FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2078693672> ?p ?o ?g. }

• W2078693672 endingPage "19508" @default.
• W2078693672 startingPage "19503" @default.
• W2078693672 abstract "In LTK− cells stably transfected with rat D1A receptor cDNA, fenoldopam, a D1 agonist, increased phosphatidylinositol 4,5-bisphosphate hydrolysis in a time-dependent manner. In the cytosol, phospholipase C (PLC) activity increased (50 ± 7%) in 30 s, returned to basal level at 4 h, and decreased below basal values by 24 h; in the membrane, PLC activity also increased (36 ± 13%) in 30 s, returned to basal level at 10 min, and decreased below basal value at 4 and 24 h. Fenoldopam also increased PLC-γ protein in a time-dependent manner. The latter was blocked by the D1 antagonist SKF83742 and by a D1A antisense oligodeoxynucleotide, indicating involvement of the D1A receptor. The fenoldopam-induced increase in PLC-γ and activity was mediated by protein kinase A (PKA) since it was blocked by the PKA antagonist Rp-8-CTP-adenosine cyclic 3′:5′-monophosphorothioate (Rp-8-CTP-cAMP-S) and mimicked by direct stimulation of adenylyl cyclase with forskolin or by a PKA agonist, Sp-cAMP-S. Protein kinase C (PKC) was also involved, since the fenoldopam-induced increase in PLC-γ protein was blocked by two different PKC inhibitors, calphostin C and chelerythrine; calphostin C also blocked the fenoldopam-induced increase in PLC activity. In addition, forskolin and a PKA agonist, Sp-8-CTP-cAMP-S, increased PKC activity, and direct stimulation of PKC with phorbol 12-myristate 13-acetate increased PLC-γ protein and activity, effects that were blocked by calphostin C. We suggest that the D1A-mediated stimulation of PLC occurs as a result of PKA activation. PKA then stimulates PLC-γ in cytosol and membrane via activation of PKC. In LTK− cells stably transfected with rat D1A receptor cDNA, fenoldopam, a D1 agonist, increased phosphatidylinositol 4,5-bisphosphate hydrolysis in a time-dependent manner. In the cytosol, phospholipase C (PLC) activity increased (50 ± 7%) in 30 s, returned to basal level at 4 h, and decreased below basal values by 24 h; in the membrane, PLC activity also increased (36 ± 13%) in 30 s, returned to basal level at 10 min, and decreased below basal value at 4 and 24 h. Fenoldopam also increased PLC-γ protein in a time-dependent manner. The latter was blocked by the D1 antagonist SKF83742 and by a D1A antisense oligodeoxynucleotide, indicating involvement of the D1A receptor. The fenoldopam-induced increase in PLC-γ and activity was mediated by protein kinase A (PKA) since it was blocked by the PKA antagonist Rp-8-CTP-adenosine cyclic 3′:5′-monophosphorothioate (Rp-8-CTP-cAMP-S) and mimicked by direct stimulation of adenylyl cyclase with forskolin or by a PKA agonist, Sp-cAMP-S. Protein kinase C (PKC) was also involved, since the fenoldopam-induced increase in PLC-γ protein was blocked by two different PKC inhibitors, calphostin C and chelerythrine; calphostin C also blocked the fenoldopam-induced increase in PLC activity. In addition, forskolin and a PKA agonist, Sp-8-CTP-cAMP-S, increased PKC activity, and direct stimulation of PKC with phorbol 12-myristate 13-acetate increased PLC-γ protein and activity, effects that were blocked by calphostin C. We suggest that the D1A-mediated stimulation of PLC occurs as a result of PKA activation. PKA then stimulates PLC-γ in cytosol and membrane via activation of PKC." @default.
• W2078693672 created "2016-06-24" @default.
• W2078693672 creator A5057651031 @default.
• W2078693672 creator A5062110120 @default.
• W2078693672 creator A5067384035 @default.
• W2078693672 creator A5075088009 @default.
• W2078693672 creator A5082424410 @default.
• W2078693672 creator A5084875771 @default.
• W2078693672 date "1996-08-01" @default.
• W2078693672 modified "2023-10-15" @default.
• W2078693672 title "Dopamine D1A Receptor Regulation of Phospholipase C Isoform" @default.
• W2078693672 cites W1493688737 @default.
• W2078693672 cites W1502124600 @default.
• W2078693672 cites W1504432233 @default.
• W2078693672 cites W1504737180 @default.
• W2078693672 cites W1509189642 @default.
• W2078693672 cites W1518153787 @default.
• W2078693672 cites W1532123823 @default.
• W2078693672 cites W1541533178 @default.
• W2078693672 cites W1546511617 @default.
• W2078693672 cites W1554714271 @default.
• W2078693672 cites W1565496454 @default.
• W2078693672 cites W1580174349 @default.
• W2078693672 cites W1593673222 @default.
• W2078693672 cites W1609084115 @default.
• W2078693672 cites W1669965315 @default.
• W2078693672 cites W1967385667 @default.
• W2078693672 cites W1970843048 @default.
• W2078693672 cites W1973715749 @default.
• W2078693672 cites W1980166477 @default.
• W2078693672 cites W1994518490 @default.
• W2078693672 cites W2004956333 @default.
• W2078693672 cites W2008612581 @default.
• W2078693672 cites W2009578696 @default.
• W2078693672 cites W2010669453 @default.
• W2078693672 cites W2017100096 @default.
• W2078693672 cites W2022151784 @default.
• W2078693672 cites W2024669394 @default.
• W2078693672 cites W2027177269 @default.
• W2078693672 cites W2029704856 @default.
• W2078693672 cites W2034853255 @default.
• W2078693672 cites W2043001547 @default.
• W2078693672 cites W2085623494 @default.
• W2078693672 cites W2087688448 @default.
• W2078693672 cites W2095782370 @default.
• W2078693672 cites W2102541501 @default.
• W2078693672 cites W2130726286 @default.
• W2078693672 cites W2157091785 @default.
• W2078693672 cites W4231195547 @default.
• W2078693672 cites W4248350370 @default.
• W2078693672 doi "https://doi.org/10.1074/jbc.271.32.19503" @default.
• W2078693672 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/8702641" @default.
• W2078693672 hasPublicationYear "1996" @default.
• W2078693672 type Work @default.
• W2078693672 sameAs 2078693672 @default.
• W2078693672 citedByCount "62" @default.
• W2078693672 countsByYear W20786936722012 @default.
• W2078693672 countsByYear W20786936722013 @default.
• W2078693672 countsByYear W20786936722014 @default.
• W2078693672 countsByYear W20786936722015 @default.
• W2078693672 countsByYear W20786936722017 @default.
• W2078693672 countsByYear W20786936722018 @default.
• W2078693672 countsByYear W20786936722019 @default.
• W2078693672 crossrefType "journal-article" @default.
• W2078693672 hasAuthorship W2078693672A5057651031 @default.
• W2078693672 hasAuthorship W2078693672A5062110120 @default.
• W2078693672 hasAuthorship W2078693672A5067384035 @default.
• W2078693672 hasAuthorship W2078693672A5075088009 @default.
• W2078693672 hasAuthorship W2078693672A5082424410 @default.
• W2078693672 hasAuthorship W2078693672A5084875771 @default.
• W2078693672 hasBestOaLocation W20786936721 @default.
• W2078693672 hasConcept C11960822 @default.
• W2078693672 hasConcept C126322002 @default.
• W2078693672 hasConcept C134018914 @default.
• W2078693672 hasConcept C170493617 @default.
• W2078693672 hasConcept C185592680 @default.
• W2078693672 hasConcept C195794163 @default.
• W2078693672 hasConcept C24998067 @default.
• W2078693672 hasConcept C2776108454 @default.
• W2078693672 hasConcept C2778597717 @default.
• W2078693672 hasConcept C2778938600 @default.
• W2078693672 hasConcept C2779178603 @default.
• W2078693672 hasConcept C2779276759 @default.
• W2078693672 hasConcept C2779867896 @default.
• W2078693672 hasConcept C2780245509 @default.
• W2078693672 hasConcept C2781168148 @default.
• W2078693672 hasConcept C55493867 @default.
• W2078693672 hasConcept C62478195 @default.
• W2078693672 hasConcept C71924100 @default.
• W2078693672 hasConcept C86803240 @default.
• W2078693672 hasConcept C97029542 @default.
• W2078693672 hasConceptScore W2078693672C11960822 @default.
• W2078693672 hasConceptScore W2078693672C126322002 @default.
• W2078693672 hasConceptScore W2078693672C134018914 @default.
• W2078693672 hasConceptScore W2078693672C170493617 @default.
• W2078693672 hasConceptScore W2078693672C185592680 @default.
• W2078693672 hasConceptScore W2078693672C195794163 @default.
• W2078693672 hasConceptScore W2078693672C24998067 @default.

• next