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Article ; Online: Insulin Keeps PYK-ing on eNOS: Enhanced Insulin Receptor Signaling Induces Endothelial Dysfunction.

Siragusa, Mauro / Fisslthaler, Beate

2017 Volume 120, Issue 5, Page(s) 748–750

MeSH term(s)	Endothelium ; Humans ; Insulin ; Insulin Resistance ; Nitric Oxide Synthase Type III ; Receptor, Insulin ; Signal Transduction
Chemical Substances	Insulin ; Nitric Oxide Synthase Type III (EC 1.14.13.39) ; Receptor, Insulin (EC 2.7.10.1)
Language	English
Publishing date	2017-03-02
Publishing country	United States
Document type	Editorial ; Research Support, Non-U.S. Gov't ; Comment
ZDB-ID	80100-8
ISSN	1524-4571 ; 0009-7330 ; 0931-6876
ISSN (online)	1524-4571
ISSN	0009-7330 ; 0931-6876
DOI	10.1161/CIRCRESAHA.117.310576
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Article ; Online: Effect of Thrombin on the Metabolism and Function of Murine Macrophages.

Ukan, Ürün / Delgado Lagos, Fredy / Kempf, Sebastian / Günther, Stefan / Siragusa, Mauro / Fisslthaler, Beate / Fleming, Ingrid

Cells

2022 Volume 11, Issue 10

Abstract: Macrophages are plastic and heterogeneous immune cells that adapt pro- or anti-inflammatory phenotypes upon exposure to different stimuli. Even though there has been evidence supporting a crosstalk between coagulation and innate immunity, the way in ... ...

Abstract	Macrophages are plastic and heterogeneous immune cells that adapt pro- or anti-inflammatory phenotypes upon exposure to different stimuli. Even though there has been evidence supporting a crosstalk between coagulation and innate immunity, the way in which protein components of the hemostasis pathway influence macrophages remains unclear. We investigated the effect of thrombin on macrophage polarization. On the basis of gene expression and cytokine secretion, our results suggest that polarization with thrombin induces an anti-inflammatory, M2-like phenotype. In functional studies, thrombin polarization promoted oxLDL phagocytosis by macrophages, and conditioned medium from the same cells increased endothelial cell proliferation. There were, however, clear differences between the classical M2a polarization and the effects of thrombin on gene expression. Finally, the deletion and inactivation of secreted modular Ca
MeSH term(s)	Animals ; Anti-Inflammatory Agents/metabolism ; Macrophage Activation ; Macrophages/metabolism ; Mice ; Phagocytosis ; Thrombin/pharmacology
Chemical Substances	Anti-Inflammatory Agents ; Thrombin (EC 3.4.21.5)
Language	English
Publishing date	2022-05-23
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2661518-6
ISSN	2073-4409 ; 2073-4409
ISSN (online)	2073-4409
ISSN	2073-4409
DOI	10.3390/cells11101718
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Article ; Online: Effect of Thrombin on the Metabolism and Function of Murine Macrophages

Ürün Ukan / Fredy Delgado Lagos / Sebastian Kempf / Stefan Günther / Mauro Siragusa / Beate Fisslthaler / Ingrid Fleming

Cells, Vol 11, Iss 1718, p

2022 Volume 1718

Abstract	Macrophages are plastic and heterogeneous immune cells that adapt pro- or anti-inflammatory phenotypes upon exposure to different stimuli. Even though there has been evidence supporting a crosstalk between coagulation and innate immunity, the way in which protein components of the hemostasis pathway influence macrophages remains unclear. We investigated the effect of thrombin on macrophage polarization. On the basis of gene expression and cytokine secretion, our results suggest that polarization with thrombin induces an anti-inflammatory, M2-like phenotype. In functional studies, thrombin polarization promoted oxLDL phagocytosis by macrophages, and conditioned medium from the same cells increased endothelial cell proliferation. There were, however, clear differences between the classical M2a polarization and the effects of thrombin on gene expression. Finally, the deletion and inactivation of secreted modular Ca 2+ -binding protein 1 (SMOC1) attenuated phagocytosis by thrombin-stimulated macrophages, a phenomenon revered by the addition of recombinant SMOC1. Manipulation of SMOC1 levels also had a pronounced impact on the expression of TGF-β-signaling-related genes. Taken together, our results show that thrombin induces an anti-inflammatory macrophage phenotype with similarities as well as differences to the classical alternatively activated M2 polarization states, highlighting the importance of tissue levels of SMOC1 in modifying thrombin-induced macrophage polarization.
Keywords	SMOC1 ; macrophage polarization ; thrombin ; Biology (General) ; QH301-705.5
Subject code	616
Language	English
Publishing date	2022-05-01T00:00:00Z
Publisher	MDPI AG
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Endothelial AMP-Activated Kinase α1 Phosphorylates eNOS on Thr495 and Decreases Endothelial NO Formation.

Zippel, Nina / Loot, Annemarieke E / Stingl, Heike / Randriamboavonjy, Voahanginirina / Fleming, Ingrid / Fisslthaler, Beate

International journal of molecular sciences

2018 Volume 19, Issue 9

Abstract: AMP-activated protein kinase (AMPK) is frequently reported to phosphorylate Ser1177 of the endothelial nitric-oxide synthase (eNOS), and therefore, is linked with a relaxing effect. However, previous studies failed to consistently demonstrate a major ... ...

Abstract	AMP-activated protein kinase (AMPK) is frequently reported to phosphorylate Ser1177 of the endothelial nitric-oxide synthase (eNOS), and therefore, is linked with a relaxing effect. However, previous studies failed to consistently demonstrate a major role for AMPK on eNOS-dependent relaxation. As AMPK also phosphorylates eNOS on the inhibitory Thr495 site, this study aimed to determine the role of AMPKα1 and α2 subunits in the regulation of NO-mediated vascular relaxation. Vascular reactivity to phenylephrine and acetylcholine was assessed in aortic and carotid artery segments from mice with global (AMPKα
MeSH term(s)	AMP-Activated Protein Kinases/genetics ; AMP-Activated Protein Kinases/metabolism ; Animals ; Endothelial Cells/metabolism ; Humans ; Mice ; Mice, Knockout ; Nitric Oxide/metabolism ; Nitric Oxide Synthase Type III/metabolism ; Phenylephrine/metabolism ; Phosphorylation ; Vasoconstriction/genetics ; Vasoconstriction/physiology
Chemical Substances	Phenylephrine (1WS297W6MV) ; Nitric Oxide (31C4KY9ESH) ; Nitric Oxide Synthase Type III (EC 1.14.13.39) ; AMP-Activated Protein Kinases (EC 2.7.11.31)
Language	English
Publishing date	2018-09-13
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms19092753
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Cyp2c44 epoxygenase-derived epoxyeicosatrienoic acids in vascular smooth muscle cells elicit vasoconstriction of the murine ophthalmic artery.

Hu, Jiong / Sisignano, Marco / Brecht, Roman / Perumal, Natarajan / Angioni, Carlo / Bibli, Iris-Sofia / Fisslthaler, Beate / Kleinert, Hartmut / Pfeiffer, Norbert / Fleming, Ingrid / Manicam, Caroline

Scientific reports

2021 Volume 11, Issue 1, Page(s) 18764

Abstract: Cytochrome P450 (CYP) signalling pathway has been shown to play a vital role in the vasoreactivity of wild type mouse ophthalmic artery. In this study, we determined the expression, vascular responses and potential mechanisms of the CYP-derived ... ...

Abstract	Cytochrome P450 (CYP) signalling pathway has been shown to play a vital role in the vasoreactivity of wild type mouse ophthalmic artery. In this study, we determined the expression, vascular responses and potential mechanisms of the CYP-derived arachidonic acid metabolites. The expression of murine CYP (Cyp2c44) and soluble epoxide hydrolase (sEH) in the wild type ophthalmic artery was determined with immunofluorescence, which showed predominant expression of Cyp2c44 in the vascular smooth muscle cells (VSMC), while sEH was found mainly in the endothelium of the wild type ophthalmic artery. Artery of Cyp2c44
MeSH term(s)	Animals ; Cytochrome P450 Family 2/chemistry ; Cytochrome P450 Family 2/metabolism ; Epoxide Hydrolases/metabolism ; Fatty Acids, Monounsaturated/chemistry ; Fatty Acids, Monounsaturated/pharmacology ; Mice ; Ophthalmic Artery/drug effects ; Ophthalmic Artery/enzymology ; Ophthalmic Artery/physiology ; Vasoconstriction/drug effects
Chemical Substances	Fatty Acids, Monounsaturated ; Cyp2c23 protein, mouse (EC 1.14.14.1) ; Cytochrome P450 Family 2 (EC 1.14.14.1) ; Epoxide Hydrolases (EC 3.3.2.-) ; Ephx2 protein, mouse (EC 3.3.2.10) ; eicosenoic acid (UDX6WPL94T)
Language	English
Publishing date	2021-09-21
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-021-98236-w
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Article ; Online: Secreted modular calcium-binding protein 1 binds and activates thrombin to account for platelet hyperreactivity in diabetes.

Delgado Lagos, Fredy / Elgheznawy, Amro / Kyselova, Anastasia / Meyer Zu Heringdorf, Dagmar / Ratiu, Corina / Randriamboavonjy, Voahanginirina / Mann, Alexander W / Fisslthaler, Beate / Siragusa, Mauro / Fleming, Ingrid

Blood

2021 Volume 137, Issue 12, Page(s) 1641–1651

Abstract: Secreted modular calcium-binding protein 1 (SMOC1) is an osteonectin/SPARC-related matricellular protein, whose expression is regulated by microRNA-223 (miR-223). Given that platelets are rich in miR-223, this study investigated the expression of SMOC1 ... ...

Abstract	Secreted modular calcium-binding protein 1 (SMOC1) is an osteonectin/SPARC-related matricellular protein, whose expression is regulated by microRNA-223 (miR-223). Given that platelets are rich in miR-223, this study investigated the expression of SMOC1 and its contribution to platelet function. Human and murine platelets expressed SMOC1, whereas platelets from SMOC1+/- mice did not present detectable mature SMOC1 protein. Platelets from SMOC1+/- mice demonstrated attenuated responsiveness to thrombin (platelet neutrophil aggregate formation, aggregation, clot formation, Ca2+ increase, and β3 integrin phosphorylation), whereas responses to other platelet agonists were unaffected. SMOC1 has been implicated in transforming growth factor-β signaling, but no link to this pathway was detected in platelets. Rather, the SMOC1 Kazal domain directly bound thrombin to potentiate its activity in vitro, as well as its actions on isolated platelets. The latter effects were prevented by monoclonal antibodies against SMOC1. Platelets from miR-223-deficient mice expressed high levels of SMOC1 and exhibited hyperreactivity to thrombin that was also reversed by preincubation with monoclonal antibodies against SMOC1. Similarly, SMOC1 levels were markedly upregulated in platelets from individuals with type 2 diabetes, and the SMOC1 antibody abrogated platelet hyperresponsiveness to thrombin. Taken together, we have identified SMOC1 as a novel thrombin-activating protein that makes a significant contribution to the pathophysiological changes in platelet function associated with type 2 diabetes. Thus, strategies that target SMOC1 or its interaction with thrombin may be attractive therapeutic approaches to normalize platelet function in diabetes.
MeSH term(s)	Adult ; Animals ; Blood Platelets/cytology ; Blood Platelets/metabolism ; Diabetes Mellitus, Type 2/metabolism ; Female ; Humans ; Male ; Mice ; Mice, Inbred C57BL ; Middle Aged ; Osteonectin/metabolism ; Platelet Activation ; Platelet Aggregation ; Thrombin/metabolism
Chemical Substances	Osteonectin ; SMOC-1 protein, mouse ; SMOC1 protein, human ; Thrombin (EC 3.4.21.5)
Language	English
Publishing date	2021-02-02
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80069-7
ISSN	1528-0020 ; 0006-4971
ISSN (online)	1528-0020
ISSN	0006-4971
DOI	10.1182/blood.2020009405
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Article ; Online: Endothelial AMP-Activated Kinase α1 Phosphorylates eNOS on Thr495 and Decreases Endothelial NO Formation

Nina Zippel / Annemarieke E. Loot / Heike Stingl / Voahanginirina Randriamboavonjy / Ingrid Fleming / Beate Fisslthaler

International Journal of Molecular Sciences, Vol 19, Iss 9, p

2018 Volume 2753

Abstract	AMP-activated protein kinase (AMPK) is frequently reported to phosphorylate Ser1177 of the endothelial nitric-oxide synthase (eNOS), and therefore, is linked with a relaxing effect. However, previous studies failed to consistently demonstrate a major role for AMPK on eNOS-dependent relaxation. As AMPK also phosphorylates eNOS on the inhibitory Thr495 site, this study aimed to determine the role of AMPKα1 and α2 subunits in the regulation of NO-mediated vascular relaxation. Vascular reactivity to phenylephrine and acetylcholine was assessed in aortic and carotid artery segments from mice with global (AMPKα−/−) or endothelial-specific deletion (AMPKαΔEC) of the AMPKα subunits. In control and AMPKα1-depleted human umbilical vein endothelial cells, eNOS phosphorylation on Ser1177 and Thr495 was assessed after AMPK activation with thiopental or ionomycin. Global deletion of the AMPKα1 or α2 subunit in mice did not affect vascular reactivity. The endothelial-specific deletion of the AMPKα1 subunit attenuated phenylephrine-mediated contraction in an eNOS- and endothelium-dependent manner. In in vitro studies, activation of AMPK did not alter the phosphorylation of eNOS on Ser1177, but increased its phosphorylation on Thr495. Depletion of AMPKα1 in cultured human endothelial cells decreased Thr495 phosphorylation without affecting Ser1177 phosphorylation. The results of this study indicate that AMPKα1 targets the inhibitory phosphorylation Thr495 site in the calmodulin-binding domain of eNOS to attenuate basal NO production and phenylephrine-induced vasoconstriction.
Keywords	endothelial nitric-oxide synthase ; vasodilation ; phenylephrine ; vasoconstriction ; endothelial cells ; ionomycin ; Biology (General) ; QH301-705.5 ; Chemistry ; QD1-999
Subject code	570
Language	English
Publishing date	2018-09-01T00:00:00Z
Publisher	MDPI AG
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Activation and signaling by the AMP-activated protein kinase in endothelial cells.

Fisslthaler, Beate / Fleming, Ingrid

Circulation research

2009 Volume 105, Issue 2, Page(s) 114–127

Abstract: The AMP-activated protein kinase (AMPK) was initially identified as the kinase that phosphorylates the 3-hydroxy 3-methylglutaryl coenzyme A reductase, the rate-limiting enzyme for cholesterol biosynthesis. As the name suggests, the AMPK is activated by ... ...

Abstract	The AMP-activated protein kinase (AMPK) was initially identified as the kinase that phosphorylates the 3-hydroxy 3-methylglutaryl coenzyme A reductase, the rate-limiting enzyme for cholesterol biosynthesis. As the name suggests, the AMPK is activated by increased intracellular concentrations of AMP, and is generally described as a "metabolite-sensing kinase" and when activated initiates steps to conserve cellular energy. Although there is a strong link between the activity of the AMPK and metabolic control in muscle cells, the activity of the AMPK in endothelial cells can be regulated by stimuli that affect cellular ATP levels, such as hypoxia as well as by fluid shear stress, Ca(2+)-elevating agonists, and hormones such as adiponectin. To date the AMPK in endothelial cells has been implicated in the regulation of fatty acid oxidation, small G protein activity and nitric oxide production as well as inflammation and angiogenesis. Moreover, there is evidence indicating that the activation of the AMPK may help to prevent the vascular complications associated with the metabolic syndrome.
MeSH term(s)	AMP-Activated Protein Kinases/antagonists & inhibitors ; AMP-Activated Protein Kinases/metabolism ; Animals ; Cardiovascular Diseases/drug therapy ; Cardiovascular Diseases/enzymology ; Endothelial Cells/drug effects ; Endothelial Cells/enzymology ; Energy Metabolism ; Enzyme Activation ; Enzyme Activators/pharmacology ; Gene Expression Regulation ; Homeostasis ; Humans ; Isoenzymes ; NADPH Oxidases/metabolism ; Nitric Oxide Synthase Type III/metabolism ; Oxidation-Reduction ; Phosphorylation ; Protein Kinase Inhibitors/pharmacology ; Proto-Oncogene Proteins c-akt/metabolism ; Signal Transduction/drug effects
Chemical Substances	Enzyme Activators ; Isoenzymes ; Protein Kinase Inhibitors ; Nitric Oxide Synthase Type III (EC 1.14.13.39) ; NADPH Oxidases (EC 1.6.3.-) ; Proto-Oncogene Proteins c-akt (EC 2.7.11.1) ; AMP-Activated Protein Kinases (EC 2.7.11.31)
Language	English
Publishing date	2009-07-17
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	80100-8
ISSN	1524-4571 ; 0009-7330 ; 0931-6876
ISSN (online)	1524-4571
ISSN	0009-7330 ; 0931-6876
DOI	10.1161/CIRCRESAHA.109.201590
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Article ; Online: NFAT5/TonEBP Limits Pulmonary Vascular Resistance in the Hypoxic Lung by Controlling Mitochondrial Reactive Oxygen Species Generation in Arterial Smooth Muscle Cells.

Laban, Hebatullah / Siegmund, Sophia / Zappe, Maren / Trogisch, Felix A / Heineke, Jörg / Torre, Carolina De La / Fisslthaler, Beate / Arnold, Caroline / Lauryn, Jonathan / Büttner, Michael / Mogler, Carolin / Kato, Katsuhiro / Adams, Ralf H / Kuk, Hanna / Fischer, Andreas / Hecker, Markus / Kuebler, Wolfgang M / Korff, Thomas

Cells

2021 Volume 10, Issue 12

Abstract: Chronic hypoxia increases the resistance of pulmonary arteries by stimulating their contraction and augmenting their coverage by smooth muscle cells (SMCs). While these responses require adjustment of the vascular SMC transcriptome, regulatory elements ... ...

Abstract	Chronic hypoxia increases the resistance of pulmonary arteries by stimulating their contraction and augmenting their coverage by smooth muscle cells (SMCs). While these responses require adjustment of the vascular SMC transcriptome, regulatory elements are not well defined in this context. Here, we explored the functional role of the transcription factor nuclear factor of activated T-cells 5 (NFAT5/TonEBP) in the hypoxic lung. Regulatory functions of NFAT5 were investigated in cultured artery SMCs and lungs from control (
MeSH term(s)	Animals ; Blood Pressure ; Electrocardiography ; Gene Expression Regulation ; Heart Ventricles/diagnostic imaging ; Heart Ventricles/physiopathology ; Hypoxia/pathology ; Lung/pathology ; Metabolome ; Mice ; Mitochondria/metabolism ; Myocytes, Smooth Muscle/metabolism ; Myocytes, Smooth Muscle/pathology ; Oxidative Phosphorylation ; Oxygen Consumption ; Protein Transport ; Pulmonary Artery/pathology ; Reactive Oxygen Species/metabolism ; Systole ; Transcription Factors/deficiency ; Transcription Factors/metabolism ; Vascular Resistance/genetics
Chemical Substances	Nfat5 protein, mouse ; Reactive Oxygen Species ; Transcription Factors
Language	English
Publishing date	2021-11-24
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2661518-6
ISSN	2073-4409 ; 2073-4409
ISSN (online)	2073-4409
ISSN	2073-4409
DOI	10.3390/cells10123293
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Article ; Online: Cyp2c44 epoxygenase-derived epoxyeicosatrienoic acids in vascular smooth muscle cells elicit vasoconstriction of the murine ophthalmic artery

Jiong Hu / Marco Sisignano / Roman Brecht / Natarajan Perumal / Carlo Angioni / Iris-Sofia Bibli / Beate Fisslthaler / Hartmut Kleinert / Norbert Pfeiffer / Ingrid Fleming / Caroline Manicam

Scientific Reports, Vol 11, Iss 1, Pp 1-

2021 Volume 14

Abstract: Abstract Cytochrome P450 (CYP) signalling pathway has been shown to play a vital role in the vasoreactivity of wild type mouse ophthalmic artery. In this study, we determined the expression, vascular responses and potential mechanisms of the CYP-derived ... ...

Abstract	Abstract Cytochrome P450 (CYP) signalling pathway has been shown to play a vital role in the vasoreactivity of wild type mouse ophthalmic artery. In this study, we determined the expression, vascular responses and potential mechanisms of the CYP-derived arachidonic acid metabolites. The expression of murine CYP (Cyp2c44) and soluble epoxide hydrolase (sEH) in the wild type ophthalmic artery was determined with immunofluorescence, which showed predominant expression of Cyp2c44 in the vascular smooth muscle cells (VSMC), while sEH was found mainly in the endothelium of the wild type ophthalmic artery. Artery of Cyp2c44−/− and sEH−/− mice were used as negative controls. Targeted mass spectrometry-based lipidomics analysis of endogenous epoxide and diols of the wild type artery detected only 14, 15-EET. Vasorelaxant responses of isolated vessels in response to selective pharmacological blockers and agonist were analysed ex vivo. Direct antagonism of epoxyeicosatrienoic acids (EETs) with a selective inhibitor caused partial vasodilation, suggesting that EETs may behave as vasoconstrictors. Exogenous administration of synthetic EET regioisomers significantly constricted the vessels in a concentration-dependent manner, with the strongest responses elicited by 11, 12- and 14, 15-EETs. Our results provide the first experimental evidence that Cyp2c44-derived EETs in the VSMC mediate vasoconstriction of the ophthalmic artery.
Keywords	Medicine ; R ; Science ; Q
Subject code	610
Language	English
Publishing date	2021-09-01T00:00:00Z
Publisher	Nature Portfolio
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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