FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2008396525> ?p ?o ?g. }

• W2008396525 endingPage "5799" @default.
• W2008396525 startingPage "5792" @default.
• W2008396525 abstract "Adenosine exerts a mitogenic effect on human endothelial cells via stimulation of the A2A-adenosine receptor. This effect can also be elicited by the β2-adrenergic receptor but is not mimicked by elevation of intracellular cAMP levels. In the present work, we report that stimulation of the A2A-adenosine receptor and of the β2-adrenergic receptor activates mitogen-activated protein kinase (MAP kinase) in human endothelial cells based on the following criteria: adenosine analogues and β-adrenergic agonists cause an (i) increase in tyrosine phosphorylation of the p42 isoform and to a lesser extent of the p44 isoform of MAP kinase and (ii) stimulate the phosphorylation of myelin basic protein by MAP kinase; (iii) this is accompanied by a redistribution of the enzyme to the perinuclear region. Pretreatment of the cells with cholera toxin (to down-regulate Gsα) abolishes activation of MAP kinase by isoproterenol but not that induced by adenosine analogues. In addition, MAP kinase stimulation via the A2A-adenosine receptor is neither impaired following pretreatment of the cells with pertussis toxin (to block Gi-dependent pathways) nor affected by GF109203X (1 μM; to inhibit typical protein kinase C isoforms) nor by a monoclonal antibody, which blocks epidermal growth factor-dependent signaling. In contrast, MAP kinase activation is blocked by PD 098059, an inhibitor of MAP kinase kinase 1 (MEK1) activation, which also blunts the A2A-adenosine receptor-mediated increase in [3H]thymidine incorporation. Activation of the A2A-adenosine receptor is associated with increased levels of GTP-bound p21ras. Thus, our experiments define stimulation of MAP kinase as the candidate cellular target mediating the mitogenic action of the A2A-adenosine receptor on primary human endothelial cells; the signaling pathway operates via p21ras and MEK1 but is independent of Gi, Gs, and the typical protein kinase C isoforms. This implies an additional G protein which links this prototypical Gs-coupled receptor to the MAP kinase cascade. Adenosine exerts a mitogenic effect on human endothelial cells via stimulation of the A2A-adenosine receptor. This effect can also be elicited by the β2-adrenergic receptor but is not mimicked by elevation of intracellular cAMP levels. In the present work, we report that stimulation of the A2A-adenosine receptor and of the β2-adrenergic receptor activates mitogen-activated protein kinase (MAP kinase) in human endothelial cells based on the following criteria: adenosine analogues and β-adrenergic agonists cause an (i) increase in tyrosine phosphorylation of the p42 isoform and to a lesser extent of the p44 isoform of MAP kinase and (ii) stimulate the phosphorylation of myelin basic protein by MAP kinase; (iii) this is accompanied by a redistribution of the enzyme to the perinuclear region. Pretreatment of the cells with cholera toxin (to down-regulate Gsα) abolishes activation of MAP kinase by isoproterenol but not that induced by adenosine analogues. In addition, MAP kinase stimulation via the A2A-adenosine receptor is neither impaired following pretreatment of the cells with pertussis toxin (to block Gi-dependent pathways) nor affected by GF109203X (1 μM; to inhibit typical protein kinase C isoforms) nor by a monoclonal antibody, which blocks epidermal growth factor-dependent signaling. In contrast, MAP kinase activation is blocked by PD 098059, an inhibitor of MAP kinase kinase 1 (MEK1) activation, which also blunts the A2A-adenosine receptor-mediated increase in [3H]thymidine incorporation. Activation of the A2A-adenosine receptor is associated with increased levels of GTP-bound p21ras. Thus, our experiments define stimulation of MAP kinase as the candidate cellular target mediating the mitogenic action of the A2A-adenosine receptor on primary human endothelial cells; the signaling pathway operates via p21ras and MEK1 but is independent of Gi, Gs, and the typical protein kinase C isoforms. This implies an additional G protein which links this prototypical Gs-coupled receptor to the MAP kinase cascade." @default.
• W2008396525 created "2016-06-24" @default.
• W2008396525 creator A5010150886 @default.
• W2008396525 creator A5034547672 @default.
• W2008396525 creator A5050283760 @default.
• W2008396525 creator A5060360807 @default.
• W2008396525 creator A5077764148 @default.
• W2008396525 creator A5079620940 @default.
• W2008396525 date "1997-02-01" @default.
• W2008396525 modified "2023-10-14" @default.
• W2008396525 title "Stimulation of the Mitogen-activated Protein Kinase via the A2A-Adenosine Receptor in Primary Human Endothelial Cells" @default.
• W2008396525 cites W1481591305 @default.
• W2008396525 cites W1509317138 @default.
• W2008396525 cites W1530463005 @default.
• W2008396525 cites W1542412714 @default.
• W2008396525 cites W1547923771 @default.
• W2008396525 cites W1556619518 @default.
• W2008396525 cites W1558848958 @default.
• W2008396525 cites W1560455251 @default.
• W2008396525 cites W1567065545 @default.
• W2008396525 cites W1570736076 @default.
• W2008396525 cites W1571499921 @default.
• W2008396525 cites W1573821584 @default.
• W2008396525 cites W1594412667 @default.
• W2008396525 cites W1608533627 @default.
• W2008396525 cites W1925041868 @default.
• W2008396525 cites W1977929190 @default.
• W2008396525 cites W1979658307 @default.
• W2008396525 cites W1980352092 @default.
• W2008396525 cites W1981493299 @default.
• W2008396525 cites W1992472345 @default.
• W2008396525 cites W1992896836 @default.
• W2008396525 cites W1992965538 @default.
• W2008396525 cites W2028404746 @default.
• W2008396525 cites W2031610264 @default.
• W2008396525 cites W2035936653 @default.
• W2008396525 cites W2036842366 @default.
• W2008396525 cites W2039166377 @default.
• W2008396525 cites W2055171145 @default.
• W2008396525 cites W2059215487 @default.
• W2008396525 cites W2067689884 @default.
• W2008396525 cites W2068502127 @default.
• W2008396525 cites W2075272342 @default.
• W2008396525 cites W2080999736 @default.
• W2008396525 cites W2084839593 @default.
• W2008396525 cites W2086795928 @default.
• W2008396525 cites W2088823687 @default.
• W2008396525 cites W2095774675 @default.
• W2008396525 cites W2108366710 @default.
• W2008396525 cites W2128029362 @default.
• W2008396525 cites W2135189810 @default.
• W2008396525 cites W2150157600 @default.
• W2008396525 cites W2224551723 @default.
• W2008396525 cites W4245635197 @default.
• W2008396525 cites W64852952 @default.
• W2008396525 cites W97473470 @default.
• W2008396525 doi "https://doi.org/10.1074/jbc.272.9.5792" @default.
• W2008396525 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/9038193" @default.
• W2008396525 hasPublicationYear "1997" @default.
• W2008396525 type Work @default.
• W2008396525 sameAs 2008396525 @default.
• W2008396525 citedByCount "182" @default.
• W2008396525 countsByYear W20083965252012 @default.
• W2008396525 countsByYear W20083965252013 @default.
• W2008396525 countsByYear W20083965252014 @default.
• W2008396525 countsByYear W20083965252015 @default.
• W2008396525 countsByYear W20083965252016 @default.
• W2008396525 countsByYear W20083965252017 @default.
• W2008396525 countsByYear W20083965252018 @default.
• W2008396525 countsByYear W20083965252019 @default.
• W2008396525 countsByYear W20083965252021 @default.
• W2008396525 countsByYear W20083965252022 @default.
• W2008396525 crossrefType "journal-article" @default.
• W2008396525 hasAuthorship W2008396525A5010150886 @default.
• W2008396525 hasAuthorship W2008396525A5034547672 @default.
• W2008396525 hasAuthorship W2008396525A5050283760 @default.
• W2008396525 hasAuthorship W2008396525A5060360807 @default.
• W2008396525 hasAuthorship W2008396525A5077764148 @default.
• W2008396525 hasAuthorship W2008396525A5079620940 @default.
• W2008396525 hasBestOaLocation W20083965251 @default.
• W2008396525 hasConcept C124160383 @default.
• W2008396525 hasConcept C134018914 @default.
• W2008396525 hasConcept C137361374 @default.
• W2008396525 hasConcept C138227536 @default.
• W2008396525 hasConcept C158424129 @default.
• W2008396525 hasConcept C159479382 @default.
• W2008396525 hasConcept C16587737 @default.
• W2008396525 hasConcept C170493617 @default.
• W2008396525 hasConcept C184235292 @default.
• W2008396525 hasConcept C185592680 @default.
• W2008396525 hasConcept C2776991684 @default.
• W2008396525 hasConcept C2778938600 @default.
• W2008396525 hasConcept C55493867 @default.
• W2008396525 hasConcept C59143045 @default.
• W2008396525 hasConcept C67907053 @default.
• W2008396525 hasConcept C82495950 @default.
• W2008396525 hasConcept C86803240 @default.
• W2008396525 hasConcept C90934575 @default.

• next