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CD23
CD23
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FCER2
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesFCER2, BLAST-2, CD23, CD23A, CLEC4J, FCE2, IGEBF, Fc fragment of IgE receptor II, FCErII, Fc epsilon receptor II
External IDsOMIM: 151445; MGI: 95497; HomoloGene: 1517; GeneCards: FCER2; OMA:FCER2 - orthologs
Orthologs
SpeciesHumanMouse
Entrez

2208

14128

Ensembl

ENSG00000104921

ENSMUSG00000005540

UniProt

P06734

P20693

RefSeq (mRNA)

NM_001207019
NM_001220500
NM_002002

RefSeq (protein)

NP_001193948
NP_001207429
NP_001993

Location (UCSC)Chr 19: 7.69 – 7.7 MbChr 8: 3.73 – 3.74 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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.[5]

Function

[edit]

CD23 is known to have a role of transportation in antibody feedback regulation. Antigens which enter the blood stream can be 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.[6]

Clinical significance

[edit]

The allergen responsible in dust mite allergy—Der p 1—is known to cleave CD23 from a cell's 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).[7]

Patterns of CD23 (and CD21) expression by the follicular dendritic cells in follicular lymphoma.[8]

In flow cytometry, CD23 is helpful in the differentiation of chronic lymphocytic leukemia (CD23-positive) from mantle cell lymphoma (CD23-negative).[9] CD23 can also be demonstrated in germinal centre follicular dendritic cells using immunohistochemistry but is minimally expressed by benign germinal center B cells. In contrast to neoplastic mantle cells (which are negative for CD23), the resting cells of physiologic mantle zone express CD23. Paradoxically, Lymphomas arising from the mantle zone are generally negative for CD23, while most B-cell chronic lymphomocytic leukaemias are positive, allowing immunohistochemistry to distinguish these conditions, which otherwise have a similar appearance. Reed–Sternberg cells are usually positive for CD23.[10]

See also

[edit]

References

[edit]

Further reading

[edit]
[edit]
Revisions and contributorsEdit on WikipediaRead on Wikipedia

CD23

View on Grokipedia
from Grokipedia
CD23, also known as FcεRII, is the low-affinity receptor for immunoglobulin E (IgE), a type II transmembrane glycoprotein primarily expressed on B cells, where it regulates IgE synthesis and immune responses. Encoded by the FCER2 gene on chromosome 19p13.3, CD23 features a C-type lectin-like extracellular domain that binds IgE with low affinity (K_D ≈ 10⁻⁶–10⁻⁷ M) and also interacts with CD21 (complement receptor 2), enabling simultaneous ligand binding to modulate IgE homeostasis. It exists in two isoforms, CD23a and CD23b, differing in their N-terminal cytoplasmic tails, which influence signaling and endocytosis. CD23's structure includes a stalk region with leucine zipper motifs that facilitate trimerization, a single transmembrane , and a short cytoplasmic domain, allowing it to function as both a membrane-bound receptor and a soluble form upon proteolytic cleavage by enzymes like ADAM10. Soluble CD23 fragments (e.g., 37 kDa, 33 kDa) act as mitogenic factors, promoting B-cell growth and release, such as IL-1α and , while membrane-bound CD23 enhances via interactions with and like αvβ3. Expression is upregulated by interleukin-4 (IL-4), CD40 ligation, and Epstein-Barr , primarily on B lymphocytes, monocytes, and dendritic cells. In , CD23 exerts dual regulatory effects on IgE: trimeric forms upregulate IgE production through CD21 cross-linking on , whereas monomeric or cleaved forms inhibit it, contributing to feedback control in allergic responses. It also supports B-cell differentiation and is implicated in pathogen defense, such as antimycobacterial activity in macrophages. Clinically, elevated soluble CD23 levels serve as a prognostic marker in (CLL) and are associated with autoimmune diseases like and systemic (SLE). Therapeutic targeting, such as with anti-CD23 monoclonal antibodies like lumiliximab, has shown promise in treating CLL and allergic conditions by modulating IgE regulation.

Molecular biology

Gene

The FCER2 , encoding the low-affinity IgE receptor CD23, is situated on the short arm of human at cytogenetic band p13.2. It spans approximately 13 kb of genomic DNA and comprises 11 exons. Transcription from the FCER2 yields an mRNA transcript of approximately 1.7 kb, which encodes a 321-amino acid precursor protein that undergoes processing to form the mature CD23 . Alternative splicing and differential promoter usage produce isoforms such as CD23a and CD23b, differing in their N-terminal sequences. The FCER2 gene exhibits evolutionary conservation across mammalian species, with orthologs in mice designated as Fcer2a and Fcer2b, which display high sequence similarity to the human gene particularly in the region encoding the extracellular domain. A notable polymorphism in FCER2 is the R62W (rs2228137) in 4, which results in an substitution that confers resistance to proteolytic cleavage and has been associated with altered CD23 function in immune responses.

Protein structure and isoforms

CD23, also known as FcεRII, is a type II transmembrane encoded by the located on 19p13.2. The isoform, CD23a, consists of and features a short N-terminal cytoplasmic of 23 amino acids, a hydrophobic spanning 23 amino acids (residues 24–46), and a large extracellular region comprising approximately 275 . The extracellular domain includes a stalk region rich in charged residues and leucine zipper motifs that facilitate oligomerization, followed by a C-type lectin homology domain (also called the lectin domain) of about 150 amino acids at the C-terminus (residues 172–321). The lectin domain adopts a C-type lectin fold characterized by a β-sheet-rich with eight β-strands arranged in two antiparallel sheets and two α-helices, as revealed by and subsequent crystal structures. Although structurally homologous to calcium-dependent s, CD23 exhibits calcium-independent ligand binding, with its two potential calcium-binding sites remaining unoccupied in the apo form and showing only minor conformational adjustments upon calcium coordination. The stalk region's leucine zipper-like repeats enable the formation of trimers or higher-order oligomers on the cell surface, which are crucial for multivalent interactions. Two isoforms of CD23 arise from of the FCER2 transcript: CD23a, which is constitutively expressed primarily on B cells with a 23-amino-acid cytoplasmic containing a tyrosine-based motif, and CD23b, an inducible form upregulated by interleukin-4 (IL-4) or CD40 ligation in B cells and other leukocytes, featuring a 29-amino-acid cytoplasmic due to a 6-amino-acid insertion near the . Both isoforms share identical extracellular and transmembrane regions, allowing similar membrane-bound functions, but differ in intracellular signaling and trafficking; for instance, CD23a associates with the and undergoes efficient clathrin-mediated via AP-2 adaptor binding. Both isoforms can generate soluble forms (sCD23) through proteolytic shedding by metalloproteases such as ADAM10, which cleaves at specific sites near the (e.g., between Ala80 and Leu81 or Arg101 and Ser102), yielding fragments of 25–45 , including a predominant 37- species. These soluble fragments retain the lectin domain and stalk elements, often forming trimers that preserve ligand-binding capacity, though with reduced compared to the membrane-bound form. Smaller derivatives, such as 16- fragments from further cleavage (e.g., at Ser155/Ser156), have been observed in certain contexts but are less common.

Expression and regulation

Cellular expression

CD23 is predominantly expressed on the surface of mature B cells, including naive and subsets, as well as on activated macrophages, , follicular dendritic cells, and platelets. In contrast, expression is low or absent on T cells, plasma cells, and resting monocytes. However, CD23 can be upregulated on specific subsets, such as IgG1+ memory B cells, particularly in the context of type 2 immune responses associated with allergies. In terms of tissue distribution, CD23 is primarily found in lymphoid organs, including the spleen and lymph nodes, where it is associated with B cell-rich areas and follicular structures. It is also present on mucosal surfaces, such as in the intestinal epithelium, and can appear in the skin during inflammatory conditions. The pattern of CD23 expression is largely similar between humans and mice, with both species showing predominant localization on B cells, activated macrophages, and follicular dendritic cells. However, glycan-binding capabilities of CD23 vary across mammalian species; human CD23 shows no detectable binding to sugars, while mouse CD23 exhibits binding that is weaker than in species like cows. Expression on human B cells, for instance, can be induced by cytokines such as IL-4.

Regulation of expression

The expression of CD23 is tightly regulated at multiple levels, including transcriptional, post-transcriptional, post-translational, and developmental stages, ensuring appropriate control in immune responses. Interleukin-4 (IL-4) is a key that upregulates CD23 expression in B cells and monocytes through activation of the STAT6 signaling pathway, which promotes transcription of the FCER2 gene and preferentially induces the CD23b isoform. In contrast, interferon-gamma (IFN-γ) counteracts this by inhibiting IL-4-induced STAT6 activation and downregulating CD23 expression, thereby suppressing the overall levels of both membrane-bound and soluble forms. Post-transcriptional regulation involves microRNAs (miRNAs) that target FCER2 mRNA to suppress its stability and translation; for instance, miR-24, miR-30b, and miR-142-3p have been shown to reduce CD23 expression in macrophages and dendritic cells. Epigenetic modifications also play a critical role, with increased acetylation at the CD23b promoter correlating strongly with enhanced transcriptional activity and expression levels. Post-translational control occurs through proteolytic shedding, where the metalloprotease ADAM10 cleaves the extracellular domain of membrane-bound CD23, releasing soluble CD23 (sCD23) and thereby reducing surface expression; this process is upregulated under inflammatory conditions, such as exposure to IL-4 or . During development, CD23 expression is high on immature transitional s, particularly the CD23+ subset, which supports their survival and proliferation, but it is downregulated as these cells differentiate into plasma cells, marking a shift away from toward secretion.

Ligands and interactions

Binding to IgE

CD23 functions as the low-affinity receptor for the Fc portion of (IgE), with a (K_d) of approximately 10^{-6} to 10^{-7} M for monomeric CD23 binding to IgE. On B cells, where CD23 is expressed at relatively low density, it primarily binds free monomeric IgE to regulate IgE production. In contrast, on other cell types such as macrophages or epithelial cells, CD23 more effectively engages multimeric IgE, often in the form of IgE-antigen immune complexes, due to enhanced from receptor clustering. Recent structural studies have revealed that IgE adopts distinct open and closed conformations, with flexibility in the Cε2-Cε4 domains influencing binding specificity and affinity to CD23. The primary binding site for IgE resides within the -like domain of CD23, located at the extracellular "head" region. Structural studies, including the 2005 NMR solution structure of the human CD23 domain, reveal that key interactions involve residues such as Arg188, Arg224, Asp227, Glu257, and Tyr189 on CD23, which contribute significantly to the binding interface with the Cε3 domain of IgE. On the IgE side, critical residues include Arg376, Lys380, Asp409, and Glu412, which form hydrogen bonds and electrostatic interactions at the Cε3-Cε4 junction. The 2012 of the CD23 head domain bound to IgE-Fc further confirms a 2:1 , with two CD23 molecules asymmetrically engaging the IgE dimer without involving recognition typical of . Notably, despite its domain architecture, IgE binding by CD23 does not require calcium ions, as the interaction interface lacks coordination with metal sites present in classical . IgE binding to CD23 exhibits temperature sensitivity, with stronger association at lower temperatures such as compared to 37°C, likely due to reduced conformational dynamics or internalization at physiological temperatures. Oligomerization of CD23, particularly into trimers on the cell surface, dramatically increases binding to IgE—up to 10-fold higher than monomeric forms—through multivalent interactions that stabilize the complex. Soluble CD23 (sCD23), generated by proteolytic cleavage of membrane-bound CD23, retains a similar intrinsic affinity for IgE as the monomeric form but promotes IgE across epithelial barriers, facilitating delivery without the need for membrane anchoring.

Interactions with other molecules

CD23 interacts with CD21 (complement receptor 2, CR2) on B cells, forming a co-receptor complex that enhances B-cell activation through association with the ITAM-containing CD19 signaling pathway. This binding occurs via the domain of CD23 and the short consensus repeats of CD21, allowing CD23 to bridge IgE and CD21 in a ternary complex. CD23 binds to αv such as αvβ3 and αvβ5, facilitating and supporting interactions with components. These bindings, which involve an RGD-independent RKC motif in a disulfide-bonded loop at the N-terminus of the CD23 head domain, facilitate and support by immune cells. In certain mammalian species, CD23 exhibits glycan-binding activity, recognizing structures such as the GlcNAcβ1-2Man, which may contribute to recognition. However, this lectin-like function is minimal in humans due to evolutionary mutations in the CD23 gene that abolish sugar-binding capacity, unlike in mice where binding is weaker but present. Additionally, CD23 forms associations with IgE-CD21 complexes on B cells, promoting efficient transport of IgE without direct interactions with T cells.

Biological functions

Role in IgE homeostasis

CD23 plays a pivotal role in regulating IgE homeostasis by modulating its synthesis, binding, and clearance through both membrane-bound and soluble forms. Early studies in the 1980s demonstrated that monoclonal antibodies targeting CD23 inhibit IgE production in human cultures stimulated by interleukin-4, establishing CD23 as a key negative regulator of IgE responses in experimental models. Membrane-bound CD23 on downregulates IgE synthesis through multiple mechanisms. It competes allosterically with the high-affinity IgE receptor FcεRI for binding to free IgE, albeit with lower affinity (K_D ≈ 10^{-7} to 10^{-8} M compared to FcεRI's 10^{-10} to 10^{-11} M), thereby limiting IgE availability for sensitization of effector cells like mast cells and . Additionally, IgE-immune complexes co-ligate membrane CD23 with CD21 () on , inhibiting IgE production by suppressing proliferation. Soluble CD23 (sCD23), generated by proteolytic cleavage of membrane CD23, functions as a feedback inhibitor in IgE . sCD23 binds IgE with moderate affinity, sequestering it from high-affinity receptors such as FcεRI and thereby dampening IgE-mediated immune . Furthermore, membrane-bound CD23 promotes IgE by facilitating the of IgE-immune complexes in antigen-presenting cells, leading to their lysosomal degradation and reducing circulating IgE levels. Differences between CD23 isoforms influence IgE handling efficiency. The CD23b isoform, predominantly expressed in hematopoietic cells like B cells and dendritic cells, is more efficient at mediating the of IgE-antigen complexes compared to CD23a, directing them toward degradation pathways that accelerate IgE clearance.

Other immunological roles

CD23 plays a multifaceted role in B-cell beyond its involvement in IgE regulation. The interaction between membrane-bound CD23 and CD21 (also known as CR2) on the surface of B cells delivers co-stimulatory signals that promote B-cell . Soluble CD23 (sCD23), generated through proteolytic cleavage of the membrane form, further sustains the proliferation of activated mature B lymphocytes via autocrine mechanisms and enhances the differentiation of centroblasts toward the lineage, particularly in synergy with cytokines such as IL-1α. This process is mediated by specific residues in the CD23 stalk region, facilitating homotypic with a (K_D) of approximately 8.7 × 10⁻⁷ M. In parallel, CD23 acts as a negative regulator of B-cell receptor (BCR) signaling to prevent excessive B-cell activation and maintain immune . Upon BCR engagement, CD23 promotes B-cell contraction and the coalescence of BCR microclusters into central signaling-competent clusters, which dampens downstream signaling pathways. This regulation involves modulation of cytoskeleton reorganization; in the absence of CD23, as observed in CD23 knockout mice, B cells exhibit increased spreading, enhanced accumulation, and elevated phosphorylation of key signaling molecules such as (Btk) and WASP-interacting protein (WIP), leading to hyperactive BCR responses. These effects occur independently of IgE-immune complexes, underscoring CD23's intrinsic role in fine-tuning B-cell activation thresholds. CD23 also contributes to capture and presentation by facilitating and in key immune cells. On (FDCs), CD23 expression supports the retention and processing of antigens, enabling efficient presentation to cognate B cells within germinal centers through interactions with molecules in the CD23 stalk region (residues Glu48 to Lys59). Similarly, activated s bearing CD23 utilize to internalize antigens, enhancing their phagocytic capacity and subsequent presentation to T cells; this includes roles in antimycobacterial defense where CD23 promotes macrophage activation and pathogen clearance. CD23-positive B cells further transport captured antigens to splenic follicles, amplifying T- and B-cell responses. In the context of Th2-biased immune responses, CD23 influences survival and , as well as broader modulation. express CD23, and engagement of this receptor on their surface contributes to their and prolonged survival in inflammatory environments, supporting eosinophil recruitment and function during type 2 immunity. Additionally, sCD23 from activated cells induces the production of pro-inflammatory such as IL-1β and TNF-α by monocytes and macrophages. CD23 was initially identified as a B-cell marker in the context of Epstein-Barr virus (EBV) infection. EBV nuclear antigen 2 (EBNA-2) specifically transactivates CD23 expression in infected B cells, leading to upregulation of the CD23b isoform and contributing to the virus's ability to drive B-cell immortalization and proliferation. This superinduction of CD23 serves as an early indicator of EBV-mediated B-cell transformation, correlating with the establishment of latency and the outgrowth of lymphoblastoid cell lines.

Clinical significance

In allergic diseases

CD23 plays a pivotal role in allergic diseases through its cleavage by , which releases soluble CD23 (sCD23) and perturbs . The major Der p 1, a , specifically cleaves membrane-bound CD23 from the surface of human B cells, generating sCD23 fragments that can upregulate IgE synthesis by disrupting CD23's inhibitory feedback on B-cell activation. This proteolytic activity enhances the potency of by promoting Th2-skewed immune responses, including increased production and recruitment, thereby exacerbating allergic in conditions such as and . Elevated sCD23 levels are a hallmark of atopic conditions and strongly correlate with total and allergen-specific IgE concentrations. In patients with and , higher serum sCD23 reflects ongoing B-cell activation and is significantly associated with disease severity, as seen in studies of allergic children where sCD23 was markedly increased compared to non-allergic controls. Recent 2025 research further links CD23 expression on B-lymphocytes to specific IgE against pollen components like Bet v 1 and Phl p 1, showing a stronger correlation in patients treated with , suggesting CD23's involvement in modulating pollen-induced . In food allergies, CD23-expressing IgG1+ memory B cells are particularly relevant, as they are enriched in patients with and poised for class-switch recombination to produce pathogenic IgE. These cells, identified through single-cell sequencing, bear high-affinity receptors for peanut allergens like Ara h 2 and correlate with serum peanut-specific IgE levels, contributing to the persistence of allergic responses. CD23 dysregulation in is also associated with and impaired lung function. Increased numbers of CD23+IgG1+ B cells in asthmatic patients positively correlate with blood counts and inversely with forced expiratory volume in 1 second (FEV1), indicating a role in driving and progressive airway obstruction.

In hematological malignancies

CD23 serves as a valuable immunohistochemical and marker in the of several hematological malignancies, particularly in distinguishing B-cell neoplasms based on expression patterns. In (CLL) and small lymphocytic lymphoma (SLL), CD23 is typically expressed on the surface of neoplastic B cells, with positivity observed in approximately 87% of cases by on peripheral blood mononuclear cells. This positive expression aids in differentiating CLL/SLL from (MCL), which is characteristically CD23-negative, thereby facilitating accurate classification in CD5-positive small B-cell . Similarly, CD23 positivity is common in low-grade (grades 1-2), where it is detected in up to 83% of cases, further supporting its utility in pathological differentiation from CD23-negative counterparts like MCL. In mediastinal biopsies, CD23 expression helps distinguish primary mediastinal large B-cell lymphoma (a subtype of ) from classical , with recent analyses confirming its sensitivity of 85% and positive predictive value of 92% as an adjunct marker to histomorphology and other immunostains. This application remains relevant in 2025 diagnostic workflows for mediastinal masses, where CD23 positivity favors over . and are the primary methods for assessing CD23, with the former particularly effective in CLL where 80-90% of cases show membranous staining on CD19+ CD5+ B cells. CD23 expression is notably low in , occurring in only about 10% of plasma cell myeloma cases and specifically associated with abnormalities. In certain B-cell neoplasms, such as CLL, low CD23 expression correlates with advanced disease stages, higher counts, and prolymphocyte infiltration, providing prognostic insights alongside diagnostic value. These patterns underscore CD23's role as a targeted marker in hematological , enhancing precision in subtyping without reliance on broader B-cell expression profiles.

Therapeutic implications

Anti-CD23 monoclonal antibodies, such as lumiliximab, have been investigated for their ability to induce and (ADCC) in (CLL) cells, which overexpress CD23. In preclinical studies, lumiliximab demonstrated antitumor activity by triggering the intrinsic pathway in CD23-positive B cells. Phase I/II trials combining lumiliximab with , , and rituximab (FCR) in relapsed CLL patients reported an overall response rate of approximately 70% and complete remission in 50% of cases, suggesting enhanced efficacy over FCR alone. However, the phase III LUCID trial, which compared lumiliximab plus FCR to FCR monotherapy in untreated CLL, failed to meet its primary endpoint of improvement, with similar overall response rates (71% vs. 72%) and no significant clinical benefit, leading to discontinuation of development. In allergic diseases, strategies to enhance CD23 function aim to reduce IgE production by promoting membrane-bound CD23's inhibitory role in IgE homeostasis. Combining CD23 modulation with anti-IgE therapies like has shown potential for management, as omalizumab neutralizes free IgE and may indirectly support CD23-mediated regulation. Studies indicate that , an IL-4/IL-13 inhibitor, alters CD23 expression on B cells in patients, with higher CD23 levels on switched memory B cells correlating with specific IgE against allergens such as components, suggesting CD23's role in IgE regulation that could complement anti-IgE agents. Therapeutic targeting of CD23 is complicated by soluble CD23 (sCD23) forms, which arise from proteolytic shedding and can either inhibit or stimulate IgE synthesis depending on oligomerization, potentially counteracting membrane CD23 effects and reducing antibody specificity. Emerging chimeric antigen receptor () T-cell approaches indirectly modulate CD23 via B-cell targeting in CLL, where CD23-specific T cells, enhanced by , exhibit potent antileukemic activity in preclinical models without affecting normal B cells. Future directions include ADAM10 inhibitors to prevent CD23 shedding, thereby preserving membrane-bound CD23 and suppressing IgE secretion, as demonstrated where ADAM10 blockade reduced sCD23 release and IgE production in human B cells. Such inhibitors hold promise for allergic disorders by maintaining CD23's negative regulatory function on IgE .

References

  1. https://www.ncbi.nlm.nih.gov/gene/2208
  2. https://pmc.ncbi.nlm.nih.gov/articles/PMC2212946/
  3. https://pmc.ncbi.nlm.nih.gov/articles/PMC2990925/
  4. https://onlinelibrary.wiley.com/doi/10.1111/j.1365-2249.2010.04210.x
  5. https://www.atsjournals.org/doi/10.1164/ajrccm.161.3.9810056
  6. https://www.atsjournals.org/doi/full/10.1165/rcmb.2013-0112OC
  7. https://www.uniprot.org/uniprotkb/P06734/entry
  8. https://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=2935
  9. https://rupress.org/jem/article/202/6/751/52846/The-structure-of-human-CD23-and-its-interactions
  10. https://pubmed.ncbi.nlm.nih.gov/16765898/
  11. https://pubmed.ncbi.nlm.nih.gov/12070780/
  12. https://pmc.ncbi.nlm.nih.gov/articles/PMC2988358/
  13. https://www.sciencedirect.com/science/article/pii/S0021925820636365
  14. https://www.pathologyoutlines.com/topic/cdmarkerscd23.html
  15. https://www.sciencedirect.com/topics/neuroscience/cd23
  16. https://pubmed.ncbi.nlm.nih.gov/8645974/
  17. https://www.frontiersin.org/journals/immunology/articles/10.3389/fimmu.2021.744573/full
  18. https://www.science.org/doi/10.1126/scitranslmed.adi0673
  19. https://www.jacionline.org/article/S0091-6749(15)01251-8/fulltext
  20. https://www.atsjournals.org/doi/full/10.1164/ajrccm.161.3.9905046
  21. https://pmc.ncbi.nlm.nih.gov/articles/PMC6791321/
  22. https://pmc.ncbi.nlm.nih.gov/articles/PMC1173127/
  23. https://pubmed.ncbi.nlm.nih.gov/10713330/
  24. https://www.sciencedirect.com/science/article/abs/pii/S0145212699001915
  25. https://www.pnas.org/doi/10.1073/pnas.96.19.10800
  26. https://pubmed.ncbi.nlm.nih.gov/11067899/
  27. https://www.atsjournals.org/doi/full/10.1165/rcmb.2004-0195OC
  28. https://journals.sagepub.com/doi/full/10.1177/1753425916661042
  29. https://pubmed.ncbi.nlm.nih.gov/23583387/
  30. https://www.sciencedirect.com/science/article/abs/pii/S0006291X13006062
  31. https://pmc.ncbi.nlm.nih.gov/articles/PMC2582392/
  32. https://www.sciencedirect.com/science/article/pii/S0021925820467286
  33. https://pubmed.ncbi.nlm.nih.gov/11809735/
  34. https://pubmed.ncbi.nlm.nih.gov/34925321/
  35. https://ashpublications.org/blood/article/137/9/1166/474072/Plasmablasts-derive-from-CD23-activated-B-cells
  36. https://www.nature.com/articles/s41467-019-13815-w
  37. https://www.jacionline.org/article/S0091-6749(19)31049-8/fulltext
  38. https://www.frontiersin.org/journals/allergy/articles/10.3389/falgy.2023.1117611/full
  39. https://onlinelibrary.wiley.com/doi/10.1111/imr.70031
  40. https://www.jbc.org/article/S0021-9258(20)63093-9/fulltext
  41. https://www.pnas.org/doi/10.1073/pnas.1207278109
  42. https://pubmed.ncbi.nlm.nih.gov/12574349/
  43. https://www.sciencedirect.com/science/article/pii/S0016508506007116
  44. https://www.jbc.org/article/S0021-9258(20)58804-2/fulltext
  45. https://pubmed.ncbi.nlm.nih.gov/1689660/
  46. https://pmc.ncbi.nlm.nih.gov/articles/PMC8359454/
  47. https://onlinelibrary.wiley.com/doi/10.1111/all.14724
  48. https://www.nature.com/articles/srep25629
  49. https://pubmed.ncbi.nlm.nih.gov/19805542/
  50. https://www.sciencedirect.com/topics/immunology-and-microbiology/cd23
  51. https://europepmc.org/article/pmc/304889
  52. https://pubmed.ncbi.nlm.nih.gov/2984280/
  53. https://pubmed.ncbi.nlm.nih.gov/7489763/
  54. https://pubmed.ncbi.nlm.nih.gov/8582422/
  55. https://pubmed.ncbi.nlm.nih.gov/40432597/
  56. https://pmc.ncbi.nlm.nih.gov/articles/PMC12465039/
  57. https://haematologica.org/article/view/820/4663
  58. https://mayoclinic.elsevierpure.com/en/publications/cd23-expression-in-follicular-lymphoma-clinicopathologic-correlat
  59. https://pubmed.ncbi.nlm.nih.gov/19223373/
  60. https://www.ejcancer.com/article/S0959-8049%2825%2900150-9/fulltext
  61. https://pmc.ncbi.nlm.nih.gov/articles/PMC7810253/
  62. https://pubmed.ncbi.nlm.nih.gov/20064156/
  63. https://onlinelibrary.wiley.com/doi/full/10.1002/hon.2244
  64. https://ashpublications.org/blood/article/111/3/1594/25567/Mediation-of-apoptosis-by-and-antitumor-activity
  65. https://ascopubs.org/doi/10.1200/jco.2008.26.15_suppl.7003
  66. https://pubmed.ncbi.nlm.nih.gov/25130401/
  67. https://www.jidonline.org/article/S0022-202X%2820%2932044-3/fulltext
  68. https://pmc.ncbi.nlm.nih.gov/articles/PMC10363832/
  69. https://www.tandfonline.com/doi/full/10.1080/1547691X.2025.2531794
  70. https://www.jbc.org/article/S0021-9258%2820%2954392-5/fulltext
  71. https://pmc.ncbi.nlm.nih.gov/articles/PMC9828187/
  72. https://pmc.ncbi.nlm.nih.gov/articles/PMC3378639/
  73. https://pmc.ncbi.nlm.nih.gov/articles/PMC3963393/
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