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TextLocation
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Results
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a(SCHEM:"lysophosphatidic acid") -> p(HGNC:GSK3B,pmod(P,S,9))
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Approximately 2000 hand curated statements drawn from 57 PubMeds.
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Copyright (c) 2011-2012, Selventa. All Rights Reserved.
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BEL Framework Small Corpus Document
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Creative Commons Attribution-Non-Commercial-ShareAlike 3.0 Unported License
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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)
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support@belframework.org
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2014-07-03T14:29:34.648+02:00
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