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C-Type Lectin-Like Receptors As Emerging Orchestrators of Sterile Inflammation Represent Potential Therapeutic Targets

Elise Chiffoleau

Frontiers in Immunology · 2018 · Review

doi:10.3389/fimmu.2018.00227

Abstract

Over the last decade, C-type lectin-like receptors (CTLRs), expressed mostly by myeloid cells, have gained increasing attention for their role in the fine-tuning of both innate and adaptive immunity. Not only, CTLRs recognize pathogen-derived ligands to protect against infection, but also endogenous ligands such as self-carbohydrates, proteins or lipids to control homeostasis and tissue injury. Interestingly, CTLRs act as antigen-uptake receptors via their carbohydrate recognition domain for internalization and subsequent presentation to T-cells. Furthermore, CTLRs signal through a complex intracellular network leading to the secretion of a particular set of cytokines that differently polarizes downstream effector T-cell responses according to the ligand and pattern recognition receptor co-engagement. Thus, by orchestrating the balance between inflammatory and resolution pathways, CTLRs are now considered as driving players of sterile inflammation whose dysregulation leads to the development of various pathologies such as auto-immune diseases, allergy or cancer. For examples, the macrophage-inducible C-type lectin (MINCLE), by sensing glycolipids released during cell-damage, promotes skin allergy and the pathogenesis of experimental autoimmune uveoretinitis. Besides, recent studies described that tumors use physiological process of the CTLRs dendritic cells-associated C-type lectin-1 DECTIN-1 and MINCLE to locally suppress myeloid cell activation and promote immune evasion. Therefore, we aim here to overview the current knowledge of the pivotal role of CTLRs in sterile inflammation with special attention given to the “Dectin-1” and “Dectin-2” families. Moreover, we will discuss the potential of these receptors as promising therapeutic targets to treat a wide range of acute and chronic diseases.

Full text

From PubMed Central, U.S. National Library of Medicine, as current on Oct 26, 2026. Paragraph numbers are ours, so an answer can point at one.

Introduction

C-type lectin receptors (CLRs) are a large family of transmembrane and soluble receptors that contain one or more carbohydrate-recognition domain able to recognize a wide variety of glycans on pathogens or on self-proteins. The hallmark of classical CLRs is the dependence on Ca2+ for glycan recognition. However, many other CLRs lack the coordinated Ca2+ ions and are therefore referred as C-type lectin-like molecules. These C-type lectin-like receptors (CTLRs) are still able to recognize carbohydrates but independently of Ca2+ but also recognize more diverse ligands such as lipids and proteins. Of particular interest for their role in coupling both innate and adaptive immunity, are the CTLR genes of the “Dectin-1” and “Dectin-2” families localized on the telomeric region of the natural killer cluster of genes. These two groups of CTLRs are expressed mostly by cells of myeloid lineage such as monocytes, macrophages, dendritic cells (DCs), and neutrophils. CTLRs not only serve as antigen-uptake receptors for internalization and presentation to T cells but also trigger multiple signaling pathways leading to NF-κB, type I interferon (IFN), and/or inflammasome activation. This leads, in turn, to the production of pro- or anti-inflammatory cytokines and chemokines, subsequently fine tuning adaptive immune responses. CTLRs can signal either directly, through integral signaling domains, or indirectly, by associating with adaptor molecules. As illustrated in Figure 1, activation of immune-receptor tyrosine-based activation motif (ITAM) directly or via adaptor proteins such as FcγR, leads to the recruitment of SYK family kinases and the formation of the Card9/Bcl10/Malt1 complex that downstream activates NF-κB pathway and various cellular responses. By contrast, activation of immune-receptor tyrosine-based inhibition motif (ITIM) induces the recruitment and activation of protein tyrosine phosphatases such as SHP-1 and SHP-2 and the dephosphorylation of motifs. Consequently, ITIM signaling can inhibit cellular activation mediated by other immunoreceptors to tightly regulate immune response. Such checkpoints allow to prevent uncontrolled immune responses that may lead to harmful, or even fatal, consequences. In addition, some CTLRs were also reported to signal via SYK-independent pathway through the serine/threonine kinase RAF-1 to drive particular Th differentiation. Besides, by integrating simultaneous signals from other pattern recognition receptors (PRRs), CTLRs can exert synergistic or antagonistic response to achieve appropriate biological responses. This cross talk is regulated by the level and localization of their expression, by their interaction and by their collaborative or conflicting signaling. To date, CTLRs “Dectin” families were best known for their involvement in host defense as referred in these excellent reviews. However, over recent years, these receptors have gained growing interest for their ability to respond also to a wide variety of endogenous ligands (Figure 1). Identification of self-glycans, lipids, or proteins expressed or released by modified or damaged cells reinforced the hypothesis for their implication in sterile inflammation whose dysregulation foster the development of wide range of diseases. In this mini review, we aim to focus on some of the CTLRs of the “Dendritic cell-associated C-type lectin (Dectin)” families, discussing the recent discoveries on their implication in the control of tissue injury, autoimmune diseases, or tumorigenesis. In addition, we will underscore their therapeutic potential and impact on human health.

DECTIN-1 (Alias CLEC7A, CLECSF12, CANDF4, CD369, BGR)

The CTLR, DECTIN-1 has been reported to be enhanced by pro-inflammatory conditions and to be a potent inducer of Th1 and/or Th17 responses in response to pathogens. Thereby, pathogenic ligands of DECTIN-1 are currently used to bolster immune responses notably in cancer. For example, administration of β glucans was shown to inhibit tumor growth in murine carcinoma models, in human melanoma, neuroblastoma, mastocytosis, and lymphoma xenograft models and in ovarian, breast, lung, and gastric cancer. Mechanistically, β glucans were shown to convert immunosuppressive macrophages into an M1-like antitumoral phenotype, to promote NK and CD8+ T cell cytotoxicity as well as a decrease in myeloid-derived suppressor cells and regulatory T cells. Interestingly, Zhao et al. recently reported that β glucans upregulate particularly the expression of TNFSF15 and OX40L in DCs in mice, thus promoting efficient Th9 priming and potent anti-melanoma response following vaccination. On the contrary, some investigations have described an inhibitory function of DECTIN-1 in sterile inflammation notably during hepatic fibrosis and hepatocellular carcinoma. Authors showed that DECTIN-1 inhibit TLR4 signaling and downstream inflammation such as TNFα, IL-6, and chemokines secretion. Moreover, DECTIN-1 was reported to be associated with mechanisms of peritumoral immune tolerance by programming suppressive macrophages in pancreatic ductal adenocarcinoma. Strikingly, they showed that blockade of DECTIN-1 or its endogenous ligand Galectin-9, both strongly expressed on infiltrating myeloid cells and tumor, delayed tumor progression and extended mice survival. A similar tolerogenic signal of DECTIN-1 has been shown in myeloid cells in response to mucus in the intestine through interaction with Galectin-3. In addition, DECTIN-1-deficient mice were described to exacerbate inflammation in a model of colitis suggesting an important role of DECTIN-1 in gut homeostasis. Therefore, DECTIN-1 seems to act as double-edged swords on the regulation of inflammation. Such discrepancy may depend of the type of the response, the nature and the property of the ligands, and of the complex signal network that integrates diverse engaged PRRs.

LOX-1 (Alias OLR-1, CLEC8A)

The CTLR lectin-like oxidized low-density lipoprotein receptor-1 (LOX-1) is particularly expressed by endothelial cells and platelets and is upregulated during inflammatory and pathological conditions. By recognizing oxidized and acetylated low-density lipoproteins, LOX-1 is largely described to play critical functions in vascular diseases, including atherosclerosis. However, recent investigations have revealed that LOX-1 is also expressed by human macrophages and DCs, and its triggering increases secretion of IL-6 to potentiate B-cell class-switch. Moreover, LOX-1 enhances CCR10, APRIL, and BAFF secretion for plasma cell differentiation and migration to mucosal site. In line with these findings, targeting influenza histocompatibility antigen-1 to LOX-1 elicits antigen-specific protective antibody response to virus in macaques suggesting a good candidate for vaccine development. Besides, several studies have reported a high expression of LOX-1 in various tumors including gastric, colorectal, and prostate cancers, which correlates with a poor prognosis in patients. Functionally, LOX-1 was shown to promote tumor angiogenesis, metastasis, and the migration and invasion of gastric cancer cells by notably driving epithelial–mesenchymal transition. Interestingly, LOX-1 was recently identified to be particularly expressed by potent polymorphonuclear myeloid-derived suppressor cells from blood and tumor of patients with non-small cell lung or head neck cancer and to be associated with worse survival. In fact, LOX-1 expression seems to be upregulated following endoplasmic reticulum stress that occurs during hypoxia or nutrient deprivation inside tumors. These data render this marker an attractive therapeutic target as well as a diagnostic tool for cancer screening.

CLEC-1 (Alias CLEC1, CLEC1A)

Although the C-type lectin-like receptor-1 (CLEC-1) was identified a long time ago, the downstream signaling and ligand(s) remain uncharacterized. We and others described CLEC-1 expression in human and rodent by myeloid cells such as monocytes, DC, and macrophages but also by endothelial cells. CLEC-1 expression is decreased by pro-inflammatory stimuli and is enhanced by TGFβ. Interestingly, CLEC-1 was found to be expressed mostly intracellular particularly in human endothelial cells and neutrophils, suggesting the requirement of particular conditions for cell-surface expression or for recycling from intracellular pools. Alternatively, CLEC-1 may play a role in intracellular organelles. Using CLEC-1-deficient rodents, we showed that disruption of CLEC-1 signaling enhances Il12p40 subunit expression in DCs and accordingly exacerbates downstream CD4+ Th1 and Th17 responses following in vivo immunization with exogeneous antigens.

CLEC-2 (Alias CLEC2, CLEC2B, CLEC1B)

C-type lectin-like receptor 2 (CLEC-2) is found on platelets and DCs and is largely described for its interaction with its endogeneous ligand podoplanin expressed by lymphatic endothelial cells, myeloid cells, and fibroblast reticular cells. The CLEC-2/Podoplanin axis was shown to be critical in platelet activation, lymph node microarchitecture, reticular network, and vascular integrity. Besides, this interaction promotes tumor cell-induced platelet aggregation, tumor growth, and metastasis in various types of cancer including brain, lung, and larynx. Furthermore, CLEC-2 is enhanced by inflammation, promotes DC migration and together with LPS enhances the production of the anti-inflammatory cytokine IL-10 suggesting also a role in the resolution of inflammation.

MICL (Alias CLEC12A, DCAL-2, CLL1, CLL-1, KLRL1)

Myeloid inhibitory C-type lectin-like receptor (MICL) is expressed predominantly by granulocytes and monocytes, and its expression is downregulated by pro-inflammatory stimuli. MICL recruits inhibitory phosphatases and again seems to differently shape T-cell responses according to the cross talk with simultaneous PRR signals. Chen and colleges demonstrated that co-engagement of MICL with TLR4 suppress IL-12 expression in human DCs and downstream Th1 polarization whereas co-engagement with CD40 does the opposite. Interestingly, putative endogenous ligands of MICL were identified on various mouse tissues in steady-state conditions, proposing a role for MICL in the control of homeostasis and self-tolerance. Corroborating this notion, an inhibitory function for MICL has been put in light in an in vivo model of induced rheumatoid arthritis. In an original way, MICL was proposed to modulate myeloid cell activation threshold by acting as an autoantigen during arthritis development.

CLEC9A (Alias DNGR1, DNGR-1, CD370)

CLEC9A is selectively expressed on the mouse subsets of CD8α+ and CD103+ DCs, and on their human BDCA3+ DCs counterparts. CLEC9A expression is lost further TLR-induced maturation. Importantly, CLEC9A by recognizing F-actin released by necrotic cells is capable of internalizing bound dead cell-associated antigens for cross-presentation to CD8+ T cells. Thereby, CLEC9A has been demonstrated to be a powerful target for peptide vaccination to boost antitumor immunity. Interestingly, it has recently been shown that necrotic debris that accumulated during atherosclerosis development, trigger through CLEC9A, the downregulation of the anti-inflammatory cytokine IL-10 and the disease progression.

DCIR (Alias CLEC4A, CLECSF6, CD367, LLIR)

DC immunoreceptor (DCIR) is expressed on monocytes, neutrophils, DC, and plasmacytoid DCs, and its expression is decreased by pro-inflammatory stimuli. The human genome encodes only a single DCIR gene, whereas the mouse genome presents four DCIR-like genes (DCIR1–4). DCIR via its canonical ITIM domain is largely recognized to exert inhibitory cross talk with other PRRs to maintain immune homeostasis and prevent excessive detrimental inflammation and immunopathogenesis. DCIR inhibits TLR8-induced IL-12 and TNFα production in human moDCs following cross-linking with monoclonal antibody. Furthermore, DCIR1 KO mice develop a late spontaneous autoimmune disease associated with elevated levels of autoantibodies, are more susceptible to collagen-induced arthritis, and aggravated experimental autoimmune encephalomyelitis. These effects were described to be mediated at least by unrestrained growth of DC population in these mice. However, in support for a role of DCIR in tempering DC activation, a recent study demonstrated that DCIR2 selectively expressed by mouse CD8α− DCs, strongly moderates pro-inflammatory and downstream T-cell responses. In vivo, DCIR2-deficient mice are more susceptible to endotoxic shock and aggravate experimental autoimmune encephalomyelitis development by increasing both Th1 and Th17 differentiation. Authors demonstrated that putative endogeneous ligands of DCIR are expressed also on cell surface of DCs. In line with these data, DCIR2 was described in DCs to sustain STAT-1 type I IFN signaling leading to a reduction of IL-12p70 production and Th1 differentiation in response to endogeneous ligand(s) released during cell culture. Therefore, by regulating also the IFN responses, DCIR may be a critical player in the control of a number of inflammatory diseases. Interestingly, DCIR was also reported to bind to commensal intestinal microbes. However, DCIR-deficient mice only exhibit a slightly increased severity of colitis in a dextran sulfate sodium model.

DECTIN-2 (Alias CLEC6A, CLEC4N, CLECSF10)

Several studies suggest a role for DC-associated C-type lectin-2 (DECTIN-2) in the inhibition of sterile inflammation. DECTIN-2 is enhanced in pro-inflammatory conditions and was shown notably to bind to a putative ligand on regulatory CD4+CD25+ T cells to mediate ultraviolet radiation-induced tolerance. In addition, DECTIN-2 recognizes glycan mannose on the lysosomal enzyme β-glucuronidase, known to moderate arthritis pathogenesis by preventing accumulation of pro-inflammatory glycosaminoglycans within inflamed joint tissue. Thus, β-glucuronidase released by dead myeloid cells following tissue damage may act via DECTIN-2 as an inhibitory loop in DCs to temper inflammation. Besides, polymorphism of this enzyme was reported to be associated with mucopolysaccharidoses characterized by a pro-inflammatory response. In addition, a role for DECTIN-2 in suppression of liver metastasis has been highlighted by its ability to phagocytose cancer cells via CD11b F4/80 Kupffer cells during extravasation step.

BDCA-2 (Alias CLEC4C, BDCA2, CD303, CLECSF11, CLECSF7)

Interestingly, blood DC antigen-2 (BDCA-2) is the most specific marker for human plasmacytoid DC but intriguingly is not expressed in mice. Expression of BDCA-2 is downregulated following maturation. Surprisingly, unlike many other ITAM-coupled receptors, signaling through BDCA-2 inhibits activation of the NF-κB pathway and the production of type I IFNs and cytokines in response to TLR9 ligands or following recognition of galactose terminal residues notably expressed on tumor cells. BDCA-2 engagement was also shown to block TRAIL-mediated cytotoxic activity. In an interestingly way, BDCA-2 was suggested to function as an Fc receptor by binding glycans on immunoglobulins G and thus, dampens down inflammation in response to rising levels of serum immunoglobulins G.

MINCLE (Alias CLEC4E, CLECSF9)

Macrophage-inducible C-type lectin (MINCLE) is an ITAM-coupled CTLR that forms a heterodimer with the macrophage C-type lectin (MCL). MINCLE expression is enhanced after exposure to pro-inflammatory stimuli or cellular stresses and is translocated to the cell surface via interaction with the stalk region of MCL. MINCLE was shown to activate in DCs both NF-κB and inflammasome to greatly enhance IL-1β expression in synergy with TLR7/8 (R848) or following in vivo immunization with Freund adjuvant. MINCLE senses self-damage by recognizing “unfamiliar” glycolipids that are not present in the extracellular milieu under normal, healthy conditions. For example, MINCLE was reported to bind crystalline cholesterol present in atheriosclerotic plaques that are associated with inflammation and macrophage infiltrates. Likewise, as depicted in Figure 2, MINCLE is enhanced on plasmacytoid DCs following skin damage and by recognizing cholesterol sulfate, induces IL-1 α and β secretion, and promotes skin allergy and allergic contact dermatitis. Moreover, MINCLE was also reported to bind to the ubiquitous intracellular metabolite β-glucosylceramide released by damaged cells to promote production of pro-inflammatory cytokines by myeloid cells. In an opposite way, recent investigations have revealed that MINCLE rather than purely inducing pro-inflammatory responses can also promote the expression of the anti-inflammatory cytokines IL-10. In addition, MINCLE was reported to counter regulate pro-inflammatory signaling pathways mediated by DECTIN-1 to temper IL12p35 production. Therefore, MINCLE seems to also exert opposite role on immune responses depending of the ligands and PRR interference. This dual effect is illustrated by the recognition by MINCLE of the spliceosome-associated protein 130 (SAP130), a component of small nuclear ribonucleoprotein released during non homeostatic cell death. On one hand, MINCLE/SAP130 axis was shown to be involved in the pathogenesis of inflammation during tissue damages or ischemia/reperfusion and to contribute to the development of experimental autoimmune uveoretinitis. This pro-inflammatory side of MINCLE is supported by a high expression of MINCLE in patients with rheumatoid arthritis and by the link to arthritis of the rat chromosome 4q42 encoding Mincle. On the other hand, in the context of cancer, MINCLE/SAP130 axis was reported to be pro-tumorigenic in mouse and human pancreatic ductal adenocarcinoma. Both MINCLE and SAP130 released by programmed necrosis are highly expressed in mouse and human carcinoma and as depicted in Figure 2, this interaction leads to an immunosuppressive reprogramming of infiltrating myeloid cells. Future research is required to provide insight as to how MINCLE needs to integrate with other PRR signals to differently define the type of immune response.

Therapeutic Potential of CTLRs

Therefore, by their capacity to present antigen and ensure the balance between cellular activation and suppression, CTLRs have emerged as challenging pharmacological targets to treat a wide variety of diseases governed by sterile inflammation including cancers, autoimmune diseases or allergy. Ligands such as carbohydrate structures, antibodies, or mimetic peptides could be therapeutically exploited as agonists or antagonists of CTLR signaling. As previously mentioned, the DECTIN-1 agonist β-glucans is used to elicit of potent antitumor immune responses in various types of cancer. Furthermore, CTLRs such as DEC-205 or CLEC9A have been exploited for the in vivo delivery target of vaccine antigens in cancer. In addition, synthetic ligands of MINCLE were generated to specifically enhance immune response. Besides, several specific antibodies generated against cancer-specific highly glycosylated podoplanin were shown to efficiently block the CLEC-2/Podoplanin interaction, subsequent platelet aggregation and tumor metastasis. Importantly, a particular antibody that reacts with podoplanin-expressing cancer cells but not with the one from normal cells has been successfully generated and will be useful for molecular targeting therapy against podoplanin-expressing cancer cells only. However, since CTLRs have overlapping ligands that induce distinct and even contrasting immune responses, antibodies targeting specific CTLRs could be more appropriate. Also, inhibitors such as recombinant peptide spanning the CTLR binding region and modulating the receptor–ligand interaction could be considered. Only a few drug-like molecules have been developed for the CTLR family but studies indicate high in silico druggability scores as well as high experimental hit rates from peptide fragment screenings.

To conclude, CTLR modulation seems to represent promising strategy for disease management although attempts at identifying endogenous ligands as well as efforts to elucidate their role in sterile inflammation are still warrant.

Author Contributions

The author confirms being the sole contributor of this work and approved it for publication.

Conflict of Interest Statement

The author declares that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.

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    Not in our library10.1371/journal.pone.0106219

  43. 43.

    Liang M Zhang P Fu J. Up-regulation of LOX-1 expression by TNF-alpha promotes trans-endothelial migration of MDA-MB-231 breast cancer cells. Cancer Lett (2007 ) 258(1):31–7.

    Not in our library10.1016/j.canlet.2007.08.003

  44. 44.

    Condamine T Dominguez GA Youn J-I Kossenkov AV Mony S Alicea-Torres K Lectin-type oxidized LDL receptor-1 distinguishes population of human polymorphonuclear myeloid-derived suppressor cells in cancer patients. Sci Immunol (2016 ) 1(2):aaf8943.

    Not in our library10.1126/sciimmunol.aaf8943

  45. 45.

    Colonna M Samaridis J Angman L. Molecular characterization of two novel C-type lectin-like receptors, one of which is selectively expressed in human dendritic cells. Eur J Immunol (2000 ) 30(2):697–704.

    Not in our library10.1002/1521-4141(200002)30:2<697::aid-immu697>3.0.co;2-m

  46. 46.

    Sobanov Y Bernreiter A Derdak S Mechtcheriakova D Schweighofer B Duchler M A novel cluster of lectin-like receptor genes expressed in monocytic, dendritic and endothelial cells maps close to the NK receptor genes in the human NK gene complex. Eur J Immunol (2001 ) 31(12):3493–503.

    Not in our library10.1002/1521-4141(200112)31:12<3493::aid-immu3493>3.0.co;2-9

  47. 47.

    Flornes LM Nylenna O Saether PC Daws MR Dissen E Fossum S. The complete inventory of receptors encoded by the rat natural killer cell gene complex. Immunogenetics (2010 ) 62(8):521–30.

    Not in our library10.1007/s00251-010-0455-y

  48. 48.

    Thebault P Lhermite N Tilly G Le Texier L Quillard T Heslan M The C-type lectin-like receptor CLEC-1, expressed by myeloid cells and endothelial cells, is up-regulated by immunoregulatory mediators and moderates T cell activation. J Immunol (2009 ) 183(5):3099–108.

    Not in our library10.4049/jimmunol.0803767

  49. 49.

    Suzuki-Inoue K Inoue O Ozaki Y. Novel platelet activation receptor CLEC-2: from discovery to prospects. J Thromb Haemost (2011 ) 9(Suppl 1):44–55.

    Not in our library10.1111/j.1538-7836.2011.04335.x

  50. 50.

    Herzog BH Fu J Wilson SJ Hess PR Sen A McDaniel JM Podoplanin maintains high endothelial venule integrity by interacting with platelet CLEC-2. Nature (2013 ) 502(7469):105–9.

    Not in our library10.1038/nature12501

  51. 51.

    Benezech C Nayar S Finney BA Withers DR Lowe K Desanti GE CLEC-2 is required for development and maintenance of lymph nodes. Blood (2014 ) 123(20):3200–7.

    Not in our library10.1182/blood-2013-03-489286

  52. 52.

    Acton SE Farrugia AJ Astarita JL Mourao-Sa D Jenkins RP Nye E Dendritic cells control fibroblastic reticular network tension and lymph node expansion. Nature (2014 ) 514(7523):498–502.

    Not in our library10.1038/nature13814

  53. 53.

    Suzuki-Inoue K Kato Y Inoue O Kaneko MK Mishima K Yatomi Y Involvement of the snake toxin receptor CLEC-2, in podoplanin-mediated platelet activation, by cancer cells. J Biol Chem (2007 ) 282(36):25993–6001.

    Not in our library10.1074/jbc.m702327200

  54. 54.

    Christou CM Pearce AC Watson AA Mistry AR Pollitt AY Fenton-May AE Renal cells activate the platelet receptor CLEC-2 through podoplanin. Biochem J (2008 ) 411(1):133–40.

    Not in our library10.1042/bj20071216

  55. 55.

    Kato Y Kaneko MK Kunita A Ito H Kameyama A Ogasawara S Molecular analysis of the pathophysiological binding of the platelet aggregation-inducing factor podoplanin to the C-type lectin-like receptor CLEC-2. Cancer Sci (2008 ) 99(1):54–61.

    Not in our library10.1111/j.1349-7006.2007.00634.x

  56. 56.

    Lowe KL Navarro-Nunez L Watson SP. Platelet CLEC-2 and podoplanin in cancer metastasis. Thromb Res (2012 ) 129(Suppl 1):S30–7.

    Not in our library10.1016/s0049-3848(12)70013-0

  57. 57.

    Mishima K Kato Y Kaneko MK Nishikawa R Hirose T Matsutani M. Increased expression of podoplanin in malignant astrocytic tumors as a novel molecular marker of malignant progression. Acta Neuropathol (2006 ) 111(5):483–8.

    Not in our library10.1007/s00401-006-0063-y

  58. 58.

    Kato Y Fujita N Kunita A Sato S Kaneko M Osawa M Molecular identification of Aggrus/T1alpha as a platelet aggregation-inducing factor expressed in colorectal tumors. J Biol Chem (2003 ) 278(51):51599–605.

    Not in our library10.1074/jbc.m309935200

  59. 59.

    Rodrigo JP Garcia-Carracedo D Gonzalez MV Mancebo G Fresno MF Garcia-Pedrero J. Podoplanin expression in the development and progression of laryngeal squamous cell carcinomas. Mol Cancer (2010 ) 9:48.

    Not in our library10.1186/1476-4598-9-48

  60. 60.

    Kato Y Kaneko M Sata M Fujita N Tsuruo T Osawa M. Enhanced expression of Aggrus (T1alpha/podoplanin), a platelet-aggregation-inducing factor in lung squamous cell carcinoma. Tumour Biol (2005 ) 26(4):195–200.

    Not in our library10.1159/000086952

  61. 61.
    Podoplanin-Rich Stromal Networks Induce Dendritic Cell Motility via Activation of the C-type Lectin Receptor CLEC-2 · 2012
    No notice
  62. 62.

    Mourao-Sa D Robinson MJ Zelenay S Sancho D Chakravarty P Larsen R CLEC-2 signaling via Syk in myeloid cells can regulate inflammatory responses. Eur J Immunol (2011 ) 41(10):3040–53.

    Not in our library10.1002/eji.201141641

  63. 63.

    Marshall AS Willment JA Lin HH Williams DL Gordon S Brown GD. Identification and characterization of a novel human myeloid inhibitory C-type lectin-like receptor (MICL) that is predominantly expressed on granulocytes and monocytes. J Biol Chem (2004 ) 279(15):14792–802.

    Not in our library10.1074/jbc.m313127200

  64. 64.

    Marshall AS Willment JA Pyz E Dennehy KM Reid DM Dri P Human MICL (CLEC12A) is differentially glycosylated and is down-regulated following cellular activation. Eur J Immunol (2006 ) 36(8):2159–69.

    Not in our library10.1002/eji.200535628

  65. 65.

    Pyz E Huysamen C Marshall AS Gordon S Taylor PR Brown GD. Characterisation of murine MICL (CLEC12A) and evidence for an endogenous ligand. Eur J Immunol (2008 ) 38(4):1157–63.

    Not in our library10.1002/eji.200738057

  66. 66.

    Chen CH Floyd H Olson NE Magaletti D Li C Draves K Dendritic-cell-associated C-type lectin 2 (DCAL-2) alters dendritic-cell maturation and cytokine production. Blood (2006 ) 107(4):1459–67.

    Not in our library10.1182/blood-2005-08-3264

  67. 67.

    Redelinghuys P Whitehead L Augello A Drummond RA Levesque JM Vautier S MICL controls inflammation in rheumatoid arthritis. Ann Rheum Dis (2016 ) 75(7):1386–91.

    Not in our library10.1136/annrheumdis-2014-206644

  68. 68.

    Schreibelt G Klinkenberg LJ Cruz LJ Tacken PJ Tel J Kreutz M The C-type lectin receptor CLEC9A mediates antigen uptake and (cross-) presentation by human blood BDCA3+ myeloid dendritic cells. Blood (2012 ) 119(10):2284–92.

    Not in our library10.1182/blood-2011-08-373944

  69. 69.

    Ahrens S Zelenay S Sancho D Hanc P Kjaer S Feest C F-actin is an evolutionarily conserved damage-associated molecular pattern recognized by DNGR-1, a receptor for dead cells. Immunity (2012 ) 36(4):635–45.

    Not in our library10.1016/j.immuni.2012.03.008

  70. 70.

    Zhang JG Czabotar PE Policheni AN Caminschi I Wan SS Kitsoulis S The dendritic cell receptor Clec9A binds damaged cells via exposed actin filaments. Immunity (2012 ) 36(4):646–57.

    Not in our library10.1016/j.immuni.2012.03.009

  71. 71.

    Sancho D Mourao-Sa D Joffre OP Schulz O Rogers NC Pennington DJ Tumor therapy in mice via antigen targeting to a novel, DC-restricted C-type lectin. J Clin Invest (2008 ) 118(6):2098–110.

    Not in our library10.1172/jci34584

  72. 72.

    Yan Z Wu Y Du J Li G Wang S Cao W A novel peptide targeting Clec9a on dendritic cell for cancer immunotherapy. Oncotarget (2016 ) 7(26):40437–50.

    Not in our library10.18632/oncotarget.9624

  73. 73.

    Tullett KM Leal Rojas IM Minoda Y Tan PS Zhang JG Smith C Targeting CLEC9A delivers antigen to human CD141+ DC for CD4+ and CD8+T cell recognition. JCI Insight (2016 ) 1(7):e87102.

    Not in our library10.1172/jci.insight.87102

  74. 74.

    Haddad Y Lahoute C Clement M Laurans L Metghalchi S Zeboudj L The dendritic cell receptor DNGR-1 promotes the development of atherosclerosis in mice. Circ Res (2017 ) 121(3):234–43.

    Not in our library10.1161/circresaha.117.310960

  75. 75.

    Bates EE Fournier N Garcia E Valladeau J Durand I Pin JJ APCs express DCIR, a novel C-type lectin surface receptor containing an immunoreceptor tyrosine-based inhibitory motif. J Immunol (1999 ) 163(4):1973–83.

    Not in our library

  76. 76.

    Flornes LM Bryceson YT Spurkland A Lorentzen JC Dissen E Fossum S. Identification of lectin-like receptors expressed by antigen presenting cells and neutrophils and their mapping to a novel gene complex. Immunogenetics (2004 ) 56(7):506–17.

    Not in our library10.1007/s00251-004-0714-x

  77. 77.

    Lambert AA Barabe F Gilbert C Tremblay MJ. DCIR-mediated enhancement of HIV-1 infection requires the ITIM-associated signal transduction pathway. Blood (2011 ) 117(24):6589–99.

    Not in our library10.1182/blood-2011-01-331363

  78. 78.

    Massoud AH Yona M Xue D Chouiali F Alturaihi H Ablona A Dendritic cell immunoreceptor: a novel receptor for intravenous immunoglobulin mediates induction of regulatory T cells. J Allergy Clin Immunol (2014 ) 133(3):853–63.e5.

    Not in our library10.1016/j.jaci.2013.09.029

  79. 79.

    Meyer-Wentrup F Cambi A Joosten B Looman MW de Vries IJ Figdor CG DCIR is endocytosed into human dendritic cells and inhibits TLR8-mediated cytokine production. J Leukoc Biol (2009 ) 85(3):518–25.

    Not in our library10.1189/jlb.0608352

  80. 80.

    Fujikado N Saijo S Yonezawa T Shimamori K Ishii A Sugai S DCIR deficiency causes development of autoimmune diseases in mice due to excess expansion of dendritic cells. Nat Med (2008 ) 14(2):176–80.

    Not in our library10.1038/nm1697

  81. 81.

    Seno A Maruhashi T Kaifu T Yabe R Fujikado N Ma G Exacerbation of experimental autoimmune encephalomyelitis in mice deficient for DCIR, an inhibitory C-type lectin receptor. Exp Anim (2015 ) 64(2):109–19.

    Not in our library10.1538/expanim.14-0079

  82. 82.
    Clec4A4 is a regulatory receptor for dendritic cells that impairs inflammation and T-cell immunity · 2016
    Not checked
  83. 83.

    Troegeler A Mercier I Cougoule C Pietretti D Colom A Duval C C-type lectin receptor DCIR modulates immunity to tuberculosis by sustaining type I interferon signaling in dendritic cells. Proc Natl Acad Sci U S A (2017 ) 114(4):E540–9.

    Not in our library10.1073/pnas.1613254114

  84. 84.

    Hütter J Eriksson M Johannssen T Klopfleisch R von Smolinski D Gruber AD Role of the C-type lectin receptors MCL and DCIR in experimental colitis. PLoS One (2014 ) 9(7):e103281.

    Not in our library10.1371/journal.pone.0103281

  85. 85.

    Taylor PR Reid DM Heinsbroek SEM Brown GD Gordon S Wong SYC. Dectin-2 is predominantly myeloid restricted and exhibits unique activation-dependent expression on maturing inflammatory monocytes elicited in vivo. Eur J Immunol (2005 ) 35(7):2163–74.

    Not in our library10.1002/eji.200425785

  86. 86.

    Aragane Y Maeda A Schwarz A Tezuka T Ariizumi K Schwarz T. Involvement of dectin-2 in ultraviolet radiation-induced tolerance. J Immunol (2003 ) 171(7):3801–7.

    Not in our library10.4049/jimmunol.171.7.3801

  87. 87.

    Depke M Breitbach K Dinh Hoang Dang K Brinkmann L Salazar MG Dhople VM Bone marrow-derived macrophages from BALB/c and C57BL/6 mice fundamentally differ in their respiratory chain complex proteins, lysosomal enzymes and components of antioxidant stress systems. J Proteomics (2014 ) 103:72–86.

    Not in our library10.1016/j.jprot.2014.03.027

  88. 88.

    Mori D Shibata K Yamasaki S C-type lectin receptor dectin-2 binds to an endogenous protein beta-glucuronidase on dendritic cells. PLoS One (2017 ) 12(1):e0169562

    Not in our library10.1371/journal.pone.0169562

  89. 89.

    McGreal EP Rosas M Brown GD Zamze S Wong SY Gordon S The carbohydrate-recognition domain of dectin-2 is a C-type lectin with specificity for high mannose. Glycobiology (2006 ) 16(5):422–30.

    Not in our library10.1093/glycob/cwj077

  90. 90.

    Robinson MJ Osorio F Rosas M Freitas RP Schweighoffer E Gross O Dectin-2 is a Syk-coupled pattern recognition receptor crucial for Th17 responses to fungal infection. J Exp Med (2009 ) 206(9):2037–51.

    Not in our library10.1084/jem.20082818

  91. 91.

    Bramwell KK Ma Y Weis JH Chen X Zachary JF Teuscher C Lysosomal beta-glucuronidase regulates Lyme and rheumatoid arthritis severity. J Clin Invest (2014 ) 124(1):311–20.

    Not in our library10.1172/jci72339

  92. 92.

    Tomatsu S Montano AM Dung VC Grubb JH Sly WS. Mutations and polymorphisms in GUSB gene in mucopolysaccharidosis VII (sly syndrome). Hum Mutat (2009 ) 30(4):511–9.

    Not in our library10.1002/humu.20828

  93. 93.

    Kimura Y Inoue A Hangai S Saijo S Negishi H Nishio J The innate immune receptor dectin-2 mediates the phagocytosis of cancer cells by Kupffer cells for the suppression of liver metastasis. Proc Natl Acad Sci U S A (2016 ) 113(49):14097–102.

    Not in our library10.1073/pnas.1617903113

  94. 94.

    Dzionek A Sohma Y Nagafune J Cella M Colonna M Facchetti F BDCA-2, a novel plasmacytoid dendritic cell-specific type II C-type lectin, mediates antigen capture and is a potent inhibitor of interferon alpha/beta induction. J Exp Med (2001 ) 194(12):1823–34.

    Not in our library10.1084/jem.194.12.1823

  95. 95.

    Dzionek A Fuchs A Schmidt P Cremer S Zysk M Miltenyi S BDCA-2, BDCA-3, and BDCA-4: three markers for distinct subsets of dendritic cells in human peripheral blood. J Immunol (2000 ) 165(11):6037–46.

    Not in our library10.4049/jimmunol.165.11.6037

  96. 96.

    Rock J Schneider E Grun JR Grutzkau A Kuppers R Schmitz J CD303 (BDCA-2) signals in plasmacytoid dendritic cells via a BCR-like signalosome involving Syk, Slp65 and PLCgamma2. Eur J Immunol (2007 ) 37(12):3564–75.

    Not in our library10.1002/eji.200737711

  97. 97.

    Riboldi E Daniele R Parola C Inforzato A Arnold PL Bosisio D Human C-type lectin domain family 4, member C (CLEC4C/BDCA-2/CD303) is a receptor for asialo-galactosyl-oligosaccharides. J Biol Chem (2011 ) 286(41):35329–33.

    Not in our library10.1074/jbc.c111.290494

  98. 98.

    Riboldi E Daniele R Cassatella MA Sozzani S Bosisio D. Engagement of BDCA-2 blocks TRAIL-mediated cytotoxic activity of plasmacytoid dendritic cells. Immunobiology (2009 ) 214(9–10):868–76.

    Not in our library10.1016/j.imbio.2009.06.016

  99. 99.

    Jegouzo SA Feinberg H Dungarwalla T Drickamer K Weis WI Taylor ME. A novel mechanism for binding of galactose-terminated glycans by the C-type carbohydrate recognition domain in blood dendritic cell antigen 2. J Biol Chem (2015 ) 290(27):16759–71.

    Not in our library10.1074/jbc.m115.660613

  100. 100.

    Matsumoto M Tanaka T Kaisho T Sanjo H Copeland NG Gilbert DJ A novel LPS-inducible C-type lectin is a transcriptional target of NF-IL6 in macrophages. J Immunol (1999 ) 163(9):5039–48.

    Not in our library

  101. 101.

    Lobato-Pascual A Saether PC Fossum S Dissen E Daws MR Mincle, the receptor for mycobacterial cord factor, forms a functional receptor complex with MCL and FcepsilonRI-gamma. Eur J Immunol (2013 ) 43(12):3167–74.

    Not in our library10.1002/eji.201343752

  102. 102.

    Ostrop J Jozefowski K Zimmermann S Hofmann K Strasser E Lepenies B Contribution of MINCLE-SYK signaling to activation of primary human APCs by mycobacterial cord factor and the novel adjuvant TDB. J Immunol (2015 ) 195(5):2417–28.

    Not in our library10.4049/jimmunol.1500102

  103. 103.
    Stat6-dependent inhibition of Mincle expression in mouse and human antigen-presenting cells by the Th2 cytokine IL-4 · 2016
    Not checked
  104. 104.

    Miyake Y Masatsugu OH Yamasaki S. C-type lectin receptor MCL facilitates MINCLE expression and signaling through complex formation. J Immunol (2015 ) 194(11):5366–74.

    Not in our library10.4049/jimmunol.1402429

  105. 105.

    van Haren SD Dowling DJ Foppen W Christensen D Andersen P Reed SG Age-specific adjuvant synergy: dual TLR7/8 and MINCLE activation of human newborn dendritic cells enables Th1 polarization. J Immunol (2016 ) 197(11):4413–24.

    Not in our library10.4049/jimmunol.1600282

  106. 106.

    Shenderov K Barber DL Mayer-Barber KD Gurcha SS Jankovic D Feng CG Cord factor and peptidoglycan recapitulate the Th17-promoting adjuvant activity of mycobacteria through mincle/CARD9 signaling and the inflammasome. J Immunol (2013 ) 190(11):5722–30.

    Not in our library10.4049/jimmunol.1203343

  107. 107.

    Kiyotake R Oh-Hora M Ishikawa E Miyamoto T Ishibashi T Yamasaki S. Human MINCLE binds to cholesterol crystals and triggers innate immune responses. J Biol Chem (2015 ) 290(42):25322–32.

    Not in our library10.1074/jbc.m115.645234

  108. 108.

    Kostarnoy AV Gancheva PG Lepenies B Tukhvatulin AI Dzharullaeva AS Polyakov NB Receptor MINCLE promotes skin allergies and is capable of recognizing cholesterol sulfate. Proc Natl Acad Sci U S A (2017 ) 114(13):E2758–65.

    Not in our library10.1073/pnas.1611665114

  109. 109.

    Nagata M Izumi Y Ishikawa E Kiyotake R Doi R Iwai S Intracellular metabolite beta-glucosylceramide is an endogenous MINCLE ligand possessing immunostimulatory activity. Proc Natl Acad Sci U S A (2017 ) 114(16):E3285–94.

    Not in our library10.1073/pnas.1618133114

  110. 110.

    Patin EC Willcocks S Orr S Ward TH Lang R Schaible UE. Mincle-mediated anti-inflammatory IL-10 response counter-regulates IL-12 in vitro. Innate Immun (2016 ) 22(3):181–5.

    Not in our library10.1177/1753425916636671

  111. 111.

    Wevers BA Kaptein TM Zijlstra-Willems EM Theelen B Boekhout T Geijtenbeek TB Fungal engagement of the C-type lectin MINCLE suppresses dectin-1-induced antifungal immunity. Cell Host Microbe (2014 ) 15(4):494–505.

    Not in our library10.1016/j.chom.2014.03.008

  112. 112.

    Yamasaki S Ishikawa E Sakuma M Hara H Ogata K Saito T. MINCLE is an ITAM-coupled activating receptor that senses damaged cells. Nat Immunol (2008 ) 9(10):1179–88.

    Not in our library10.1038/ni.1651

  113. 113.

    Suzuki Y Nakano Y Mishiro K Takagi T Tsuruma K Nakamura M Involvement of MINCLE and Syk in the changes to innate immunity after ischemic stroke. Sci Rep (2013 ) 3:3177.

    Not in our library10.1038/srep03177

  114. 114.

    Arumugam TV Manzanero S Furtado M Biggins PJ Hsieh YH Gelderblom M An atypical role for the myeloid receptor MINCLE in central nervous system injury. J Cereb Blood Flow Metab (2017 ) 37(6):2098–111.

    Not in our library10.1177/0271678x16661201

  115. 115.

    Lee EJ Brown BR Vance EE Snow PE Silver PB Heinrichs D MINCLE activation and the Syk/Card9 signaling axis are central to the development of autoimmune disease of the eye. J Immunol (2016 ) 196(7):3148–58.

    Not in our library10.4049/jimmunol.1502355

  116. 116.

    Nakamura N Shimaoka Y Tougan T Onda H Okuzaki D Zhao H Isolation and expression profiling of genes upregulated in bone marrow-derived mononuclear cells of rheumatoid arthritis patients. DNA Res (2006 ) 13(4):169–83.

    Not in our library10.1093/dnares/dsl006

  117. 117.

    Ribbhammar U Flornes L Backdahl L Luthman H Fossum S Lorentzen JC. High resolution mapping of an arthritis susceptibility locus on rat chromosome 4, and characterization of regulated phenotypes. Hum Mol Genet (2003 ) 12(17):2087–96.

    Not in our library10.1093/hmg/ddg224

  118. 118.

    Seifert L Werba G Tiwari S Giao Ly NN Alothman S Alqunaibit D The necrosome promotes pancreatic oncogenesis via CXCL1 and mincle-induced immune suppression. Nature (2016 ) 532(7598):245–9.

    Not in our library10.1038/nature17403

  119. 119.

    Yan H Kamiya T Suabjakyong P Tsuji NM. Targeting C-type lectin receptors for cancer immunity. Front Immunol (2015 ) 6:408.

    Not in our library10.3389/fimmu.2015.00408

  120. 120.

    Bonifaz L Bonnyay D Mahnke K Rivera M Nussenzweig MC Steinman RM. Efficient targeting of protein antigen to the dendritic cell receptor DEC-205 in the steady state leads to antigen presentation on major histocompatibility complex class I products and peripheral CD8+ T cell tolerance. J Exp Med (2002 ) 196(12):1627–38.

    Not in our library10.1084/jem.20021598

  121. 121.

    Bonifaz LC Bonnyay DP Charalambous A Darguste DI Fujii S Soares H In vivo targeting of antigens to maturing dendritic cells via the DEC-205 receptor improves T cell vaccination. J Exp Med (2004 ) 199(6):815–24.

    Not in our library10.1084/jem.20032220

  122. 122.

    Temizoz B Kuroda E Ishii KJ. Vaccine adjuvants as potential cancer immunotherapeutics. Int Immunol (2016 ) 28(7):329–38.

    Not in our library10.1093/intimm/dxw015

  123. 123.
    Platelets Promote Tumor Growth and Metastasis via Direct Interaction between Aggrus/Podoplanin and CLEC-2 · 2013
    No notice
  124. 124.

    Kaneko MK Nakamura T Honma R Ogasawara S Fujii Y Abe S Development and characterization of anti-glycopeptide monoclonal antibodies against human podoplanin, using glycan-deficient cell lines generated by CRISPR/Cas9 and TALEN. Cancer Med (2017 ) 6(2):382–96.

    Not in our library10.1002/cam4.954

  125. 125.

    Kaneko MK Yamada S Nakamura T Abe S Nishioka Y Kunita A Antitumor activity of chLpMab-2, a human-mouse chimeric cancer-specific antihuman podoplanin antibody, via antibody-dependent cellular cytotoxicity. Cancer Med (2017 ) 6(4):768–77.

    Not in our library10.1002/cam4.1049

  126. 126.
    A Cancer-specific Monoclonal Antibody Recognizes the Aberrantly Glycosylated Podoplanin · 2014
    No notice
  127. 127.

    Chang Y-W Hsieh P-W Chang Y-T Lu M-H Huang T-F Chong K-Y Identification of a novel platelet antagonist that binds to CLEC-2 and suppresses podoplanin-induced platelet aggregation and cancer metastasis. Oncotarget (2015 ) 6(40):42733–48.

    Not in our library10.18632/oncotarget.5811

  128. 128.

    Shirai T Inoue O Tamura S Tsukiji N Sasaki T Endo H C-type lectin-like receptor 2 promotes hematogenous tumor metastasis and prothrombotic state in tumor-bearing mice. J Thromb Haemost (2017 ) 15(3):513–25.

    Not in our library10.1111/jth.13604

  129. 129.

    Lang R Schoenen H Desel C. Targeting Syk-Card9-activating C-type lectin receptors by vaccine adjuvants: findings, implications and open questions. Immunobiology (2011 ) 216(11):1184–91.

    Not in our library10.1016/j.imbio.2011.06.005

  130. 130.

    Chang J Patton JT Sarkar A Ernst B Magnani JL Frenette PS. GMI-1070, a novel pan-selectin antagonist, reverses acute vascular occlusions in sickle cell mice. Blood (2010 ) 116(10):1779–86.

    Not in our library10.1182/blood-2009-12-260513

  131. 131.

    Aretz J Wamhoff EC Hanske J Heymann D Rademacher C. Computational and experimental prediction of human C-type lectin receptor druggability. Front Immunol (2014 ) 5:323.

    Not in our library10.3389/fimmu.2014.00323

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