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Artikel ; Online: trans

Alzahrani, Seraj O / McRobbie, Graeme / Khan, Abid / D'huys, Thomas / Van Loy, Tom / Walker, Ashlie N / Renard, Isaline / Hubin, Timothy J / Schols, Dominique / Burke, Benjamin P / Archibald, Stephen J

Dalton transactions (Cambridge, England : 2003)

2024 Band 53, Heft 12, Seite(n) 5616–5623

Abstract: The chemokine receptor CXCR4 is implicated in multiple diseases including inflammatory disorders, cancer growth and metastasis, and HIV/AIDS. CXCR4 targeting has been evaluated in treating cancer metastasis and therapy resistance. Cyclam derivatives, ... ...

Abstract	The chemokine receptor CXCR4 is implicated in multiple diseases including inflammatory disorders, cancer growth and metastasis, and HIV/AIDS. CXCR4 targeting has been evaluated in treating cancer metastasis and therapy resistance. Cyclam derivatives, most notably AMD3100 (Plerixafor™), are a common motif in small molecule CXCR4 antagonists. However, AMD3100 has not been shown to be effective in cancer treatment as an individual agent. Configurational restriction and transition metal complex formation increases receptor binding affinity and residence time. In the present study, we have synthesized novel
Mesh-Begriff(e)	Benzylamines ; Coordination Complexes/pharmacology ; Cyclams ; Heterocyclic Compounds/pharmacology ; Heterocyclic Compounds/chemistry ; Receptors, CXCR4/antagonists & inhibitors
Chemische Substanzen	Benzylamines ; Coordination Complexes ; cyclam (295-37-4) ; Cyclams ; Heterocyclic Compounds ; plerixafor (S915P5499N) ; Receptors, CXCR4
Sprache	Englisch
Erscheinungsdatum	2024-03-19
Erscheinungsland	England
Dokumenttyp	Journal Article
ZDB-ID	1472887-4
ISSN	1477-9234 ; 1364-5447 ; 0300-9246 ; 1477-9226
ISSN (online)	1477-9234 ; 1364-5447
ISSN	0300-9246 ; 1477-9226
DOI	10.1039/d3dt01729j
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel: CXCR7/ACKR3-targeting ligands interfere with X7 HIV-1 and HIV-2 entry and replication in human host cells.

D'huys, Thomas / Claes, Sandra / Van Loy, Tom / Schols, Dominique

Heliyon

2018 Band 4, Heft 3, Seite(n) e00557

Abstract: Chemokine receptors CCR5 and CXCR4 are considered the main coreceptors for initial HIV infection, replication and transmission, and subsequent AIDS progression. Over the years, other chemokine receptors, belonging to the family of G protein-coupled ... ...

Abstract	Chemokine receptors CCR5 and CXCR4 are considered the main coreceptors for initial HIV infection, replication and transmission, and subsequent AIDS progression. Over the years, other chemokine receptors, belonging to the family of G protein-coupled receptors, have also been identified as candidate coreceptors for HIV entry into human host cells. Amongst them, CXCR7, also known as atypical chemokine receptor 3 (ACKR3), was suggested as a coreceptor candidate capable of facilitating both HIV-1 and HIV-2 entry
Sprache	Englisch
Erscheinungsdatum	2018-03-01
Erscheinungsland	England
Dokumenttyp	Journal Article
ZDB-ID	2835763-2
ISSN	2405-8440
ISSN	2405-8440
DOI	10.1016/j.heliyon.2018.e00557
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: Biological characterization of ligands targeting the human CC chemokine receptor 8 (CCR8) reveals the biased signaling properties of small molecule agonists.

Liu, Libao / Doijen, Jordi / D'huys, Thomas / Verhaegen, Yenthel / Dehaen, Wim / De Jonghe, Steven / Schols, Dominique / Van Loy, Tom

Biochemical pharmacology

2021 Band 188, Seite(n) 114565

Abstract: The human CC chemokine receptor 8 (CCR8) is a promising drug target for cancer immunotherapy and autoimmune disease. Besides human and viral chemokines, previous studies revealed diverse classes of CCR8-targeting small molecules. We characterized a ... ...

Abstract	The human CC chemokine receptor 8 (CCR8) is a promising drug target for cancer immunotherapy and autoimmune disease. Besides human and viral chemokines, previous studies revealed diverse classes of CCR8-targeting small molecules. We characterized a selection of these CCR8 ligands (hCCL1, vCCL1, ZK756326, AZ6; CCR8 agonists and a naphthalene-sulfonamide-based CCR8 antagonist), in in vitro cell-based assays (hCCL1
Mesh-Begriff(e)	Chemokine CCL1/administration & dosage ; Chemokine CCL1/metabolism ; Chemokine CCL8/administration & dosage ; Chemokine CCL8/metabolism ; Chemokines, CC/administration & dosage ; Chemokines, CC/metabolism ; Dose-Response Relationship, Drug ; Drug Delivery Systems/methods ; Humans ; Jurkat Cells ; Ligands ; Receptors, CCR8/agonists ; Receptors, CCR8/antagonists & inhibitors ; Receptors, CCR8/metabolism ; Signal Transduction/drug effects ; Signal Transduction/physiology
Chemische Substanzen	CCL1 protein, human ; CCL18 protein, human ; CCL8 protein, human ; CCR8 protein, human ; Chemokine CCL1 ; Chemokine CCL8 ; Chemokines, CC ; Ligands ; Receptors, CCR8
Sprache	Englisch
Erscheinungsdatum	2021-04-17
Erscheinungsland	England
Dokumenttyp	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	208787-x
ISSN	1873-2968 ; 0006-2952
ISSN (online)	1873-2968
ISSN	0006-2952
DOI	10.1016/j.bcp.2021.114565
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel: CXCR7/ACKR3-targeting ligands interfere with X7 HIV-1 and HIV-2 entry and replication in human host cells

D'huys, Thomas / Claes, Sandra / Van Loy, Tom / Schols, Dominique

Heliyon. 2018 Mar., v. 4, no. 3

2018

Abstract	Chemokine receptors CCR5 and CXCR4 are considered the main coreceptors for initial HIV infection, replication and transmission, and subsequent AIDS progression. Over the years, other chemokine receptors, belonging to the family of G protein-coupled receptors, have also been identified as candidate coreceptors for HIV entry into human host cells. Amongst them, CXCR7, also known as atypical chemokine receptor 3 (ACKR3), was suggested as a coreceptor candidate capable of facilitating both HIV-1 and HIV-2 entry in vitro. In this study, a cellular infection model was established to further decipher the role of CXCR7 as an HIV coreceptor. Using this model, CXCR7-mediated viral entry was demonstrated for several clinical HIV isolates as well as laboratory strains. Of interest, the X4-tropic HIV-1 HE strain showed rapid adaptation towards CXCR7-mediated infection after continuous passaging on CD4- and CXCR7-expressing cells. Furthermore, we uncovered anti-CXCR7 monoclonal antibodies, small molecule CXCR7 inhibitors and the natural CXCR7 chemokine ligands as potent inhibitors of CXCR7 receptor-mediated HIV entry and replication. Even though the clinical relevance of CXCR7-mediated HIV infection remains poorly understood, our data suggest that divergent HIV-1 and HIV-2 strains can quickly adapt their coreceptor usage depending on the cellular environment, which warrants further investigation.
Schlagwörter	HIV infections ; atypical chemokine receptor 3 ; chemokines ; humans ; ligands ; models
Sprache	Englisch
Erscheinungsverlauf	2018-03
Erscheinungsort	Elsevier Ltd
Dokumenttyp	Artikel
Anmerkung	NAL-AP-2-clean
ZDB-ID	2835763-2
ISSN	2405-8440
ISSN	2405-8440
DOI	10.1016/j.heliyon.2018.e00557
Datenquelle	NAL Katalog (AGRICOLA)

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Artikel: A kinetic fluorescence-based ca2+ mobilization assay to identify g protein-coupled receptor agonists, antagonists, and allosteric modulators

Claes, Sandra / D'huys, Thomas / Van Hout, Anneleen / Schols, Dominique / Van Loy, Tom

Journal of visualized experiments. 2018 Feb. 20, , no. 132

2018

Abstract: G protein-coupled receptors (GPCRs) are of great importance to the pharmaceutical industry as they are involved in many human diseases and include well-validated targets for therapeutic intervention. Discovery of lead compounds, including small synthetic ...

Abstract	G protein-coupled receptors (GPCRs) are of great importance to the pharmaceutical industry as they are involved in many human diseases and include well-validated targets for therapeutic intervention. Discovery of lead compounds, including small synthetic molecules, that specifically inhibit the receptor's function, is an important initial step in drug development and relies on sensitive, specific, and robust cell-based assays. Here, we describe a kinetic cellular assay with a fluorescent readout primarily designed to identify receptor-specific antagonists that inhibit the intracellular Ca2+ release evoked upon the activation of the CXC chemokine receptor 4 (CXCR4) by its endogenous ligand, the CXC chemokine ligand 12 (CXCL12). A key advantage of this method is that it also enables screening of compounds endowed with intrinsic agonistic properties (i.e., compounds eliciting an increase in intracellular Ca2+ concentration in the absence of CXCL12) or compounds modulating the receptor's function via interaction with allosteric binding sites (i.e., positive and negative allosteric modulators (PAMs and NAMs, respectively)). On the down side, autofluorescent compounds might interfere with the assay's readout, thereby hampering reliable data interpretation. Most likely this assay can be implemented, with minimal adaptations, as a generic drug discovery assay for many other GPCRs of which the activation leads to a release of intracellular Ca2+.
Schlagwörter	CXCR4 receptor ; agonists ; antagonists ; binding sites ; calcium ; chemokine CXCL12 ; drugs ; fluorescence ; human diseases ; ligands ; pharmaceutical industry ; screening ; therapeutics
Sprache	Englisch
Erscheinungsverlauf	2018-0220
Umfang	p. e56780.
Erscheinungsort	Journal of Visualized Experiments
Dokumenttyp	Artikel
ZDB-ID	2259946-0
ISSN	1940-087X
ISSN	1940-087X
DOI	10.3791/56780
Datenquelle	NAL Katalog (AGRICOLA)

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Artikel: A flow cytometry-based assay to identify compounds that disrupt binding of fluorescently-labeled cxc chemokine ligand 12 to cxc chemokine receptor 4

Schoofs, Geert / Van Hout, Anneleen / D'huys, Thomas / Schols, Dominique / Van Loy, Tom

Journal of visualized experiments. 2018 Mar. 10, , no. 133

2018

Abstract: Pharmacological targeting of G protein-coupled receptors (GPCRs) is of great importance to human health, as dysfunctional GPCR-mediated signaling contributes to the progression of many diseases. The ligand/receptor pair CXC chemokine ligand 12 (CXCL12)/ ... ...

Abstract	Pharmacological targeting of G protein-coupled receptors (GPCRs) is of great importance to human health, as dysfunctional GPCR-mediated signaling contributes to the progression of many diseases. The ligand/receptor pair CXC chemokine ligand 12 (CXCL12)/CXC chemokine receptor 4 (CXCR4) has raised significant clinical interest, for instance as a potential target for the treatment of cancer and inflammatory diseases. Small molecules as well as therapeutic antibodies that specifically target CXCR4 and inhibit the receptor's function are therefore considered to be valuable pharmacological tools. Here, a flow cytometry-based cellular assay that allows identification of compounds (e.g., small molecules) that abrogate CXCL12 binding to CXCR4, is described. Essentially, the assay relies on the competition for receptor binding between a fixed amount of fluorescently labeled CXCL12, the natural chemokine agonist for CXCR4, and unlabeled compounds. Hence, the undesirable use of radioactively labeled probes is avoided in this assay. In addition, living cells are used as the source of receptor (CXCR4) instead of cell membrane preparations. This allows easy adaptation of the assay to a plate format, which increases the throughput. This assay has been shown to be a valuable generic drug discovery assay to identify CXCR4-targeting compounds. The protocol can likely be adapted to other GPCRs, at least if fluorescently labeled ligands are available or can be generated. Prior knowledge concerning the intracellular signaling pathways that are induced upon activation of these GPCRs, is not required.
Schlagwörter	CXCR4 receptor ; agonists ; antibodies ; cell membranes ; chemokine CXCL12 ; human health ; ligands ; neoplasms ; signal transduction ; therapeutics
Sprache	Englisch
Erscheinungsverlauf	2018-0310
Umfang	p. e57271.
Erscheinungsort	Journal of Visualized Experiments
Dokumenttyp	Artikel
ZDB-ID	2259946-0
ISSN	1940-087X
ISSN	1940-087X
DOI	10.3791/57271
Datenquelle	NAL Katalog (AGRICOLA)

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Artikel ; Online: Carbohydrate-binding protein from stinging nettle as fusion inhibitor for SARS-CoV-2 variants of concern.

Vanhulle, Emiel / D'huys, Thomas / Provinciael, Becky / Stroobants, Joren / Camps, Anita / Noppen, Sam / Schols, Dominique / Van Damme, Els J M / Maes, Piet / Stevaert, Annelies / Vermeire, Kurt

Frontiers in cellular and infection microbiology

2022 Band 12, Seite(n) 989534

Abstract: ... Urtica ... ...

Abstract	Urtica dioica
Mesh-Begriff(e)	Angiotensin-Converting Enzyme 2 ; Anti-Retroviral Agents ; Antiviral Agents/pharmacology ; COVID-19 ; Carbohydrates ; Europium ; Humans ; Receptors, Cell Surface ; SARS-CoV-2/genetics ; Spike Glycoprotein, Coronavirus/genetics ; Spike Glycoprotein, Coronavirus/metabolism ; Urtica dioica/metabolism ; Viral Proteins
Chemische Substanzen	Anti-Retroviral Agents ; Antiviral Agents ; Carbohydrates ; Receptors, Cell Surface ; Spike Glycoprotein, Coronavirus ; Viral Proteins ; saccharide-binding proteins ; spike protein, SARS-CoV-2 ; Europium (444W947O8O) ; Angiotensin-Converting Enzyme 2 (EC 3.4.17.23)
Sprache	Englisch
Erscheinungsdatum	2022-08-30
Erscheinungsland	Switzerland
Dokumenttyp	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	2619676-1
ISSN	2235-2988 ; 2235-2988
ISSN (online)	2235-2988
ISSN	2235-2988
DOI	10.3389/fcimb.2022.989534
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: A Kinetic Fluorescence-based Ca2+ Mobilization Assay to Identify G Protein-coupled Receptor Agonists, Antagonists, and Allosteric Modulators.

Claes, Sandra / D'huys, Thomas / Van Hout, Anneleen / Schols, Dominique / Van Loy, Tom

Journal of visualized experiments : JoVE

2018 , Heft 132

Abstract	G protein-coupled receptors (GPCRs) are of great importance to the pharmaceutical industry as they are involved in many human diseases and include well-validated targets for therapeutic intervention. Discovery of lead compounds, including small synthetic molecules, that specifically inhibit the receptor's function, is an important initial step in drug development and relies on sensitive, specific, and robust cell-based assays. Here, we describe a kinetic cellular assay with a fluorescent readout primarily designed to identify receptor-specific antagonists that inhibit the intracellular Ca
Mesh-Begriff(e)	Allosteric Regulation/physiology ; Fluorescence ; Humans ; Kinetics ; Receptors, G-Protein-Coupled/metabolism
Chemische Substanzen	Receptors, G-Protein-Coupled
Sprache	Englisch
Erscheinungsdatum	2018-02-20
Erscheinungsland	United States
Dokumenttyp	Journal Article ; Research Support, Non-U.S. Gov't ; Video-Audio Media
ZDB-ID	2259946-0
ISSN	1940-087X ; 1940-087X
ISSN (online)	1940-087X
ISSN	1940-087X
DOI	10.3791/56780
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: A Flow Cytometry-based Assay to Identify Compounds That Disrupt Binding of Fluorescently-labeled CXC Chemokine Ligand 12 to CXC Chemokine Receptor 4.

Schoofs, Geert / Van Hout, Anneleen / D'huys, Thomas / Schols, Dominique / Van Loy, Tom

Journal of visualized experiments : JoVE

2018 , Heft 133

Abstract	Pharmacological targeting of G protein-coupled receptors (GPCRs) is of great importance to human health, as dysfunctional GPCR-mediated signaling contributes to the progression of many diseases. The ligand/receptor pair CXC chemokine ligand 12 (CXCL12)/CXC chemokine receptor 4 (CXCR4) has raised significant clinical interest, for instance as a potential target for the treatment of cancer and inflammatory diseases. Small molecules as well as therapeutic antibodies that specifically target CXCR4 and inhibit the receptor's function are therefore considered to be valuable pharmacological tools. Here, a flow cytometry-based cellular assay that allows identification of compounds (e.g., small molecules) that abrogate CXCL12 binding to CXCR4, is described. Essentially, the assay relies on the competition for receptor binding between a fixed amount of fluorescently labeled CXCL12, the natural chemokine agonist for CXCR4, and unlabeled compounds. Hence, the undesirable use of radioactively labeled probes is avoided in this assay. In addition, living cells are used as the source of receptor (CXCR4) instead of cell membrane preparations. This allows easy adaptation of the assay to a plate format, which increases the throughput. This assay has been shown to be a valuable generic drug discovery assay to identify CXCR4-targeting compounds. The protocol can likely be adapted to other GPCRs, at least if fluorescently labeled ligands are available or can be generated. Prior knowledge concerning the intracellular signaling pathways that are induced upon activation of these GPCRs, is not required.
Mesh-Begriff(e)	Binding, Competitive ; Chemokine CXCL12/antagonists & inhibitors ; Chemokine CXCL12/metabolism ; Drug Evaluation, Preclinical/methods ; Flow Cytometry/methods ; Fluorescent Dyes ; Humans ; Jurkat Cells ; Ligands ; Protein Binding ; Receptors, CXCR4/antagonists & inhibitors ; Receptors, CXCR4/metabolism ; Small Molecule Libraries/pharmacology
Chemische Substanzen	CXCL12 protein, human ; CXCR4 protein, human ; Chemokine CXCL12 ; Fluorescent Dyes ; Ligands ; Receptors, CXCR4 ; Small Molecule Libraries
Sprache	Englisch
Erscheinungsdatum	2018-03-10
Erscheinungsland	United States
Dokumenttyp	Journal Article ; Research Support, Non-U.S. Gov't ; Video-Audio Media
ZDB-ID	2259946-0
ISSN	1940-087X ; 1940-087X
ISSN (online)	1940-087X
ISSN	1940-087X
DOI	10.3791/57271
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: Comparison of cell-based assays for the identification and evaluation of competitive CXCR4 inhibitors.

Van Hout, Anneleen / D'huys, Thomas / Oeyen, Merel / Schols, Dominique / Van Loy, Tom

PloS one

2017 Band 12, Heft 4, Seite(n) e0176057

Abstract: The chemokine receptor CXCR4 is activated by its unique chemokine ligand CXCL12 and regulates many physiological and developmental processes such as hematopoietic cell trafficking. CXCR4 is also one of the main co-receptors for human immunodeficiency ... ...

Abstract	The chemokine receptor CXCR4 is activated by its unique chemokine ligand CXCL12 and regulates many physiological and developmental processes such as hematopoietic cell trafficking. CXCR4 is also one of the main co-receptors for human immunodeficiency virus (HIV) entry. Dysfunction of the CXCL12/CXCR4 axis contributes to several human pathologies, including cancer and inflammatory diseases. Consequently, inhibition of CXCR4 activation is recognized as an attractive target for therapeutic intervention. In this regard, numerous agents modifying CXCR4 activity have been evaluated in in vitro experimental studies and pre-clinical models. Here, we evaluated a CXCL12 competition binding assay for its potential as a valuable initial screen for functional and competitive CXCR4 inhibitors. In total, 11 structurally diverse compounds were included in a side-by-side comparison of in vitro CXCR4 cell-based assays, such as CXCL12 competition binding, CXCL12-induced calcium signaling, CXCR4 internalization, CXCL12-guided cell migration and CXCR4-specific HIV-1 replication experiments. Our data indicated that agents that inhibit CXCL12 binding, i.e. the anti-CXCR4 peptide analogs T22, T140 and TC14012 and the small molecule antagonists AMD3100, AMD3465, AMD11070 and IT1t showed inhibitory activity with consistent relative potencies in all further applied CXCR4-related assays. Accordingly, agents exerting no or very weak receptor binding (i.e., CTCE-9908, WZ811, Me6TREN and gambogic acid) showed no or very poor anti-CXCR4 inhibitory activity. Thus, CXCL12 competition binding studies were proven to be highly valuable as an initial screening assay and indicative for the pharmacological and functional profile of competitive CXCR4 antagonists, which will help the design of new potent CXCR4 inhibitors.
Mesh-Begriff(e)	Aminopyridines/chemistry ; Aminopyridines/metabolism ; Aminopyridines/toxicity ; Anti-HIV Agents/chemistry ; Anti-HIV Agents/metabolism ; Anti-HIV Agents/toxicity ; Benzylamines/chemistry ; Benzylamines/metabolism ; Benzylamines/toxicity ; Binding, Competitive ; Calcium Signaling/drug effects ; Cell Line, Tumor ; Cell Movement/drug effects ; Cell Survival/drug effects ; Chemokine CXCL12/chemistry ; Chemokine CXCL12/metabolism ; Heterocyclic Compounds/chemistry ; Heterocyclic Compounds/metabolism ; Heterocyclic Compounds/toxicity ; Humans ; Jurkat Cells ; Protein Binding ; Pyridines/chemistry ; Pyridines/metabolism ; Pyridines/toxicity ; Receptors, CXCR4/antagonists & inhibitors ; Receptors, CXCR4/metabolism
Chemische Substanzen	Aminopyridines ; Anti-HIV Agents ; Benzylamines ; Chemokine CXCL12 ; Heterocyclic Compounds ; N,N'-di-2-pyridinyl-1,4-benzenedimethanamine ; N-(1,4,8,11- tetraazacyclotetradecanyl-1,4-phenylenebis(methylene))-2-(aminomethyl)- pyridine ; Pyridines ; Receptors, CXCR4 ; plerixafor (S915P5499N)
Sprache	Englisch
Erscheinungsdatum	2017-04-14
Erscheinungsland	United States
Dokumenttyp	Comparative Study ; Journal Article
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0176057
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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