2004
DOI: 10.1023/b:nere.0000018844.51009.40
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S100B-Mediated Inhibition of the Phosphorylation of GFAP Is Prevented by TRTK-12

Abstract: S100B belongs to a family of calcium-binding proteins involved in cell cycle and cytoskeleton regulation. We observed an inhibitory effect of S100B on glial fibrillary acidic protein (GFAP) phosphorylation, when stimulated by cAMP or Ca2+/calmodulin, in a cytoskeletal fraction from primary astrocyte cultures. We found that S100B has no direct effect on CaM KII activity, the major kinase in this cytoskeletal fraction able to phosphorylate GFAP. The inhibition of GFAP phosphorylation is most likely due to the bi… Show more

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Cited by 30 publications
(18 citation statements)
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“…Upon binding, S100β promotes disassembly of IF [72]. S100β-binding leads to inhibition of GFAP phosphorylation, which might be the mode of action that led to disassembly of IF [73]. Glial derived neurotrophic factor (GDNF) and neurturin (another glia-derived trophic factor) have also been shown to be glia-protective [74,75].…”
Section: The Role Of Gfap In Astrocyte Activation (Astrogliosis) and mentioning
confidence: 99%
“…Upon binding, S100β promotes disassembly of IF [72]. S100β-binding leads to inhibition of GFAP phosphorylation, which might be the mode of action that led to disassembly of IF [73]. Glial derived neurotrophic factor (GDNF) and neurturin (another glia-derived trophic factor) have also been shown to be glia-protective [74,75].…”
Section: The Role Of Gfap In Astrocyte Activation (Astrogliosis) and mentioning
confidence: 99%
“…Primary cultures of astrocytes express important markers, such as GFAP (glial fibrillary acidic protein), S100B and GS proteins [24], [25], [26], [27], [28], [29]. In addition, astrocyte cultures are extremely useful for metabolic studies of the glutamatergic system, oxidative stress and the inflammatory response [3], [11], [30], [31].…”
Section: Introductionmentioning
confidence: 99%
“…As with other S100 protein members, calcium binding to S100B induces a large conformational change that exposes hydrophobic residues allowing it to interact with other proteins in order to confer biological activity. [3][4][5] In this manner, S100B has been shown to control the assembly of tubulin 6,7 and other cytoskeletal proteins [8][9][10] and regulate a variety of phosphorylation events including those of Ndr kinase 11 and protein kinase II 12,13 in calcium-sensitive manners.…”
Section: Introductionmentioning
confidence: 99%