Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
28
pubmed:dateCreated
1986-1-3
pubmed:abstractText
The steady-state relationship between the activation state of cAMP-dependent protein kinase (A-kinase) and lipolysis has been defined quantitatively. A-kinase activation was assessed by measuring the ( +/- cAMP) activity ratio in adipocyte extracts, and lipolysis was determined by measuring glycerol release from cells. Both processes were stimulated either by incubating cells in a ligand-free environment achieved with adenosine deaminase or by addition of lipolytic hormones. A response spectrum was obtained with a variety of adenylate cyclase stimulators and inhibitors, both receptor- and nonreceptor-mediated. Regardless of the ligands used to manipulate adipocyte activity, lipolysis varied from nil to maximal as the A-kinase activity ratio varied from approximately 0.05 to 0.3-0.35. These data provide a quantitative description of the steady-state relationship between A-kinase activity and lipolysis and indicate that the various lipolytic and antilipolytic agents tested act on the lipolytic process exclusively by altering adenylate cyclase activity and, thus, cellular cAMP concentrations. The data reveal also that transient "peaking" of cAMP, as measured by A-kinase activity ratios, is not an inherent feature of adipocyte metabolism. Moreover, the concentration requirements for lipolytic hormone action are critically dependent on the ambient concentration of antilipolytic agents, and t concentration requirements for antilipolytic agents are dependent on the extent to which cells are stimulated. The data in this paper provide the basis for assessing the relationship between A-kinase activity ratio and lipolysis in the presence of insulin (Londos, C., Honnor, R. C., and Dhillon, G. S. (1985) J. Biol. Chem. 260, 15139-15145).
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
260
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
15130-8
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:3877723-4-(3-Butoxy-4-methoxybenzyl)-2-imidazolidinone, pubmed-meshheading:3877723-Adipose Tissue, pubmed-meshheading:3877723-Animals, pubmed-meshheading:3877723-Cosyntropin, pubmed-meshheading:3877723-Deoxyadenosines, pubmed-meshheading:3877723-Dideoxyadenosine, pubmed-meshheading:3877723-Enzyme Activation, pubmed-meshheading:3877723-Forskolin, pubmed-meshheading:3877723-Glucagon, pubmed-meshheading:3877723-Glycerol, pubmed-meshheading:3877723-Isoproterenol, pubmed-meshheading:3877723-Kinetics, pubmed-meshheading:3877723-Lipolysis, pubmed-meshheading:3877723-Male, pubmed-meshheading:3877723-Phenylisopropyladenosine, pubmed-meshheading:3877723-Protein Kinases, pubmed-meshheading:3877723-Rats, pubmed-meshheading:3877723-Rats, Inbred Strains, pubmed-meshheading:3877723-Time Factors
pubmed:year
1985
pubmed:articleTitle
cAMP-dependent protein kinase and lipolysis in rat adipocytes. II. Definition of steady-state relationship with lipolytic and antilipolytic modulators.
pubmed:publicationType
Journal Article