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Last update 08 May 2025

CLEC2A

Last update 08 May 2025

Basic Info

Synonyms

C-type lectin domain family 2 member A, CLEC2A, INPE5792

+ [5]

Introduction

Membrane-bound protein expressed mainly on keratinocytes which acts as a ligand to stimulate the activating receptor NKp65/KLRF2, expressed on the surface of natural killer (NK) cells (PubMed:25510854). Facilitates thereby dedicated immune recognition of keratinocytes leading to natural killer cell mediated cytotoxicity (PubMed:20194751). Plays also a role in modulating the extent of T-cell expansion (PubMed:18550855).

Drugs associated with CLEC2A

CLEC2A-Target CAR T(Fred Hutchinson Cancer Center)

Target

CLEC2A

Mechanism

CLEC2A inhibitors

Active Org.

Fred Hutchinson Cancer Research Center [+1]

Originator Org.

Fred Hutchinson Cancer Research Center [+1]

Active Indication

Acute Myeloid Leukemia

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with CLEC2A

100 Translational Medicine associated with CLEC2A

0 Patents (Medical) associated with CLEC2A

Literatures (Medical) associated with CLEC2A

01 Sep 2024·Molecular Therapy: Oncology

Oncolytic vaccinia virus harboring CLEC2A gene enhances viral replication and antitumor efficacy

Article

Author: Qiu, Yufeng ; Ying, Qi ; Chen, Kan ; Ye, Ting ; Zhou, Yanrong ; Gao, Chunqing ; Ren, Ningbo ; Li, Gongchu

In the field of innovative cancer treatment strategies, oncolytic vaccinia virus (VV)es have gained traction as promising vectors. In the current study, we inserted the human C-type lectin domain family 2 member A (CLEC2A) gene into VV, creating a replicating therapeutic, oncoVV-CLEC2A. The findings reveal that oncoVV-CLEC2A effectively suppresses colorectal proliferation of mouse xenografts and a range of human cancer cell lines by augmenting viral reproduction capabilities, including the lung cancer H460 cell line, colorectal cancer cell lines (HCT116 and SW620), and hepatocellular carcinoma HuH-7 cell line. Moreover, it is evident that oncoVV-CLEC2A can induce antitumor immunity by boosting cytokine production but not antivirus response, and enhancing calreticulin expression. Further investigation indicates that oncoVV-CLEC2A can enhance antitumor capabilities by activating natural killer cells to produce interferon-γ and induce M1-like macrophage polarization. These findings shed light on the antitumor mechanisms of oncoVV-CLEC2A, provide a theoretical basis for oncolytic therapies, and lay the groundwork for novel strategies for modifying VVs.

01 Apr 2024·Journal of Molecular Biology

Control of Munc13-1 Activity by Autoinhibitory Interactions Involving the Variable N-terminal Region

Article

Author: Bolembach, Agnieszka A ; Esser, Victoria ; Xu, Junjie ; Rizo, Josep ; Gołębiowska-Mendroch, Katarzyna

Regulation of neurotransmitter release during presynaptic plasticity underlies varied forms of information processing in the brain. Munc13s play essential roles in release via their conserved C-terminal region, which contains a MUN domain involved in SNARE complex assembly, and controls multiple presynaptic plasticity processes. Munc13s also have a variable N-terminal region, which in Munc13-1 includes a calmodulin binding (CaMb) domain involved in short-term plasticity and a C₂A domain that forms an inhibitory homodimer. The C₂A domain is activated by forming a heterodimer with the zinc-finger domain of αRIMs, providing a link to αRIM-dependent short- and long-term plasticity. However, it is unknown how the functions of the N- and C-terminal regions are integrated, in part because of the difficulty of purifying Munc13-1 fragments containing both regions. We describe for the first time the purification of a Munc13-1 fragment spanning its entire sequence except for a flexible region between the C₂A and CaMb domains. We show that this fragment is much less active than the Munc13-1 C-terminal region in liposome fusion assays and that its activity is strongly enhanced by the RIM2α zinc-finger domain together with calmodulin. NMR experiments show that the C₂A and CaMb domains bind to the MUN domain and that these interactions are relieved by the RIM2α ZF domain and calmodulin, respectively. These results suggest a model whereby Munc13-1 activity in promoting SNARE complex assembly and neurotransmitter release are inhibited by interactions of the C₂A and CaMb domains with the MUN domain that are relieved by αRIMs and calmodulin.

01 May 2022·Clinical Drug Investigation

Effect of Genetic Polymorphism Including NUP153 and SVEP1 on the Pharmacokinetics and Pharmacodynamics of Ticagrelor in Healthy Chinese Subjects

Article

Author: Mu, Guangyan ; Li, Jian ; Liu, Zhiyan ; Jiang, Jie ; Xie, Qiufen ; Zhou, Shuang ; Cui, Yimin ; Yang, Guoping ; Huang, Jie ; Guo, Ninghong ; Wang, Zining ; Zhang, Hanxu ; Xiang, Qian

BACKGROUND AND OBJECTIVEThe search for potential gene loci that affect the pharmacodynamics and pharmacokinetics of ticagrelor is a matter of broad clinical interest. The objective of this study was to investigate the effect of genetic polymorphisms on the pharmacokinetics and pharmacodynamics of ticagrelor in healthy Chinese subjects.METHODSThis is a multi-center study in China, including three hospitals from Beijing, Nanchang, and Changsha. Healthy Chinese subjects aged 18-45 years with unknown genotypes were included. All subjects received a single oral dose of 90 mg of ticagrelor. Platelet aggregation and the area under the concentration-time curve for ticagrelor and its major active metabolite in plasma samples were assessed. Genome-wide association studies and candidate gene association analysis related to ticagrelor were performed.RESULTSOne hundred and seventy-five native Chinese subjects were enrolled and completed the study. According to the p value, the threshold of ticagrelor population was 6.57 × 10^-7 (0.05/76106), one single-nucleotide polymorphism chr6:17616513 of gene NUP153 (p = 2.03 × 10^-7) related to the area under the concentration-time curve for plasma concentration at time zero versus the last measurable timepoint, and one single nucleotide polymorphism rs17204533 of gene SVEP1 (p = 3.96 × 10^-7) related to P2Y12 reaction unit_12h of ticagrelor was identified. In addition, L1TD1, CETP, CLEC2A, CHSY1, PDZRN3, CTU2, PIEZO1, APOBEC1, SEMA6A, KAZN, and FASN polymorphisms might influence the pharmacokinetics of ticagrelor, while PARP10, TRIB1, CYP2C19, and UGT2B7 might affected its pharmacodynamics.CONCLUSIONSGenetic variation affects the pharmacokinetics and pharmacodynamics of ticagrelor in healthy individuals. The detection of NUP153, SVEP1 gene variation will be helpful for pharmacodynamic prediction and evaluation, and the regulation of these genes may be the target of new drug development. Further studies are required to confirm the results and explore whether these single-nucleotide polymorphisms are associated only with platelet activity or also with cardiovascular events and all-cause mortality.CLINICAL TRIAL REGISTRATIONNCT03161002.

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CLEC2A

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