Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1987-9-25
pubmed:abstractText
The intact rat adipocyte was used to investigate the possibility of common intermediates in the insulin stimulation of cyclic AMP phosphodiesterase and the beta-adrenergic/adenosine regulation of adenylate cyclase. A five minute incubation of the isolated adipocytes with insulin produced a 50-100% increase in the phosphodiesterase activity found in the particulate fraction of homogenates. The insulin stimulation was not impaired by the presence of either agonist or antagonists of the inhibitory adenosine receptor which acts on adenylate cyclase. Phosphodiesterase activation by insulin was also observable above the level of stimulation produced by the beta-adrenergic agent isoproterenol and forskolin. The validity of the enzyme activity measurements was supported by measurements of the hormonal actions on cyclic AMP levels within the cells. Possible crossover between the adenylate cyclase and phosphodiesterase regulation systems at a post-receptor site was investigated using adipocytes exposed to bacterial toxins specific for the modification of guanine nucleotide binding proteins. Both cholera toxin, which irreversibly activates Gs and pertussis toxin which inactivates Gi caused some stimulation of the phosphodiesterase activity and suppressed activation by isoproterenol, but neither toxin prevented the insulin stimulation of cyclic AMP phosphodiesterase. These results suggest, while common components may participate in the beta-adrenergic stimulation of both adenylate cyclase and phosphodiesterase, the mechanism of insulin activation of the phosphodiesterase does not involve the components of adenylate cyclase regulation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/3',5'-Cyclic-AMP Phosphodiesterases, http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Deaminase, http://linkedlifedata.com/resource/pubmed/chemical/Adenylate Cyclase, http://linkedlifedata.com/resource/pubmed/chemical/Adenylate Cyclase Toxin, http://linkedlifedata.com/resource/pubmed/chemical/Cholera Toxin, http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP, http://linkedlifedata.com/resource/pubmed/chemical/Forskolin, http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Insulin, http://linkedlifedata.com/resource/pubmed/chemical/Isoproterenol, http://linkedlifedata.com/resource/pubmed/chemical/Pertussis Toxin, http://linkedlifedata.com/resource/pubmed/chemical/Phenylisopropyladenosine, http://linkedlifedata.com/resource/pubmed/chemical/Virulence Factors, Bordetella
pubmed:status
MEDLINE
pubmed:issn
0746-3898
pubmed:author
pubmed:issnType
Print
pubmed:volume
11
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
345-54
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:3040818-3',5'-Cyclic-AMP Phosphodiesterases, pubmed-meshheading:3040818-Adenosine Deaminase, pubmed-meshheading:3040818-Adenylate Cyclase, pubmed-meshheading:3040818-Adenylate Cyclase Toxin, pubmed-meshheading:3040818-Adipose Tissue, pubmed-meshheading:3040818-Animals, pubmed-meshheading:3040818-Cholera Toxin, pubmed-meshheading:3040818-Cyclic AMP, pubmed-meshheading:3040818-Forskolin, pubmed-meshheading:3040818-GTP-Binding Proteins, pubmed-meshheading:3040818-Insulin, pubmed-meshheading:3040818-Isoproterenol, pubmed-meshheading:3040818-Male, pubmed-meshheading:3040818-Pertussis Toxin, pubmed-meshheading:3040818-Phenylisopropyladenosine, pubmed-meshheading:3040818-Rats, pubmed-meshheading:3040818-Rats, Inbred Strains, pubmed-meshheading:3040818-Virulence Factors, Bordetella
pubmed:year
1986
pubmed:articleTitle
Insulin stimulation of cyclic AMP phosphodiesterase is independent from the G-protein pathways involved in adenylate cyclase regulation.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't