Disease relevance of S100b

• Reduction in S100 protein beta subunit mRNA in C6 rat glioma cells following treatment with anti-microtubular drugs [1].
• One hour of ischemia significantly increased protein S100B release from rat brain slices without altering lactate dehydrogenase leakage [2].
• Induction of S100b in myocardium: an intrinsic inhibitor of cardiac hypertrophy [3].

Psychiatry related information on S100b

• Long lasting sex-specific effects upon behavior and S100b levels after maternal separation and exposure to a model of post-traumatic stress disorder in rats [4].

High impact information on S100b

• Interactions between the microtubule-associated tau proteins and S100b regulate tau phosphorylation by the Ca2+/calmodulin-dependent protein kinase II [5].
• In addition, these neuronal cell types do not synthesize two glial proteins, S100 protein (S100P) and glial fibrillary acidic protein (GFAP) [6].
• In addition to binding Ca(2+), the S100 protein S100B binds Zn(2+) with relatively high affinity as confirmed using isothermal titration calorimetry (ITC; K(d) = 94 +/- 17 nM) [7].
• In the absence of KCl, rat brain S100b protein is characterized by two high-affinity Ca2+ binding sites with a KD of 2 X 10(-5) M and four lower affinity sites with KD about 10(-4) M [8].
• No increase in the tyrosine fluorescence quantum yield after Zn2+ binding to rat S100b was observed.(ABSTRACT TRUNCATED AT 250 WORDS)[8]

Chemical compound and disease context of S100b

• Rising the glutamate levels in the medium by each ouabain or exogenous glutamate, moreover, failed in exerting an ischemia like effect on protein S100B and LDH outputs [2].

Biological context of S100b

• Idiotypic antibodies against protein S100b inhibited synaptic transmission from Schaffer collateral axons to pyramidal neurons, but had no effect on neuronal responses to antidromic stimulation [9].
• Idiotypic antibodies against protein S100b suppressed changes in neuronal responses to orthodromic stimulation during long-term potentiation, while antiidiotypic antibodies facilitated these effects [9].
• Noncovalent interaction between tau and S100b depended on the presence of Ca2+ or Zn2+ and resulted in total inhibition of tau phosphorylation by protein kinase II [5].
• The IC50 of S100b for beta I and beta II PKC was 8 microM while for alpha and gamma PKC it was 64 microM [10].
• We studied the effects of S100b protein in doses stimulating (500 and 50 ng) or inhibiting (5 ng) apoptosis in nerve cells on acquisition, retention, and retrieval of extinction of the acoustic startle response and conditioned fear in adult rats [11].

Anatomical context of S100b

• In the three prosencephalic areas, astrocytes' cell area (GFAP-ir cells) increased after EtOH exposure and tended to return to normality after abstinence, while cytoplasmic astroglial S100b protein-ir, relative area of MAP-2-ir and Nf-200-ir fibers decreased, and later partially recovered [12].
• Effects of idiotypic and antiidiotypic antibodies against protein S100b on synaptic transmission and long-term potentiation of CA1 pyramidal neurons in rat hippocampus were studied [9].
• The data suggest that endogenous S100b is involved in the regulation of microtubule assembly in brain extracts [13].
• S100b contents in the hippocampus, hypothalamus, frontal cortex, and cerebellar hemispheres and vermis, and in the basal nuclei were measured in rat brains 0.5, 1, 2, 4, 6, 8, 24, and 48 h after long-term habituation to the startle response [14].
• The astrocytic protein S100B stimulates neurite outgrowth and neuronal survival during CNS development [15].

Associations of S100b with chemical compounds

• Although removal of extracellular Ca(+2) ions from the medium did not alter the basal lactate dehydrogenase leakage from cortical slices, an excessive increase in basal protein S100B release was seen under this condition [2].
• In contrast, exogenous glutamate added into the medium protected the slices against reoxygenation induced increments in protein S100B and lactate dehydrogenase levels [2].
• Purified rat S100b protein comigrates with bovine S100b protein in nondenaturant system electrophoresis but differs in its amino acid composition and in its electrophoretic mobility in urea-sodium dodecyl sulfate-polyacrylamide gel with bovine S100b protein [8].
• Ipsapirone (10(-9)M) was more effective on neuronal cell bodies staining and S100b (10 ng/ml) was more effective in increasing the number of synaptophysin-IR varicosities on neuronal processes [16].
• This effect in the whole animal may be due to activation of 5-HT1A receptors and a corresponding increases in S100b and corticosterone [16].

Other interactions of S100b

• The aim of this work was to evaluate the cerebrospinal fluid (CSF) levels of neuron specific enolase (NSE), protein S100B and lactate of rats submitted to acute and chronic models of ECS [17].

Analytical, diagnostic and therapeutic context of S100b

• Binding between the microtubule-associated tau protein and S100b protein was demonstrated by affinity chromatography and cross-linking experiments and was manifested in the effect of S100b on tau protein phosphorylation by protein kinase II [5].
• The properties of the Ca2+ and Zn2+ binding sites on rat S100b protein were investigated by flow dialysis and by fluorometric titration, and the conformation of rat S100b in its metal-free form as well as in the presence of Ca2+ or Zn2+ was studied [8].
• Using light and electron microscopic immunocytochemistry, we examined the expression of the Ca2+-binding protein S100B in the dentate gyrus of adult rats during lesion-induced sprouting and reactive synaptogenesis [18].

References