mProX™ Human ACKR1 Stable Cell Line
- Product Category:
- Membrane Protein Stable Cell Lines
- Subcategory:
- GPCR Cell Lines
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Published Data
Fig.1 Saturation BRET confirms CR heteromerization partners of α1a/b/d-ARs.
HEK293T cells underwent transfection involving a consistent α1a/b/d-RLuc quantity, alongside escalating quantities of CR-YFP or YFP. The data depicts saturation BRET signals, a representative set from n = 3 autonomous experiments for each receptor-receptor pairing. YFP fluorescence and luminescence measurement followed the stipulated methodology. The net BRET (528/460 nm) was graphed against YFP/Lum, illustrating the saturation BRET relationship between α-AR and ACKR1.
Ref: Enten, Garrett A., et al. "α1B/D-adrenoceptors regulate chemokine receptor-mediated leukocyte migration via formation of heteromeric receptor complexes." Proceedings of the National Academy of Sciences 119.20 (2022): e2123511119.
Pubmed: 35537053
DOI: 10.1073/pnas.2123511119
Research Highlights
Xiang N, et al. "Single-cell transcriptome profiling reveals immune and stromal cell heterogeneity ." iScience, 2023.
Primary Sjogren's syndrome (pSS) is a complex autoimmune disease characterized by lymphocytic infiltration and exocrine dysfunction, primarily affecting the salivary gland (SG). Researchers employed single-cell RNA sequencing to investigate cellular heterogeneity in 11 pSS patients and 5 non-SS controls. The study identified decreased SOX9 expression in myoepithelial cells in pSS patients, potentially linked to impaired epithelial regeneration. Furthermore, an expanded subset of ACKR1(+) endothelial cells was observed in pSS patients, indicating a possible role in facilitating lymphocyte transendothelial migration. The analysis also revealed an increase in IGHD(+) naive B cells in peripheral blood of pSS patients. Pseudotime trajectory analysis identified a separate differentiation pathway for peripheral B cells, leading to three subtypes (VPREB3(+) B, BANK1(+) B, and CD83(+) B cells) which were enriched in SGs of pSS patients. Fibroblasts were shown to play a crucial role in the stromal-immune interaction network, potentially contributing to extracellular matrix disruption, impairment of epithelial regeneration, and inflammation. This study sheds light on immune and stromal cell heterogeneity in pSS patients and provides potential insights for therapeutic strategies.
Pubmed:
37810210
DOI:
10.1016/j.isci.2023.107943
Kranjc A, et al. "Structural Space of the Duffy Antigen/Receptor for Chemokines' Intrinsically ." International journal of molecular sciences, 2023.
Plasmodium vivax malaria affects approximately 14 million individuals annually. The invasion of this disease is reliant upon the interaction between the parasitic Duffy-binding protein (PvDBP) and the N-terminal extracellular domain (ECD1) of the host's Duffy antigen/receptor for chemokines (DARC). ECD1, known for its high flexibility and intrinsic disorder, has the ability to adopt various conformations. A team of researchers conducted computational modeling for the complex ECD1 local structure. Using T-REMD simulations, they were able to obtain its dynamic behavior and acquire a representative collection of ECD1 conformations. The team's findings suggest that a majority of the DARC ECD1 domain remains in a disordered state throughout the simulated time. However, globular local conformations were discovered in the analyzed free energy minima. These conformations contain an alpha-helix spanning from Ser18 to Ser29 and often include an antiparallel beta-sheet, with beta-strands formed around Leu10 and Ala49. The formation of a parallel beta-sheet was found to be minimal. Due to experimental challenges and a lack of DARC structural information, progress towards understanding the mechanisms involved in P. vivax malaria infection of reticulocytes has been limited. However, the researchers' collection of the most probable ECD1 structural conformations will aid in further modeling of the DARC structure and exploration of DARC-ECD1 interactions with various physiological and pathological ligands.
Pubmed:
37686086
DOI:
10.3390/ijms241713280