FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2153285246> ?p ?o ?g. }

• W2153285246 abstract "Compartmentation of cAMP signaling been demonstrated to be attributable to the structural association of protein kinase A (PKA) (via association with A-kinase anchoring proteins [AKAPs]) with phosphodiesterase and AKAP-dependent effector molecules. However, other mechanisms contributing to compartmentalization have not been rigorously explored, including the possibility that different isoforms of adenylyl cyclase (AC) may be functionally “compartmentalized” because of differential association with tethering or signaling molecules. To this end, we examined the effect of adenoviral transduction of representative AC isoforms (AC1, AC2, AC5, and AC6) on cellular cAMP production, PKA activation, extracellular signal-regulated kinase (ERK) activation, cell doubling and proliferation, as well as arborization responses (an index of cAMP-mediated cytoskeletal re-organization) in vascular smooth muscle cells. When isoforms were expressed at levels to achieve comparable forskolin-stimulated AC activity, only gene transfer of AC6 significantly enhanced PKA-dependent vasodilator-stimulated phosphoprotein (VASP) phosphorylation and arborization responses. Treatment of control cells, which express AC6 endogenously, as well as vascular smooth overexpressing the AC6 isoform with small interfering RNA directed against AC6, significantly suppressed both isoproterenol-stimulated cAMP accumulation and arborization. Notably, the selective effects of AC6 expression were abrogated in the presence of phosphodiesterase suppression. In contrast, only the expression of AC1 enhanced forskolin-stimulated association of ERK with AC, demonstrated by coimmuno-isolation of ERK with Flag-tagged AC1, but not with Flag-tagged AC6. To determine whether these isoform-selective effects of AC were unique to differentiated and morphologically compartmentalized vascular smooth muscle cells or were a general property of these isoforms, we examined the consequence of expression of these various isoforms in human embryonic kidney (HEK) cells. Indeed, we observed similar isoform-dependent association of AC1 with ERK, activation of ERK by stimulation of AC1 with forskolin, and AC1-dependent lengthening of doubling time, indicating that these properties of AC1 are cell autologous and likely result from AC1-dependent protein-protein interactions. In aggregate, these findings suggest that isoform-selective signaling complexes likely contribute to various functional consequences of cAMP elevation in vascular smooth muscle cells." @default.
• W2153285246 created "2016-06-24" @default.
• W2153285246 creator A5007560814 @default.
• W2153285246 creator A5047131494 @default.
• W2153285246 creator A5072621917 @default.
• W2153285246 creator A5086900416 @default.
• W2153285246 creator A5090719615 @default.
• W2153285246 creator A5091025989 @default.
• W2153285246 date "2006-10-13" @default.
• W2153285246 modified "2023-09-23" @default.
• W2153285246 title "Adenylyl Cyclase Isoform–Selective Regulation of Vascular Smooth Muscle Proliferation and Cytoskeletal Reorganization" @default.
• W2153285246 cites W1530446990 @default.
• W2153285246 cites W1563205636 @default.
• W2153285246 cites W1966430777 @default.
• W2153285246 cites W1969389345 @default.
• W2153285246 cites W1973805487 @default.
• W2153285246 cites W1974537372 @default.
• W2153285246 cites W1982482091 @default.
• W2153285246 cites W2001220477 @default.
• W2153285246 cites W2023396177 @default.
• W2153285246 cites W2027660679 @default.
• W2153285246 cites W2064080294 @default.
• W2153285246 cites W2072543946 @default.
• W2153285246 cites W2073384126 @default.
• W2153285246 cites W2091038080 @default.
• W2153285246 cites W2133553247 @default.
• W2153285246 cites W2143220821 @default.
• W2153285246 cites W2167458726 @default.
• W2153285246 cites W2221292849 @default.
• W2153285246 cites W2498155094 @default.
• W2153285246 doi "https://doi.org/10.1161/01.res.0000245189.21703.c0" @default.
• W2153285246 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/16973907" @default.
• W2153285246 hasPublicationYear "2006" @default.
• W2153285246 type Work @default.
• W2153285246 sameAs 2153285246 @default.
• W2153285246 citedByCount "50" @default.
• W2153285246 countsByYear W21532852462012 @default.
• W2153285246 countsByYear W21532852462013 @default.
• W2153285246 countsByYear W21532852462014 @default.
• W2153285246 countsByYear W21532852462015 @default.
• W2153285246 countsByYear W21532852462016 @default.
• W2153285246 countsByYear W21532852462017 @default.
• W2153285246 countsByYear W21532852462018 @default.
• W2153285246 countsByYear W21532852462019 @default.
• W2153285246 countsByYear W21532852462020 @default.
• W2153285246 countsByYear W21532852462021 @default.
• W2153285246 countsByYear W21532852462022 @default.
• W2153285246 crossrefType "journal-article" @default.
• W2153285246 hasAuthorship W2153285246A5007560814 @default.
• W2153285246 hasAuthorship W2153285246A5047131494 @default.
• W2153285246 hasAuthorship W2153285246A5072621917 @default.
• W2153285246 hasAuthorship W2153285246A5086900416 @default.
• W2153285246 hasAuthorship W2153285246A5090719615 @default.
• W2153285246 hasAuthorship W2153285246A5091025989 @default.
• W2153285246 hasBestOaLocation W21532852461 @default.
• W2153285246 hasConcept C104317684 @default.
• W2153285246 hasConcept C11960822 @default.
• W2153285246 hasConcept C134018914 @default.
• W2153285246 hasConcept C142669718 @default.
• W2153285246 hasConcept C1491633281 @default.
• W2153285246 hasConcept C170493617 @default.
• W2153285246 hasConcept C176303035 @default.
• W2153285246 hasConcept C181199279 @default.
• W2153285246 hasConcept C195794163 @default.
• W2153285246 hasConcept C2779178603 @default.
• W2153285246 hasConcept C2779276759 @default.
• W2153285246 hasConcept C2779395532 @default.
• W2153285246 hasConcept C2992686903 @default.
• W2153285246 hasConcept C53345823 @default.
• W2153285246 hasConcept C55493867 @default.
• W2153285246 hasConcept C57074206 @default.
• W2153285246 hasConcept C62478195 @default.
• W2153285246 hasConcept C62826618 @default.
• W2153285246 hasConcept C86803240 @default.
• W2153285246 hasConcept C95444343 @default.
• W2153285246 hasConcept C97029542 @default.
• W2153285246 hasConceptScore W2153285246C104317684 @default.
• W2153285246 hasConceptScore W2153285246C11960822 @default.
• W2153285246 hasConceptScore W2153285246C134018914 @default.
• W2153285246 hasConceptScore W2153285246C142669718 @default.
• W2153285246 hasConceptScore W2153285246C1491633281 @default.
• W2153285246 hasConceptScore W2153285246C170493617 @default.
• W2153285246 hasConceptScore W2153285246C176303035 @default.
• W2153285246 hasConceptScore W2153285246C181199279 @default.
• W2153285246 hasConceptScore W2153285246C195794163 @default.
• W2153285246 hasConceptScore W2153285246C2779178603 @default.
• W2153285246 hasConceptScore W2153285246C2779276759 @default.
• W2153285246 hasConceptScore W2153285246C2779395532 @default.
• W2153285246 hasConceptScore W2153285246C2992686903 @default.
• W2153285246 hasConceptScore W2153285246C53345823 @default.
• W2153285246 hasConceptScore W2153285246C55493867 @default.
• W2153285246 hasConceptScore W2153285246C57074206 @default.
• W2153285246 hasConceptScore W2153285246C62478195 @default.
• W2153285246 hasConceptScore W2153285246C62826618 @default.
• W2153285246 hasConceptScore W2153285246C86803240 @default.
• W2153285246 hasConceptScore W2153285246C95444343 @default.
• W2153285246 hasConceptScore W2153285246C97029542 @default.
• W2153285246 hasLocation W21532852461 @default.
• W2153285246 hasLocation W21532852462 @default.
• W2153285246 hasOpenAccess W2153285246 @default.

• next