sub:provenance {
  beldoc: dce:description "Approximately 2000 hand curated statements drawn from 57 PubMeds." ;
    dce:rights "Copyright (c) 2011-2012, Selventa. All Rights Reserved." ;
    dce:title "BEL Framework Small Corpus Document" ;
    dc:license "Creative Commons Attribution-Non-Commercial-ShareAlike 3.0 Unported License" ;
    pav:authoredBy sub:_5 ;
    pav:version "1.6" .
  sub:_4 prov:value """In Rat1, NIH 3T3, and HEK293 cells, increases in the intracellular levels of cAMP
stimulate phosphorylation of GSK-3α and -β, as demonstrated by immunoblotting with
GSK-3 phosphorylation-specific antibodies. As shown in Fig. 1, the cell-permeable
cAMP analogue 8-Br-cAMP induced a marked increase in phosphorylation of GSK-3α
and - β at serine 21 and 9, respectively, whereas the structurally related
cGMP analogue 8-Br-cGMP had little effect. Forskolin, which activates adenyl cyclase
thus raising intracellular cAMP levels (15), triggered a similar elevation
in GSK-3 phosphorylation at serine 21 and 9. In Rat1 cells, isoproterenol, which
activates the b-adrenergic receptor stimulating adenylate cyclase and increasing
endogenous cAMP levels (16, 17), also efficiently stimulated GSK-3 phosphorylation
at these serine sites. In NIH 3T3 cells that contain few of the β-adrenergic
receptors, stimulation with other G-protein-coupled receptor agonists, such as
lysophosphatidic acid. also led to GSK-3 phosphorylation (data not shown)""" ;
    prov:wasQuotedFrom pubmed:11035810 .
  sub:_5 rdfs:comment "support@belframework.org" ;
    rdfs:label "Selventa" .
  sub:assertion prov:hadPrimarySource pubmed:11035810 ;
    prov:wasDerivedFrom beldoc: , sub:_4 .
}