Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1997-5-5
pubmed:abstractText
Incubation of cultured bovine vascular smooth muscle cells (VSMC) with forskolin increased cAMP as measured by an increase in cAMP-dependent protein kinase (PKA) activation (PKA ratio). Forskolin also produced a concentration- and time-dependent increase in activity (3-5-fold within 15 min) of a PDE4 (cAMP-specific cyclic nucleotide phosphodiesterase). The increase in PDE4 activity was not affected by cycloheximide and thus not likely due to increased synthesis of the enzyme. Activation, which was preserved during partial purification of the enzyme by chromatography on Sephacryl S-200 and MonoQ, was most likely due to a covalent modification. Incubation of cell homogenates with the catalytic subunit of PKA (PKA(c)) induced a approximately 5-fold activation of PDE4 with a time course similar to that in intact cells after forskolin addition. The forskolin-mediated activation was reversed during incubation of homogenates at room temperature for two hours. Addition of PKA(c) resulted in rapid reactivation of PDE4. These data are consistent with the hypothesis that rapid, reversible activation of PDE4 in cultured VSMC is mediated by PKA.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
1356
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
64-70
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Protein kinase A-dependent activation of PDE4 (cAMP-specific cyclic nucleotide phosphodiesterase) in cultured bovine vascular smooth muscle cells.
pubmed:affiliation
Department of Cell and Molecular Biology, Lund University, Sweden.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't