 71 (1): 133–40. PMID 11781389.

External links

• CD93+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)

English Journal

• Unique properties of cluster of differentiation 93 in the umbilical cord blood of neonates.

• Ikewaki N, Sonoda T, Inoko H.Author information Laboratories of Clinical Immunology, Department of Animal Pharmaceutical Science, Kyushu University of Health and Welfare School of Pharmaceutical Sciences, 1714-1 Yoshino-machi, Nobeoka-shi, Miyazaki, 882-8508.AbstractIt has previously been reported by these authors that cluster of differentiation (CD) 93 is co-expressed on naive T-lymphocytes (CD4(+) CD45RA(+) cells) in neonatal umbilical cord blood cells (UCBCs) but not on normal adult peripheral blood cells (PBCs). In this study, expression of CD93 on other lymphocyte subsets and the concentration of soluble formed CD93 (sCD93) in serum or culture supernatants from neonatal umbilical cord blood (UCB) was examined. It was found that CD93 is also co-expressed on CD2(+) , CD16(+) , CD56(+) or CD25(+) cells in the lymphocyte population of neonatal UCBCs, but not on normal adult PBCs. The concentrations of sCD93 in serum and culture supernatants from neonatal UCB were significantly greater than those from normal adult peripheral blood. The concentrations of sCD93 in culture supernatants from neonatal UCBCs and normal adult PBCs treated with phorbol 12-myristate 13-acetate (PMA) were significantly enhanced compared with those without PMA treatment. The degree of enhancement of sCD93 by PMA in culture supernatants from neonatal UCBCs was significantly greater than that of normal adult PBCs and enhancement of sCD93 by PMA in the culture supernatants from neonatal UCBCs and normal adult PBCs was significantly suppressed by PKC inhibitor. Interestingly, the high concentration of serum sCD93 in neonates was significantly decreased in sera from infants at 1 month after birth. Expression of CD93 on the lymphocyte population of PBCs from infants at 1 month after birth was also significantly decreased, compared with that for neonatal UCBCs. These findings indicate that CD93 in neonatal UCB has unique properties as an immunological biomarker.
• Microbiology and immunology.Microbiol Immunol.2013 Dec;57(12):822-32. doi: 10.1111/1348-0421.12097.
• It has previously been reported by these authors that cluster of differentiation (CD) 93 is co-expressed on naive T-lymphocytes (CD4(+) CD45RA(+) cells) in neonatal umbilical cord blood cells (UCBCs) but not on normal adult peripheral blood cells (PBCs). In this study, expression of CD93 on other ly
• PMID 24033555

• miR-29 promotes murine osteoclastogenesis by regulating osteoclast commitment and migration.

• Franceschetti T, Kessler CB, Lee SK, Delany AM.Author information From the Center for Molecular Medicine and.AbstractOsteoclast differentiation is regulated by transcriptional, post-transcriptional, and post-translational mechanisms. MicroRNAs are fundamental post-transcriptional regulators of gene expression. The function of the miR-29 (a/b/c) family in cells of the osteoclast lineage is not well understood. In primary cultures of mouse bone marrow-derived macrophages, inhibition of miR-29a, -29b, or -29c diminished formation of TRAP (tartrate-resistant acid phosphatase-positive) multinucleated osteoclasts, and the osteoclasts were smaller. Quantitative RT-PCR showed that all miR-29 family members increased during osteoclast differentiation, in concert with mRNAs for the osteoclast markers Trap (Acp5) and cathepsin K. Similar regulation was observed in the monocytic cell line RAW264.7. In stably transduced RAW264.7 cell lines expressing an inducible miR-29 competitive inhibitor (sponge construct), miR-29 knockdown impaired osteoclastic commitment and migration of pre-osteoclasts. However, miR-29 knockdown did not affect cell viability, actin ring formation, or apoptosis in mature osteoclasts. To better understand how miR-29 regulates osteoclast function, we validated miR-29 target genes using Luciferase 3'-UTR reporter assays and specific miR-29 inhibitors. We demonstrated that miR-29 negatively regulates RNAs critical for cytoskeletal organization, including Cdc42 (cell division control protein 42) and Srgap2 (SLIT-ROBO Rho GTPase-activating protein 2). Moreover, miR-29 targets RNAs associated with the macrophage lineage: Gpr85 (G protein-coupled receptor 85), Nfia (nuclear factor I/A), and Cd93. In addition, Calcr (calcitonin receptor), which regulates osteoclast survival and resorption, is a novel miR-29 target. Thus, miR-29 is a positive regulator of osteoclast formation and targets RNAs important for cytoskeletal organization, commitment, and osteoclast function. We hypothesize that miR-29 controls the tempo and amplitude of osteoclast differentiation.
• The Journal of biological chemistry.J Biol Chem.2013 Nov 15;288(46):33347-60. doi: 10.1074/jbc.M113.484568. Epub 2013 Oct 1.
• Osteoclast differentiation is regulated by transcriptional, post-transcriptional, and post-translational mechanisms. MicroRNAs are fundamental post-transcriptional regulators of gene expression. The function of the miR-29 (a/b/c) family in cells of the osteoclast lineage is not well understood. In p
• PMID 24085298

• B cell lymphoma in HIV transgenic mice.

• Curreli S, Krishnan S, Reitz M, Lunardi-Iskandar Y, Lafferty MK, Garzino-Demo A, Zella D, Gallo RC, Bryant J.Author information Institute of Human Virology, University of Maryland School of Medicine, Baltimore, MD 21201, USA. scurreli@ihv.umaryland.edu.AbstractBACKGROUND: Human Immunodeficiency Virus Type I (HIV-1) infection is associated with a high incidence of B-cell lymphomas. The role of HIV in these lymphomas is unclear and currently there are no valid in vivo models for better understanding HIV-related lymphomagenesis. Transgenic (Tg) 26 mice have a 7.4-kb pNL4-3 HIV-1 provirus lacking a 3.1-kb sequence encompassing parts of the gag-pol region. Approximately 15% of these HIV Tg mice spontaneously develop lymphoma with hallmark pre-diagnostic markers including skin lesions, diffuse lymphadenopathy and an increase in pro-inflammatory serum cytokines. Here we describe the phenotypic and molecular characteristics of the B cell leukemia/lymphoma in the Tg mice.
• Retrovirology.Retrovirology.2013 Aug 28;10:92. doi: 10.1186/1742-4690-10-92.
• BACKGROUND: Human Immunodeficiency Virus Type I (HIV-1) infection is associated with a high incidence of B-cell lymphomas. The role of HIV in these lymphomas is unclear and currently there are no valid in vivo models for better understanding HIV-related lymphomagenesis. Transgenic (Tg) 26 mice have
• PMID 23985023

Japanese Journal

• 臍帯血由来造血幹細胞表面上のCD93の発現

• 池脇 信直,園田 徹,佐藤 薫 [他]
• 九州保健福祉大学研究紀要 -(13) (-), 101-110, 2012-03
• NAID 40019276733

• 臍帯血由来造血幹細胞表面上のCD93の発現

• 池脇 信直,園田 徹,佐藤 薫,猪子 英俊
• 九州保健福祉大学研究紀要 13, 101-110, 2012-03
• … 臍帯血由来造血幹細胞表面上のCD93の発現を我々が開発したCD93モノクローナル抗体(mNI-11)、既存のCD34抗体、CD45抗体を組み合わせたフローサイトメトリー法で解析した。 … その結果、臍帯血由来造血幹細胞(CD34+細胞およびCD34+CD45dim+細胞)表面上にはCD93が発現していることが分かった。 …
• NAID 110009359873

• たいまつ米胚芽発酵GABAによるヒト単球系細胞株(U937)表面上のCD93の発現およびインターロイキンー 8(IL-8)の産生増強

• 池脇 信直,石附 亨,中村 雅彦 [他],林 裕二,樋口 元剛,後藤 牧人
• 九州保健福祉大学研究紀要 11, 159-167, 2010-03
• … たいまつ米胚芽発酵GABAによる単球系細胞株(U937)表面上のCD93抗原の発現をモノクローナル抗体を用いた酵素抗体法およびフローサイトメトリー法で解析した。 … その結果、たいまつ米胚芽発酵GABAで培養したU937細胞はCD93(C1qRp)の発現が有意に増強した。 … また、CD93の発現増強はprotein kinase C(PKC)阻害剤であるGo6976で抑制された。 …
• NAID 110007577976

Related Links

• 抗CD93 モノクローナル抗体 (clone: mNI-11) | 免疫 | 製品カタログ ...

CD93抗体 クローンmNI-11は、ヒト臍帯血中のリンパ球 (特に、ナイーブTリンパ球)の新たな機能解析、新生児の免疫システムの解明、さらには再生医療分野での応用に有益な抗体と考えれられます。

• CD93 Gene - GeneCards | C1QR1 Protein | C1QR1 Antibody

Complete information for CD93 gene (protein-coding), CD93 molecule, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium ... cDNA cloning and primary structure ...

Related Pictures

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★リンクテーブル★

リンク元	「表面抗原分類」
関連記事	「CD」

「表面抗原分類」

　　[★]

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

「CD」

　　[★]

• 表面抗原分類 cluster of differentiation
• 膠原病 collagen disease
• 集合管 collecting duct
• クローン病 Crohn's disease