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Article ; Online: Identifying G protein-coupled receptors involved in adipose tissue function using the innovative RNA-seq database FATTLAS.

Kaczmarek, Isabell / Wower, Isabel / Ettig, Katja / Kuhn, Christina Katharina / Kraft, Robert / Landgraf, Kathrin / Körner, Antje / Schöneberg, Torsten / Horn, Susanne / Thor, Doreen

iScience

2023 Volume 26, Issue 10, Page(s) 107841

Abstract: G protein-coupled receptors (GPCRs) modulate the function of adipose tissue (AT) in general and ... in AT, their repertoire as well as their regulation and function in (patho)physiological conditions (e.g., obesity) is not ...

Abstract	G protein-coupled receptors (GPCRs) modulate the function of adipose tissue (AT) in general and of adipocytes, specifically. Although it is well-established that GPCRs are widely expressed in AT, their repertoire as well as their regulation and function in (patho)physiological conditions (e.g., obesity) is not fully resolved. Here, we established FATTLAS, an interactive public database, for improved access and analysis of RNA-seq data of mouse and human AT. After extracting the GPCRome of non-obese and obese individuals, highly expressed and differentially regulated GPCRs were identified. Exemplarily, we describe four receptors (GPR146, MRGPRF, FZD5, PTGER2) and analyzed their functions in a (pre)adipocyte cell model. Besides all receptors being involved in adipogenesis, MRGPRF is essential for adipocyte viability and regulates cAMP levels, while GPR146 modulates adipocyte lipolysis via constitutive activation of Gi proteins. Taken together, by implementing and using FATTLAS we describe four hitherto unrecognized GPCRs associated with AT function and adipogenesis.
Language	English
Publishing date	2023-09-09
Publishing country	United States
Document type	Journal Article
ISSN	2589-0042
ISSN (online)	2589-0042
DOI	10.1016/j.isci.2023.107841
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Conference proceedings: Role of a G-CSF/IL-13 Ratio and Cytokine Dynamics in ALT Flares

Souleiman, Roni / Ristic, Tijana / Freyer, Erich / Steppich, Katja / Falk, Christine S. / Maasoumy, Benjamin / Wedemeyer, Heiner / Kraft, Anke / Heinrich, Bernd / Cornberg, Markus

Zeitschrift für Gastroenterologie

2024 Volume 62, Issue 01

Event/congress	40. Jahrestagung der Deutschen Arbeitsgemeinschaft zum Studium der Leber, Haus der Technik e.V., Essen, 2024-01-26
Language	German
Publishing date	2024-01-01
Publisher	Georg Thieme Verlag
Publishing place	Stuttgart ; New York
Document type	Article ; Conference proceedings
ZDB-ID	201387-3
ISSN	1439-7803 ; 0044-2771 ; 0172-8504
ISSN (online)	1439-7803
ISSN	0044-2771 ; 0172-8504
DOI	10.1055/s-0043-1777631
Database	Thieme publisher's database

In stock of ZB MED Cologne/Königswinter

Zs.A 111: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
Zs.A 111/X: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)

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Article: Label-free multiplex sensing from buffer and immunoglobulin G sensing from whole blood with photonic crystal slabs using angle-tuning of an optical interference filter.

Kraft, Fabio A / Baur, Holger / Bommer, Moritz / Latz, Andreas / Fitschen-Oestern, Stefanie / Fuchs, Sabine / Gerken, Martina

Biomedical optics express

2023 Volume 14, Issue 5, Page(s) 2293–2310

Abstract: ... In a first proof of principle experiment, we demonstrate the ability to detect immunoglobulins G (IgG ...

Abstract	Direct detection of biomarkers from unpurified whole blood has been a challenge for label-free detection platforms, such as photonic crystal slabs (PCS). A wide range of measurement concepts for PCS exist, but exhibit technical limitations, which render them unsuitable for label-free biosensing with unfiltered whole blood. In this work, we single out the requirements for a label-free point-of-care setup based on PCS and present a wavelength selecting concept by angle tuning of an optical interference filter, which fulfills these requirements. We investigate the limit of detection (LOD) for bulk refractive index changes and obtain a value of 3.4 E-4 refractive index units (RIU). We demonstrate label-free multiplex detection for different types of immobilization entities, including aptamers, antigens, and simple proteins. For this multiplex setup we detect thrombin at a concentration of 6.3 µg/ml, antibodies of glutathione S-transferase (GST) diluted by a factor of 250, and streptavidin at a concentration of 33 µg/ml. In a first proof of principle experiment, we demonstrate the ability to detect immunoglobulins G (IgG) from unfiltered whole blood. These experiments are conducted directly in the hospital without temperature control of the photonic crystal transducer surface or the blood sample. We set the detected concentration levels into a medical frame of reference and point out possible applications.
Language	English
Publishing date	2023-04-26
Publishing country	United States
Document type	Journal Article
ZDB-ID	2572216-5
ISSN	2156-7085
ISSN	2156-7085
DOI	10.1364/BOE.489138
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Article: Exploring G Protein-Coupled Receptor Signaling in Primary Pancreatic Islets.

Röthe, Juliane / Kraft, Robert / Schöneberg, Torsten / Thor, Doreen

Biological procedures online

2020 Volume 22, Page(s) 4

Abstract: Background: Targeting G protein-coupled receptors (GPCRs) in pancreatic cells is feasible ... GPCRs can couple to more than one G-protein family, results obtained in pancreatic cell lines do not ...

Abstract	Background: Targeting G protein-coupled receptors (GPCRs) in pancreatic cells is feasible to modulate glucose-induced insulin secretion. Because pancreatic islets consist of several cell types and GPCRs can couple to more than one G-protein family, results obtained in pancreatic cell lines do not always match the response in primary cells or intact islets. Therefore, we set out to establish a protocol to analyze second messenger activation in mouse pancreatic islets. Results: Activation of Gq/11-coupled receptor expressed in primary β cells increased the second messenger IP1 in an accumulation assay. Applying a Gq/11 protein inhibitor completely abolished this signal. Activation of the V1 vasopressin and ghrelin receptors, predominantly expressed in the less abundant alpha and delta cells, was not sufficient to induce a significant IP1 increase in this assay. However, fura-2-based fluorescence imaging showed calcium signals upon application of arginine vasopressin or ghrelin within intact pancreatic islets. Using the here established protocol we were also able to determine changes in intracellular cAMP levels induced by receptors coupling to Gs and Gi/o proteins. Conclusions: Detection of the second messengers IP1, cAMP, and calcium, can be used to reliably analyze GPCR activation in intact islets.
Language	English
Publishing date	2020-02-15
Publishing country	England
Document type	Journal Article
ZDB-ID	2027823-8
ISSN	1480-9222
ISSN	1480-9222
DOI	10.1186/s12575-019-0116-y
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Article ; Online: Natural biased signaling of hydroxycarboxylic acid receptor 3 and G protein-coupled receptor 84.

Peters, Anna / Rabe, Philipp / Krumbholz, Petra / Kalwa, Hermann / Kraft, Robert / Schöneberg, Torsten / Stäubert, Claudia

Cell communication and signaling : CCS

2020 Volume 18, Issue 1, Page(s) 31

Abstract: ... produced in humans, food-derived or originating from bacteria. They activate G protein-coupled receptors ...

Abstract	Background: Medium-chain fatty acids and their 3-hydroxy derivatives are metabolites endogenously produced in humans, food-derived or originating from bacteria. They activate G protein-coupled receptors, including GPR84 and HCA Methods: To study the signaling kinetics and components involved in signal transduction of both receptors we applied the label-free dynamic mass redistribution technology in combination with classical cAMP, ERK signaling and β-arrestin-2 recruitment assays. For phenotypical analyses, we used spheroid cell culture models. Results: We present strong evidence for a natural biased signaling of structurally highly similar agonists at HCA Conclusions: In summary, our results highlight that biased agonism is a physiological property of HCA
MeSH term(s)	Animals ; CHO Cells ; Cricetulus ; HEK293 Cells ; Humans ; Kinetics ; Receptors, G-Protein-Coupled/immunology ; Receptors, Nicotinic/immunology ; Signal Transduction/immunology
Chemical Substances	GPR84 protein, human ; HCAR3 protein, human ; Receptors, G-Protein-Coupled ; Receptors, Nicotinic
Language	English
Publishing date	2020-02-26
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Video-Audio Media
ISSN	1478-811X
ISSN (online)	1478-811X
DOI	10.1186/s12964-020-0516-2
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Article ; Online: Hydroxycarboxylic acid receptor 3 and GPR84 - Two metabolite-sensing G protein-coupled receptors with opposing functions in innate immune cells.

Peters, Anna / Rabe, Philipp / Liebing, Aenne-Dorothea / Krumbholz, Petra / Nordström, Anders / Jäger, Elisabeth / Kraft, Robert / Stäubert, Claudia

Pharmacological research

2021 Volume 176, Page(s) 106047

Abstract: G protein-coupled receptors (GPCRs) are key regulatory proteins of immune cell function inducing ...

Abstract	G protein-coupled receptors (GPCRs) are key regulatory proteins of immune cell function inducing signaling in response to extracellular (pathogenic) stimuli. Although unrelated, hydroxycarboxylic acid receptor 3 (HCA
MeSH term(s)	Cells, Cultured ; Cytokines/metabolism ; Escherichia coli/growth & development ; Extracellular Signal-Regulated MAP Kinases/metabolism ; Humans ; Immunity, Innate ; Lactobacillales ; Macrophages/metabolism ; Neutrophils/metabolism ; Phagocytosis ; Reactive Oxygen Species/metabolism ; Receptors, G-Protein-Coupled/genetics ; Receptors, G-Protein-Coupled/metabolism ; Receptors, Nicotinic/genetics ; Receptors, Nicotinic/metabolism
Chemical Substances	Cytokines ; GPR84 protein, human ; HCAR3 protein, human ; Reactive Oxygen Species ; Receptors, G-Protein-Coupled ; Receptors, Nicotinic ; Extracellular Signal-Regulated MAP Kinases (EC 2.7.11.24)
Language	English
Publishing date	2021-12-27
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1003347-6
ISSN	1096-1186 ; 0031-6989 ; 1043-6618
ISSN (online)	1096-1186
ISSN	0031-6989 ; 1043-6618
DOI	10.1016/j.phrs.2021.106047
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Zs.A 721: Show issues

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ab Jg. 2022: Lesesaal (EG)

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Article ; Online: Phototransduction gain at the G-protein, transducin, and effector protein, phosphodiesterase-6, stages in retinal rods.

Heck, Martin / Hofmann, Klaus Peter / Kraft, Timothy W / Lamb, Trevor D

Proceedings of the National Academy of Sciences of the United States of America

2019 Volume 116, Issue 18, Page(s) 8653–8654

MeSH term(s)	Cyclic Nucleotide Phosphodiesterases, Type 6 ; GTP-Binding Proteins ; Light Signal Transduction ; Retinal Rod Photoreceptor Cells ; Transducin
Chemical Substances	Cyclic Nucleotide Phosphodiesterases, Type 6 (EC 3.1.4.35) ; GTP-Binding Proteins (EC 3.6.1.-) ; Transducin (EC 3.6.5.1)
Language	English
Publishing date	2019-04-30
Publishing country	United States
Document type	Letter ; Comment
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.1904017116
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Zs.A 1148: Show issues

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Jg. 1995 - 2021: Lesesall (1.OG)
ab Jg. 2022: Lesesaal (EG)

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Article ; Online: Small-Molecule-Targeting Hairpin Loop of hTERT Promoter G-Quadruplex Induces Cancer Cell Death.

Song, Jin H / Kang, Hyun-Jin / Luevano, Libia A / Gokhale, Vijay / Wu, Kui / Pandey, Ritu / Sherry Chow, H-H / Hurley, Laurence H / Kraft, Andrew S

Cell chemical biology

2019 Volume 26, Issue 8, Page(s) 1110–1121.e4

Abstract: ... of targeting the telomerase enzyme directly, small molecules that bind to the G-hairpin of the hTERT G ... RG260 targets the hTERT G-quadruplex stem-loop folding but not tetrad DNAs, leading to downregulation ...

Abstract	Increased telomerase activity is associated with malignancy and poor prognosis in human cancer, but the development of targeted agents has not yet provided clinical benefit. Here we report that, instead of targeting the telomerase enzyme directly, small molecules that bind to the G-hairpin of the hTERT G-quadruplex-forming sequence kill selectively malignant cells without altering the function of normal cells. RG260 targets the hTERT G-quadruplex stem-loop folding but not tetrad DNAs, leading to downregulation of hTERT expression. To improve physicochemical and pharmacokinetic properties, we derived a small-molecule analog, RG1603, from the parent compound. RG1603 induces mitochondrial defects including PGC1α and NRF2 inhibition and increases oxidative stress, followed by DNA damage and apoptosis. RG1603 injected as a single agent has tolerable toxicity while achieving strong anticancer efficacy in a tumor xenograft mouse model. These results demonstrate a unique approach to inhibiting the hTERT that functions by impairing mitochondrial activity, inducing cell death.
MeSH term(s)	Animals ; Apoptosis/drug effects ; Cell Death/drug effects ; Cell Line, Tumor ; Cell Proliferation/drug effects ; Dose-Response Relationship, Drug ; G-Quadruplexes/drug effects ; Humans ; Male ; Mice ; Mice, SCID ; Molecular Structure ; Small Molecule Libraries/chemistry ; Small Molecule Libraries/pharmacology ; Structure-Activity Relationship ; Telomerase/antagonists & inhibitors ; Telomerase/metabolism
Chemical Substances	Small Molecule Libraries ; TERT protein, human (EC 2.7.7.49) ; Telomerase (EC 2.7.7.49)
Language	English
Publishing date	2019-05-30
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ISSN	2451-9448
ISSN (online)	2451-9448
DOI	10.1016/j.chembiol.2019.04.009
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Natural biased signaling of hydroxycarboxylic acid receptor 3 and G protein-coupled receptor 84

Anna Peters / Philipp Rabe / Petra Krumbholz / Hermann Kalwa / Robert Kraft / Torsten Schöneberg / Claudia Stäubert

Cell Communication and Signaling, Vol 18, Iss 1, Pp 1-

2020 Volume 19

Abstract: ... endogenously produced in humans, food-derived or originating from bacteria. They activate G protein-coupled ... endogenous, non-pathogenic compounds and compounds originating from e.g. pathogenic bacteria. Video Abstract ...

Abstract	Abstract Background Medium-chain fatty acids and their 3-hydroxy derivatives are metabolites endogenously produced in humans, food-derived or originating from bacteria. They activate G protein-coupled receptors, including GPR84 and HCA3, which regulate metabolism and immune functions. Although both receptors are coupled to Gi proteins, share at least one agonist and show overlapping tissue expression, GPR84 exerts pro-inflammatory effects whereas HCA3 is involved in anti-inflammatory responses. Here, we analyzed signaling kinetics of both HCA3 and GPR84, to unravel signal transduction components that may explain their physiological differences. Methods To study the signaling kinetics and components involved in signal transduction of both receptors we applied the label-free dynamic mass redistribution technology in combination with classical cAMP, ERK signaling and β-arrestin-2 recruitment assays. For phenotypical analyses, we used spheroid cell culture models. Results We present strong evidence for a natural biased signaling of structurally highly similar agonists at HCA3 and GPR84. We show that HCA3 signaling and trafficking depends on dynamin-2 function. Activation of HCA3 by 3-hydroxyoctanoic acid but not 3-hydroxydecanoic acid leads to β-arrestin-2 recruitment, which is relevant for cell-cell adhesion. GPR84 stimulation with 3-hydroxydecanoic acid causes a sustained ERK activation but activation of GPR84 is not followed by β-arrestin-2 recruitment. Conclusions In summary, our results highlight that biased agonism is a physiological property of HCA3 and GPR84 with relevance for innate immune functions potentially to differentiate between endogenous, non-pathogenic compounds and compounds originating from e.g. pathogenic bacteria. Video Abstract. Graphical abstract
Keywords	HCAR ; Hydroxycarboxylic acid receptors ; GPR109b ; GPCR ; HCA3 ; GPR84 ; Medicine ; R ; Cytology ; QH573-671
Subject code	571
Language	English
Publishing date	2020-02-01T00:00:00Z
Publisher	BMC
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: The presumed atypical chemokine receptor CXCR7 signals through G(i/o) proteins in primary rodent astrocytes and human glioma cells.

Odemis, Veysel / Lipfert, Jana / Kraft, Robert / Hajek, Peter / Abraham, Getu / Hattermann, Kirsten / Mentlein, Rolf / Engele, Jürgen

Glia

2011 Volume 60, Issue 3, Page(s) 372–381

Abstract: ... through pertussis toxin-sensitive G(i/o) proteins. SDF-1-dependent activation of G(i/o) proteins and subsequent increases ... bound CXCR7 activates G(i/o) proteins in astrocytes could help to explain some discrepancies previously ...

Abstract	SDF-1/CXCL12 binds to the chemokine receptors, CXCR4 and CXCR7, and controls cell proliferation and migration during development, tumorigenesis, and inflammatory processes. It is currently assumed that CXCR7 would represent an atypical or scavenger chemokine receptor which modulates the function of CXCR4. Contrasting this view, we demonstrated recently that CXCR7 actively mediates SDF-1 signaling in primary astrocytes. Here, we provide evidence that CXCR7 affects astrocytic cell signaling and function through pertussis toxin-sensitive G(i/o) proteins. SDF-1-dependent activation of G(i/o) proteins and subsequent increases in intracellular Ca(2+) concentration persisted in primary rodent astrocytes with depleted expression of CXCR4, but were abolished in astrocytes with depleted expression of CXCR7. Moreover, CXCR7-mediated effects of SDF-1 on Erk and Akt signaling as well as on astrocytic proliferation and migration were all sensitive to pertussis toxin. Likewise, pertussis toxin abolished SDF-1-induced activation of Erk and Akt in CXCR7-only expressing human glioma cell lines. Finally, consistent with a ligand-biased function of CXCR7 in astrocytes, the alternate CXCR7 ligand, I-TAC/CXCL11, activated Erk and Akt through β-arrestin. The demonstration that SDF-1-bound CXCR7 activates G(i/o) proteins in astrocytes could help to explain some discrepancies previously observed for the function of CXCR4 and CXCR7 in other cell types.
MeSH term(s)	Animals ; Animals, Newborn ; Arrestins/metabolism ; Astrocytoma/pathology ; Calcium/metabolism ; Cell Proliferation ; Cells, Cultured ; Cerebral Cortex/cytology ; Chemokine CXCL12/metabolism ; Chemotaxis/drug effects ; Chemotaxis/genetics ; Embryo, Mammalian ; Enzyme Inhibitors/pharmacology ; GTP-Binding Protein alpha Subunits, Gi-Go/metabolism ; Guanosine 5'-O-(3-Thiotriphosphate)/pharmacokinetics ; Humans ; Mice ; Mice, Knockout ; Neuroglia/drug effects ; Neuroglia/metabolism ; RNA Interference/physiology ; Rats ; Rats, Sprague-Dawley ; Receptors, CXCR/genetics ; Receptors, CXCR/metabolism ; Receptors, CXCR4/deficiency ; Signal Transduction/drug effects ; Signal Transduction/physiology ; Sulfur Isotopes/pharmacokinetics ; beta-Arrestins
Chemical Substances	ACKR3 protein, human ; Arrestins ; CXCR4 protein, mouse ; Chemokine CXCL12 ; Cxcl12 protein, mouse ; Enzyme Inhibitors ; Receptors, CXCR ; Receptors, CXCR4 ; Sulfur Isotopes ; beta-Arrestins ; Guanosine 5'-O-(3-Thiotriphosphate) (37589-80-3) ; GTP-Binding Protein alpha Subunits, Gi-Go (EC 3.6.5.1) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2011-11-14
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	639414-0
ISSN	1098-1136 ; 0894-1491
ISSN (online)	1098-1136
ISSN	0894-1491
DOI	10.1002/glia.22271
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