Introduction of ADGRE2
ADGRE2, also known as EGF-like module receptor 2 (EMR2) or EGF-like module-containing mucin-like hormone receptor-like 2, is a protein encoded by the human ADGRE2 gene. As a member of the adhesion GPCR family, it is characterized by an extended extracellular region often possessing N-terminal protein modules that are linked to a TM7 region via a domain known as the GPCR-Autoproteolysis Inducing (GAIN) domain.
|Basic Information of ADGRE2|
|Protein Name||Adhesion G protein-coupled receptor E2|
EGF-like module receptor 2, EGF-like module-containing mucin-like hormone
receptor-like 2, CD antigen CD312
|Organism||Homo sapiens (Human)|
Function of ADGRE2 Membrane Protein
During the past years, ADGRE2 has been widely studied. It has been reported that ADGRE2 is closely related to CD97 with 97% amino-acid identity in the EGF-like domains. As a member of the adhesion GPCR family, ADGRE2 is expressed by monocytes/macrophages, dendritic cells and all types of granulocytes. And it is rarely expressed by tumor cell lines and tumors, but has been found on breast and colorectal adenocarcinoma. Recently, the role of ADGRE2 in the migration and adhesion of myeloid cell during cell differentiation, maturation, and activation has been widely studied. It has suggested that the ligation of EMR2 could increase neutrophil adhesion, migration and anti-microbial mediator production and could enhance the systemic inflammation. What’s more, other studies had shown that EMR2 expression on the neutrophil increased in patients with SIRS and correlated with the extent of organ failure.
Fig.1 ADGRE2 protein domains.
Application of ADGRE2 Membrane Protein in Literature
1. Huang YS, et.al. Membrane-association of EMR2/ADGRE2-NTF is regulated by site-specific N-glycosylation. Scientific reports. 2018, 8(1): 4532. PubMed ID: 29540735
This article provides a novel insight into the complex interaction and activation mechanisms of aGPCRs.
2. Huang YS, et.al. Activation of Adhesion GPCR EMR2/ADGRE2 Induces Macrophage Differentiation and Inflammatory Responses via Gα16/Akt/MAPK/NF-κB Signaling Pathways. Frontiers in immunology. 2017, 8: 373. PubMed ID: 28421075
This article reveals that ADGRE2 has a new role in the differentiation and inflammatory activation of human monocytic cells and provide potential targets for myeloid cell-mediated inflammatory disorders.
3. Boyden SE, et.al. Vibratory urticaria associated with a missense variant in ADGRE2. New England Journal of Medicine. 2016, 374(7): 656-63. PubMed ID: 26841242
This article suggests that the variant probably destabilizes an autoinhibitory subunit interaction, sensitizing mast cells to IgE-independent vibration-induced degranulation.
4. Feliciano A, et.al. miR-99a reveals two novel oncogenic proteins E2F2 and EMR2 and represses stemness in lung cancer. Cell death & disease. 2017, 8(10): e3141. PubMed ID: 29072692
This article reveals that EMR2 plays a key role in lung tumorigenesis. By inhibiting E2F2 and EMR2, miR-99a represses in vivo the transition of epithelial cells through an EMT process concomitantly with the inhibition of stemness features and consequently decreasing the CSC population.
5. Burzava AL, et.al. Affinity binding of EMR2 expressing cells by surface-grafted chondroitin sulfate B. Biomacromolecules. 2017, 18(6): 1697-704. PubMed ID: 28437084
This article suggests that the EMR2 expressing human myeloid cell line U937 preferentially bound onto CS-B-modified substrates, and U937 cells preincubated with CS-B in solution exhibited reduced affinity for the substrate.
ADGRE2 Preparation Options
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