Fc fragment of IgE, low affinity II, receptor for (CD23) |
PDB rendering based on 1t8c. |
Available structures |
PDB |
Ortholog search: PDBe, RCSB |
List of PDB id codes |
1HLI, 1KJE, 1T8C, 1T8D, 2H2R, 2H2T, 4EZM, 4G96, 4G9A, 4GI0, 4GJ0, 4GJX, 4GK1, 4GKO, 4J6J, 4J6K, 4J6L, 4J6M, 4J6N, 4J6P, 4J6Q, 4KI1
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Identifiers |
Symbols |
FCER2 ; BLAST-2; CD23; CD23A; CLEC4J; FCE2; IGEBF |
External IDs |
OMIM: 151445 MGI: 95497 HomoloGene: 1517 ChEMBL: 2940 GeneCards: FCER2 Gene |
Gene ontology |
Molecular function |
• integrin binding
• IgE binding
• carbohydrate binding
• metal ion binding
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Cellular component |
• plasma membrane
• integral component of plasma membrane
• external side of plasma membrane
• extracellular vesicular exosome
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Biological process |
• positive regulation of humoral immune response mediated by circulating immunoglobulin
• Notch signaling pathway
• positive regulation of nitric-oxide synthase activity
• positive regulation of killing of cells of other organism
• positive regulation of nitric-oxide synthase biosynthetic process
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Sources: Amigo / QuickGO |
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RNA expression pattern |
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More reference expression data |
Orthologs |
Species |
Human |
Mouse |
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Entrez |
2208 |
14128 |
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Ensembl |
ENSG00000104921 |
ENSMUSG00000005540 |
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UniProt |
P06734 |
P20693 |
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RefSeq (mRNA) |
NM_001207019 |
NM_001253737 |
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RefSeq (protein) |
NP_001193948 |
NP_001240666 |
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Location (UCSC) |
Chr 19:
7.75 – 7.77 Mb |
Chr 8:
3.68 – 3.69 Mb |
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PubMed search |
[1] |
[2] |
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CD23, also known as Fc epsilon RII, or FcεRII, is the "low-affinity" receptor for IgE, an antibody isotype involved in allergy and resistance to parasites, and is important in regulation of IgE levels. Unlike many of the antibody receptors, CD23 is a C-type lectin. It is found on mature B cells, activated macrophages, eosinophils, follicular dendritic cells, and platelets.
There are two forms of CD23: CD23a and CD23b. CD23a is present on follicular B cells, whereas CD23b requires IL-4 to be expressed on T-cells, monocytes, Langerhans cells, eosinophils, and macrophages.[1]
Contents
- 1 Function
- 2 Clinical significance
- 3 References
- 4 Further reading
- 5 See also
Function
CD23 is known to have a role of transportation in antibody feedback regulation. Antigen that enters the blood stream is captured by antigen specific IgE antibodies. The IgE immune complexes that are formed bind to CD23 molecules on B cells, and are transported to the B cell follicles of the spleen. The antigen is then transferred from CD23+ B cells to CD11c+ antigen presenting cells. The CD11c+ cells in turn present the antigen to CD4+ T cells, which can lead to an enhanced antibody response.[2]
Clinical significance
The allergen responsible in dust mite allergy Der-p-1 is known to cleave CD23 from a cells surface. As CD23 is soluble, it can move freely and interact with cells in plasma. Recent studies have shown that increased levels of soluble CD23 cause the recruitment of non-sensitised B-cells in the presentation of antigen peptides to allergen-specific B-cells, therefore increasing the production of allergen specific IgE. IgE, in turn, is known to upregulate the cellular expression of CD23 and Fc epsilon RI (high-affinity IgE receptor).
In flow cytometry, CD23 is helpful in the differentiation of chronic lymphocytic leukemia (CD23-positive) from mantle cell leukemia (CD23-negative).[3] CD23 can also be demonstrated in germinal centre B-cells using immunohistochemistry, but it is not present in the resting cells of the surrounding mantle zone. Lymphomas arising from the mantle zone are generally negative for CD23, but most B-cell chronic lymphomocytic leukaemias and low-grade B-cell lymphomas are positive, allowing immunohistochemistry to distinguish these conditions, which otherwise have a similar appearance. Reed-Sternberg cells are usually positive for CD23.[4]
References
- ^ Lichtman AH, Abbas AK (2003). Cellular and molecular immunology. Philadelphia: Saunders. pp. 324–325. ISBN 0-7216-0008-5.
- ^ Henningsson F, Ding Z, Dahlin JS, Linkevicius M, Carlsson F, Grönvik KO, Hallgren J, Heyman B (2011). Metzger, Dennis W., ed. "IgE-Mediated Enhancement of CD4+ T Cell Responses in Mice Requires Antigen Presentation by CD11c+ Cells and Not by B Cells". PLoS ONE 6 (7): e21760. doi:10.1371/journal.pone.0021760. PMC 3130775. PMID 21765910.
- ^ Barna G, Reiniger L, Tátrai P, Kopper L, Matolcsy A (September 2008). "The cut-off levels of CD23 expression in the differential diagnosis of MCL and CLL". Hematol Oncol 26 (3): 167–70. doi:10.1002/hon.855. PMID 18381689.
- ^ Cooper K, Leong A S-Y (2003). Manual of diagnostic antibodies for immunohistology. London: Greenwich Medical Media. p. 95. ISBN 1-84110-100-1.
Further reading
- Kijimoto-Ochiai S (2002). "CD23 (the low-affinity IgE receptor) as a C-type lectin: a multidomain and multifunctional molecule". Cell. Mol. Life Sci. 59 (4): 648–64. doi:10.1007/s00018-002-8455-1. PMID 12022472.
- Schwarzmeier JD, Hubmann R, Düchler M et al. (2005). "Regulation of CD23 expression by Notch2 in B-cell chronic lymphocytic leukemia". Leuk. Lymphoma 46 (2): 157–65. doi:10.1080/10428190400010742. PMID 15621797.
- Maekawa N, Kawabe T, Sugie K et al. (1992). "Induction of Fc epsilon RII/CD23 on PHA-activated human peripheral blood T lymphocytes and the association of Fyn tyrosine kinase with Fc epsilon RII/CD23". Res. Immunol. 143 (4): 422–5. doi:10.1016/S0923-2494(05)80075-6. PMID 1387715.
- Rose K, Turcatti G, Graber P et al. (1992). "Partial characterization of natural and recombinant human soluble CD23". Biochem. J. 286 ( Pt 3) (Pt 3): 819–24. PMC 1132977. PMID 1417742.
- Maekawa N, Kawabe T, Sugie K et al. (1992). "Induction of Fc epsilon RII/CD23 on PHA-activated human peripheral blood T lymphocytes and association of fyn tyrosine kinase with Fc epsilon RII/CD23". International journal of tissue reactions 14 (3): 121–30. PMID 1446976.
- Sugie K, Kawakami T, Maeda Y et al. (1991). "Fyn tyrosine kinase associated with Fc epsilon RII/CD23: possible multiple roles in lymphocyte activation". Proc. Natl. Acad. Sci. U.S.A. 88 (20): 9132–5. doi:10.1073/pnas.88.20.9132. PMC 52666. PMID 1717997.
- Bettler B, Hofstetter H, Rao M et al. (1989). "Molecular structure and expression of the murine lymphocyte low-affinity receptor for IgE (Fc epsilon RII)". Proc. Natl. Acad. Sci. U.S.A. 86 (19): 7566–70. doi:10.1073/pnas.86.19.7566. PMC 298106. PMID 2529542.
- Kikutani H, Inui S, Sato R et al. (1987). "Molecular structure of human lymphocyte receptor for immunoglobulin E". Cell 47 (5): 657–65. doi:10.1016/0092-8674(86)90508-8. PMID 2877743.
- Ikuta K, Takami M, Kim CW et al. (1987). "Human lymphocyte Fc receptor for IgE: sequence homology of its cloned cDNA with animal lectins". Proc. Natl. Acad. Sci. U.S.A. 84 (3): 819–23. doi:10.1073/pnas.84.3.819. PMC 304307. PMID 2949326.
- Yokota A, Kikutani H, Tanaka T et al. (1988). "Two species of human Fc epsilon receptor II (Fc epsilon RII/CD23): tissue-specific and IL-4-specific regulation of gene expression". Cell 55 (4): 611–8. doi:10.1016/0092-8674(88)90219-X. PMID 2972386.
- Lüdin C, Hofstetter H, Sarfati M et al. (1987). "Cloning and expression of the cDNA coding for a human lymphocyte IgE receptor". EMBO J. 6 (1): 109–14. PMC 553364. PMID 3034567.
- Aubry JP, Pochon S, Gauchat JF et al. (1994). "CD23 interacts with a new functional extracytoplasmic domain involving N-linked oligosaccharides on CD21". J. Immunol. 152 (12): 5806–13. PMID 7515913.
- Lecoanet-Henchoz S, Gauchat JF, Aubry JP et al. (1995). "CD23 regulates monocyte activation through a novel interaction with the adhesion molecules CD11b-CD18 and CD11c-CD18". Immunity 3 (1): 119–25. doi:10.1016/1074-7613(95)90164-7. PMID 7621072.
- Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- Padlan EA, Helm BA (1994). "Modeling of the lectin-homology domains of the human and murine low-affinity Fc epsilon receptor (Fc epsilon RII/CD23)". Receptor 3 (4): 325–41. PMID 8142907.
- Trask B, Fertitta A, Christensen M et al. (1993). "Fluorescence in situ hybridization mapping of human chromosome 19: cytogenetic band location of 540 cosmids and 70 genes or DNA markers". Genomics 15 (1): 133–45. doi:10.1006/geno.1993.1021. PMID 8432525.
- Chirmule N, Kalyanaraman VS, Lederman S et al. (1993). "HIV-gp 160-induced T cell-dependent B cell differentiation. Role of T cell-B cell activation molecule and IL-6". J. Immunol. 150 (6): 2478–86. PMID 8450224.
- Förster HH, Wäsch R, Kretschmar T et al. (1996). "Genetic markers on chromosome 19p and prenatal diagnosis of HLA class II-deficient combined immunodeficiency". Pediatr. Res. 38 (5): 812–6. doi:10.1203/00006450-199511000-00029. PMID 8552454.
- Bajorath J, Aruffo A (1996). "Structure-based modeling of the ligand binding domain of the human cell surface receptor CD23 and comparison of two independently derived molecular models". Protein Sci. 5 (2): 240–7. doi:10.1002/pro.5560050207. PMC 2143337. PMID 8745401.
- Frémeaux-Bacchi V, Bernard I, Maillet F et al. (1996). "Human lymphocytes shed a soluble form of CD21 (the C3dg/Epstein-Barr virus receptor, CR2) that binds iC3b and CD23". Eur. J. Immunol. 26 (7): 1497–503. doi:10.1002/eji.1830260714. PMID 8766552.
See also
- Cluster of differentiation, a list of all the CD-numbered proteins
PDB gallery
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1t8c: Structure of the C-type lectin domain of CD23
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1t8d: Structure of the C-type lectin domain of CD23
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2h2r: Crystal structure of the human CD23 Lectin domain, apo form
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2h2t: CD23 Lectin domain, Calcium 2+-bound
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Cluster of differentiation by lineage
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Lymphoid |
B cell |
- Pre-B cell: CD10/CALLA
- CD79A
- mature: CD19
- CD20
- CD21/CR2
- CD23/FcεRII
- CD127
- CD40
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T/NK |
T cell |
- CD1
- CD4
- CD8
- CD13
- CD18
- CD26
- CD27
- CD28
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NK cell |
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All |
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All |
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Myeloid |
CFU-GM/
Myelomonocyte |
- CD11c
- CD14
- CD15
- CD31
- CD64
- CD68
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MEP |
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All (pan-myeloid) |
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Stem cell |
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cell/phys (coag, heme, immu, gran), csfs
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rbmg/mogr/tumr/hist, sysi/epon, btst
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drug (B1/2/3+5+6), btst, trns
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cell/phys/auag/auab/comp, igrc
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Transmembrane receptors: Immunoglobulin superfamily immune receptors
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Antibody receptor:
Fc receptor |
Epsilon (ε) |
- FcεRI
- (FcεRII is C-type lectin)
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Gamma (γ) |
- FcγRI
- FcγRII
- FcγRIII
- Neonatal
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Alpha (α)/mu (μ) |
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Secretory |
- Polymeric immunoglobulin receptor
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Antigen receptor |
B cells |
Antigen receptor |
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Co-receptor |
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Accessory molecules |
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T cells |
Ligands |
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Antigen receptor |
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Co-receptors |
- CD8 (with two glycoprotein chains CD8α and CD8β)
- CD4
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Accessory molecules |
- CD3
- CD3γ
- CD3δ
- CD3ε
- ζ-chain (also called CD3ζ and TCRζ)
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Cytokine receptor |
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Killer-cell IG-like receptors |
- KIR2DL1
- KIR2DL2
- KIR2DL3
- KIR2DL4
- KIR2DL5A
- KIR2DL5B
- KIR2DS1
- KIR2DS2
- KIR2DS3
- KIR2DS4
- KIR2DS5
- KIR3DL1
- KIR3DL2
- KIR3DL3
- KIR3DS1
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Leukocyte IG-like receptors |
- LILRA1
- LILRA2
- LILRA3
- LILRA4
- LILRA5
- LILRA6
- LILRB1
- LILRB2
- LILRB3
- LILRB4
- LILRB5
- LILRA6
- LILRA5
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B trdu: iter (nrpl/grfl/cytl/horl), csrc (lgic, enzr, gprc, igsr, intg, nrpr/grfr/cytr), itra (adap, gbpr, mapk), calc, lipd; path (hedp, wntp, tgfp+mapp, notp, jakp, fsap, hipp, tlrp)
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cell/phys/auag/auab/comp, igrc
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