Affinity Binding of EMR2 Expressing Cells by Surface-Grafted Chondroitin Sulfate B

Burzava, Anouck; Jasieniak, Marek; Cockshell, Michaelia P.; Bonder, Claudine S.; Harding, Frances J.; Griesser, Hans J.; Voelcker, Nicolas H.

doi:10.1021/acs.biomac.6b01687

Cited by 5 publications

(3 citation statements)

References 48 publications

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“…Analysis of the function of this gene family has been constrained by the lack of knowledge of likely ligands. The only evidence comes from ADGRE2 which was reported to bind selectively to the proteoglycan chondroitin sulfate ( 75 ). Interaction with various glycosaminoglycans (GAG) at portals of entry is a very common feature of microbial pathogenesis ( 76 ).…”

Section: Discussionmentioning

confidence: 99%

ADGRE1 (EMR1, F4/80) Is a Rapidly-Evolving Gene Expressed in Mammalian Monocyte-Macrophages

et al. 2018

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The F4/80 antigen, encoded by the Adgre1 locus, has been widely-used as a monocyte-macrophage marker in mice, but its value as a macrophage marker in other species is unclear, and has even been questioned. ADGRE1 is a seven transmembrane G protein-coupled receptor with an extracellular domain containing repeated Epidermal Growth Factor (EGF)-like calcium binding domains. Using a new monoclonal antibody, we demonstrated that ADGRE1 is a myeloid differentiation marker in pigs, absent from progenitors in bone marrow, highly-expressed in mature granulocytes, monocytes, and tissue macrophages and induced by macrophage colony-stimulating factor (CSF1) treatment in vivo. Based upon these observations, we utilized RNA-Seq to assess the expression of ADGRE1 mRNA in bone marrow or monocyte-derived macrophages (MDM) and alveolar macrophages from 8 mammalian species including pig, human, rat, sheep, goat, cow, water buffalo, and horse. ADGRE1 mRNA was expressed by macrophages in each species, with inter-species variation both in expression level and response to lipopolysaccharide (LPS) stimulation. Analysis of the RNA-Seq data also revealed additional exons in several species compared to current Ensembl annotations. The ruminant species and horses appear to encode a complete duplication of the 7 EGF-like domains. In every species, Sashimi plots revealed evidence of exon skipping of the EGF-like domains, which are highly-variable between species and polymorphic in humans. Consistent with these expression patterns, key elements of the promoter and a putative enhancer are also conserved across all species. The rapid evolution of this molecule and related ADGRE family members suggests immune selection and a role in pathogen recognition.

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Section: Discussionmentioning

confidence: 99%

ADGRE1 (EMR1, F4/80) Is a Rapidly-Evolving Gene Expressed in Mammalian Monocyte-Macrophages

et al. 2018

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“…EMR2 binds dermatan sulfate with its 4th EGF-like domain, existing only in the longest isoforms of EMR2(EGF1-4) and of its homologue CD97(EGF1-5) [11,48]. Indeed, the affinity binding of EMR2-and CD97-expressing myeloid U937 cells can be achieved in surface-bound dermatan sulfate but not in grafted heparan sulfate (CS-A) in vitro [49].…”

Section: Discussionmentioning

confidence: 99%

The Posttraumatic Increase of the Adhesion GPCR EMR2/ADGRE2 on Circulating Neutrophils Is Not Related to Injury Severity

Zheng,

Rang,

Fuchs

et al. 2023

Cells

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Trauma triggers a rapid innate immune response to aid the clearance of damaged/necrotic cells and their released damage-associated molecular pattern (DAMP). Here, we monitored the expression of EMR2/ADGRE2, involved in the functional regulation of innate immune cells, on circulating neutrophils in very severely and moderately/severely injured patients up to 240 h after trauma. Notably, neutrophilic EMR2 showed a uniform, injury severity- and type of injury-independent posttraumatic course in all patients. The percentage of EMR2+ neutrophils and their EMR2 level increased and peaked 48 h after trauma. Afterwards, they declined and normalized in some, but not all, patients. Circulating EMR2+ compared to EMR2− neutrophils express less CD62L and more CD11c, a sign of activation. Neutrophilic EMR2 regulation was verified in vitro. Remarkably, it increased, depending on extracellular calcium, in controls as well. Cytokines, enhanced in patients immediately after trauma, and sera of patients did not further affect this neutrophilic EMR2 increase, whereas apoptosis induction disrupted it. Likely the damaged/necrotic cells/DAMPs, unavoidable during neutrophil culture, stimulate the neutrophilic EMR2 increase. In summary, the rapidly increased absolute number of neutrophils, especially present in very severely injured patients, together with upregulated neutrophilic EMR2, may expand our in vivo capacity to react to and finally clear damaged/necrotic cells/DAMPs after trauma.

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“…ToF-SIMS has been applied to assess the modification of sugars at surfaces but has typically been limited to mono- or di-saccharides 23 – 28 . Studies of larger polysaccharides, typically heparin or HA, focussed on low mass fragments that have limited utility to discriminate between the different GAG types 29 – 35 .…”

Section: Introductionmentioning

confidence: 99%

High sensitivity analysis of nanogram quantities of glycosaminoglycans using ToF-SIMS

et al. 2021

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Glycosaminoglycans (GAGs) are important biopolymers that differ in the sequence of saccharide units and in post polymerisation alterations at various positions, making these complex molecules challenging to analyse. Here we describe an approach that enables small quantities (<200 ng) of over 400 different GAGs to be analysed within a short time frame (3–4 h). Time of flight secondary ion mass spectrometry (ToF-SIMS) together with multivariate analysis is used to analyse the entire set of GAG samples. Resultant spectra are derived from the whole molecules and do not require pre-digestion. All 6 possible GAG types are successfully discriminated, both alone and in the presence of fibronectin. We also distinguish between pharmaceutical grade heparin, derived from different animal species and from different suppliers, to a sensitivity as low as 0.001 wt%. This approach is likely to be highly beneficial in the quality control of GAGs produced for therapeutic applications and for characterising GAGs within biomaterials or from in vitro cell culture.

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Affinity Binding of EMR2 Expressing Cells by Surface-Grafted Chondroitin Sulfate B

Cited by 5 publications

References 48 publications

ADGRE1 (EMR1, F4/80) Is a Rapidly-Evolving Gene Expressed in Mammalian Monocyte-Macrophages

ADGRE1 (EMR1, F4/80) Is a Rapidly-Evolving Gene Expressed in Mammalian Monocyte-Macrophages

The Posttraumatic Increase of the Adhesion GPCR EMR2/ADGRE2 on Circulating Neutrophils Is Not Related to Injury Severity

High sensitivity analysis of nanogram quantities of glycosaminoglycans using ToF-SIMS

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