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262 results for “Chemokines”
Dataset to the publication "A unique signal sequence of the chemokine receptor CCR7 promotes package into COPII vesicles for efficient receptor trafficking"
<p>This repository accompanies the paper:</p> <p>"A unique signal sequence of the chemokine receptor CCR7 promotes package into COPII vesicles for efficient receptor trafficking".</p> <p>Organized into 14 folders it provides the data allowing the replication of all analyses and the manuscript's figures. For a more convenient download files were zipped.</p> <p>Upon publication of results using this dataset, please cite the following paper:</p> <p>Uetz-von Allmen E, Rippl AV, Farhan H, Legler DF. 2018. A unique signal sequence of the chemokine receptor CCR7 promotes package into COPII vesicles for efficient receptor trafficking. J Leukoc Biol 104(2):375-389.</p>
ACKR4 Recruits GRK3 Prior to β-arrestins but Can Scavenge Chemokines in the Absence of β-arrestins
<p>Chemokines are essential for guiding cell migration. Atypical chemokine receptors (ACKRs) contribute to the cell migration process by binding, internalizing and degrading local chemokines, which enables the formation of confined gradients. ACKRs are heptahelical membrane spanning molecules structurally related to G-protein coupled receptors (GPCRs), but seem to be unable to signal through G-proteins upon ligand binding. ACKR4 internalizes the chemokines CCL19, CCL21, and CCL25 and is best known for shaping functional CCL21 gradients. Ligand binding to ACKR4 has been shown to recruit β-arrestins that has led to the assumption that chemokine scavenging relies on β-arrestin-mediated ACKR4 trafficking, a common internalization route taken by class A GPCRs. Here, we show that CCL19, CCL21, and CCL25 readily recruited β-arrestin1 and β-arrestin2 to human ACKR4, but found no evidence for β-arrestin-dependent or independent ACKR4-mediated activation of the kinases Erk1/2, Akt, or Src. However, we demonstrate that β-arrestins interacted with ACKR4 in the steady-state and contributed to the spontaneous trafficking of the receptor in the absence of chemokines. Deleting the C-terminus of ACKR4 not only interfered with the interaction of β-arrestins, but also with the uptake of fluorescently labeled cognate chemokines. We identify the GPCR kinase GRK3, and to a lesser extent GRK2, but not GRK4, GRK5, and GRK6, to be recruited to chemokine-stimulated ACKR4. We show that GRK3 recruitment preceded the recruitment of β-arrestins upon ACKR4 engagement and that GRK2/3 inhibition partially interfered with steady-state interaction and chemokine-driven recruitment of β-arrestins to ACKR4. Overexpressing β-arrestin2 accelerated the uptake of fluorescently labeled CCL19, indicating that β-arrestins contribute to the chemokine scavenging activity of ACKR4. By contrast, cells lacking β-arrestins were still capable to take up fluorescently labeled CCL19 demonstrating that β-arrestins are dispensable for chemokine scavenging by ACKR4.</p>
Novel Peptide-Based PET Probe for Non-invasive Imaging of C-X-C Chemokine Receptor Type 4 (CXCR4) in Tumors
<p>These are RAW data datasets of the following final paper</p> <p>Trotta, A.M., Aurilio, M., D'Alterio, C., Ieranò, C., Di Martino, D., Barbieri, A., Luciano, A., Gaballo, P., Santagata, S., Portella, L., Tomassi, S., Marinelli, L., Sementa, D., Novellino, E., Lastoria, S., Scala, S., Schottelius, M., Di Maro, S.</p> <p>Novel Peptide-Based PET Probe for Non-invasive Imaging of C-X-C Chemokine Receptor Type 4 (CXCR4) in Tumors, (2021) Journal of Medicinal Chemistry, 64 (6), pp. 3449-3461. ISSN 00222623</p> <p>https://doi.org/10.1021/acs.jmedchem.1c00066</p> <p>Abstract</p> <p>The recently reported CXCR4 antagonist 3 (Ac-Arg-Ala-[DCys-Arg-2Nal-His-Pen]-CO2H) was investigated as a molecular scaffold for a CXCR4-targeted positron emission tomography (PET) tracer. Toward this end, 3 was functionalized with 1,4,7,10-tetraazacyclododecane-1,4,7,10-tetraacetic acid (DOTA) and 1,4,7-triazacyclononanetriacetic acid (NOTA). On the basis of convincing affinity data, both tracers, [68Ga]NOTA analogue ([68Ga]-5) and [68Ga]DOTA analogue ([68Ga]-4), were evaluated for PET imaging in “in vivo” models of CHO-hCXCR4 and Daudi lymphoma cells. PET imaging and biodistribution studies revealed higher CXCR4-specific tumor uptake and high tumor/background ratios for the [68Ga]NOTA analogue ([68Ga]-5) than for the [68Ga]DOTA analogue ([68Ga]-4) in both in vivo models. Moreover, [68Ga]-4 and [68Ga]-5 displayed rapid clearance and very low levels of accumulation in all nontarget tissues but the kidney. Although the high tumor/background ratios observed in the mouse xenograft model could partially derive from the hCXCR4 selectivity of [68Ga]-5, our results encourage its translation into a clinical context as a novel peptide-based tracer for imaging of CXCR4-overexpressing tumors.</p> <p> </p> <p> </p>
Development of new PET radiotracers for CXCR3 chemokine receptors
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Chemokines kill bacteria without triggering antimicrobial resistance by binding anionic phospholipids
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Chemokines kill bacteria by binding anionic phospholipids without triggering antimicrobial resistance
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Engineering of Nanobodies recognizing the human chemokine receptor CCR7
<p>raw data of each figure published in 10.3390/ijms20102597 (Engineering of Nanobodies Recognizing the Human Chemokine Receptor CCR7)</p>
Chemokine G protein-coupled receptor (GPCR) mutation data set
<p>Curated set of 2004 quantitative mutation data points covering 10 chemokine G protein-coupled receptors, annotated according to GPCRdb standards (http://gpcrdb.org/) building from the data set published by Scholten et al. in BJP 2012, 165, 1617.</p>
Chemokine G protein-coupled receptor (GPCR) mutation data set - revision
<p>Curated set of 2004 quantitative mutation data points covering 10 chemokine G protein-coupled receptors, annotated according to GPCRdb standards (http://gpcrdb.org/) building from the data set published by Scholten et al. in BJP 2012, 165, 1617.</p> <p>Errors in the previous version were corrected and new data points for CCR2 and CCR9 were added.</p>
Computational data for Structure of G protein-coupled receptor GPR1 bound to full-length chemerin adipokine reveals a chemokine-like reverse binding mode
<p>MD simulation data for the research article titled "Structure of G protein-coupled receptor GPR1 bound to full-length chemerin adipokine reveals a chemokine-like reverse binding mode".</p>
A Phase 2, Multi-Center Study To Compare The Efficacy And Safety Of A Chemokine CCR2/5 Receptor Antagonist With Ranibizumab In Adults With Diabetic Macular Edema
ClinicalTrials.gov study NCT01994291. IPD Sharing: Not stated. Countries: 9. Publications: 1.
Dataset related to article "Control of Cytoskeletal Dynamics by β-Arrestin1/Myosin Vb Signaling Regulates Endosomal Sorting and Scavenging Activity of the Atypical Chemokine Receptor ACKR2"
<p>This record contains raw data related to article "Control of Cytoskeletal Dynamics by β-Arrestin1/Myosin Vb Signaling Regulates Endosomal Sorting and Scavenging Activity of the Atypical Chemokine Receptor ACKR2"</p> <p>The atypical chemokine receptor ACKR2, formerly named D6, is a scavenger chemokine receptor with a non-redundant role in the control of inflammation and immunity. The scavenging activity of ACKR2 depends on its trafficking properties, which require actin cytoskeleton rearrangements downstream of a β-arrestin1-Rac1-PAK1-LIMK1-cofilin-dependent signaling pathway. We here demonstrate that in basal conditions, ACKR2 trafficking properties require intact actin and microtubules networks. The dynamic turnover of actin filaments is required to sustain ACKR2 constitutive endocytosis, while both actin and microtubule networks are involved in processes regulating ACKR2 constitutive sorting to rapid, Rab4-dependent and slow, Rab11-dependent recycling pathways, respectively. After chemokine engagement, ACKR2 requires myosin Vb activity to promote its trafficking from Rab11-positive recycling endosomes to the plasma membrane, which sustains its scavenging activity. Other than cofilin phosphorylation, induction of the β-arrestin1-dependent signaling pathway by ACKR2 agonists also leads to the rearrangement of microtubules, which is required to support the myosin Vb-dependent ACKR2 upregulation and its scavenging properties. Disruption of the actin-based cytoskeleton by the apoptosis-inducing agent staurosporine results in impaired ACKR2 internalization and chemokine degradation that is consistent with the emerging scavenging-independent activity of the receptor in apoptotic neutrophils instrumental for promoting efficient efferocytosis during the resolution of inflammation. In conclusion, we provide evidence that ACKR2 activates a β-arrestin1-dependent signaling pathway, triggering both the actin and the microtubule cytoskeletal networks, which control its trafficking and scavenger properties.</p>
Colonic cytokines and chemokines in DNBS colitis
<p>Abdominal pain in irritable bowel syndrome and inflammatory bowel disease is thought to be driven by processes that sensitize sensory nerves innervating the gut. How sensory nerves become sensitized is not clear, but their terminals in the gut are surrounded by enteric glia. Here, we tested the hypothesis that intercellular enteric glia-to-nociceptor signaling contributes to visceral hypersensitivity during inflammation. In vivo and in vitro models of acute inflammation were used in combination with protein and RNA labeling, and cellular assays of activity and mediator release. Mechanisms of interaction between glia and nociceptors were studied using <em><span>Trpv1</span></em><em><sup>Cre;GCaMP5gtdT</sup><span>;GFAP-hM3Dq </span></em>mice, in which glial activity is controlled by chemogenetics while simultaneously recording nociceptor activity using calcium imaging. Mice lacking glial connexin-43 were used in combination with visceromotor reflex recordings to disrupt glial intercellular signaling and study its impact on visceral sensitivity. Acute colitis induces a transient increase in proinflammatory cytokines including IL-1β, which is produced in part by glia and facilitates glial connexin-43 function. Provoking glial activity under these conditions changes the normal benign influence of glia on nociceptors to one where glia have a sensitizing effect on gut-innervating nociceptors. The mechanisms responsible for glial-driven visceral hypersensitivity involve an upregulation of glial COX-2 and an increase in stimulated glial PGE2 release which acts on nociceptor EP4 receptors. In vivo recordings show that colonic IL-1β shifts normal innocuous stimuli toward a noxious range through mechanisms that require glial connexin-43. Enteric glia sensitize gut nociceptors during inflammation. Cell-specific therapies targeting the glial mechanisms identified here could benefit treatments for visceral pain.</p>
Supplementary data to publication "Cellular detection of the chemokine receptor CXCR4 in bovine mammary glands and its distribution and regulation on bovine leukocytes"
<p>Supplementary data to publication "Cellular detection of the chemokine receptor CXCR4 in bovine mammary glands and its distribution and regulation on bovine leukocytes" in Journal of Dairy Science; https://doi.org/10.3168/jds.2021-20799</p>
Supplementary FIles for Cholesterol Biases the Conformational Landscape of the Chemokine Receptor CCR3: A MAS SSNMR-Filtered Molecular Dynamics Study
<p>This repository contains supplementary files for the initial submission of:</p> <p>Cholesterol Biases the Conformational Landscape of the Chemokine Receptor CCR3: A MAS SSNMR-Filtered Molecular Dynamics Study<br> Evan J. van Aalst, Corey J. McDonald, and Benjamin J. Wylie</p> <p>Files found in this repository include:<br> 1. Raw fids corresponding to the solid-state NMR spectra used in this work.<br> 2. The script, model structures, and predicted chemical shifts used in the COMPASS proof of concept.<br> 3. Input molecular dynamics files derived from CHARMM-GUI including all mdp files, initial model structure files, and the production script.<br> 4. Model structures per ns derived from MD trajectories with corresponding predicted chemical shift lists and associated experimental chemical shift lists.</p>
Fractalkine, a CX3C Chemokine, Act as a Mediator of Ocular Angiogenesis
ClinicalTrials.gov study NCT00728598. IPD Sharing: Not stated. Countries: 1. Publications: 2.
Effect of Smoking on Macrophage-related Chemokines Before and After Non-surgical Treatment of Initial Peri-implantitis
ClinicalTrials.gov study NCT06810401. IPD Sharing: NO. Countries: 1. Publications: 1.
Safety Study of a Chemokine Receptor (CXCR4) Antagonist in Multiple Myeloma Patients
ClinicalTrials.gov study NCT01010880. IPD Sharing: Not stated. Countries: 1. Publications: 1.
Chemokine Receptor CXCR4-targeting Molecular Imaging for Metabolic Characterization of Multiple Myeloma and Lymphoma
ClinicalTrials.gov study NCT03436342. IPD Sharing: NO. Countries: 1. Publications: 2.
A Prospective, Placebo Controlled, Double-Blind, Cross-over Study on the Effects of a Probiotic Preparation (VSL#3) on Metabolic Profile, Intestinal Permeability, Microbiota, Cytokines and Chemokines
ClinicalTrials.gov study NCT01632462. IPD Sharing: Not stated. Countries: 1. Publications: 11.
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Allen Brain Atlas
Allen Brain Atlas is an Allen Institute collection of brain map atlases, datasets, APIs, and analysis tools covering mouse, human, and non-human primate brain resources.
Annotated Behaviour and Observability Dataset (ABODe)
ABODe is a University of Edinburgh DataShare dataset for behavior classification in group-housed mice using home-cage video, identities, bounding boxes, ground-plate positions, and annotator labels.
DANDI Archive for NWB datasets
DANDI is a BRAIN Initiative archive for publishing and sharing neurophysiology data, including electrophysiology, optophysiology, and behavioral data packaged as NWB and related standards.
International Brain Laboratory public data
The International Brain Laboratory public data releases expose standardized mouse decision-making experiments, including Neuropixels recordings, widefield calcium imaging, behavior, and session metadata accessed through the ONE API.
OpenNeuro
OpenNeuro is a free, open platform for sharing neuroimaging datasets, with public search, dataset pages, and download paths for web, S3, DataLad, and the OpenNeuro CLI.