Disease relevance of S100b

• Astrocytosis and axonal proliferation in the hippocampus of S100b transgenic mice [1].
• A nucleic acid stain (to identify all ganglion cells) was combined with immunostaining for PGP9.5 and S100b to detect neurons and glial cells, respectively, in the postnatal intestine [2].
• S100b, an acidic low weight and zinc binding protein, has attracted considerable interest due to its release into the cerebrospinal fluid and blood from brain tissue following brain damage and from malignant melanomas [3].

High impact information on S100b

• Here, we demonstrate that calcium-binding protein S100B, which is synthesized in considerable amounts in astrocytes (a major glial cell subtype), modulates long-term synaptic plasticity [4].
• Characterization of the tumor suppressor protein p53 as a protein kinase C substrate and a S100b-binding protein [5].
• Divergent pathways of gene expression are activated by the RAGE ligands S100b and AGE-BSA [6].
• RESULTS: Treatment of human pancreatic islets with HG and S100b led to a three-five-fold induction of PTGS2 mRNA (p<0.001) [7].
• We previously showed that, in contrast to the distribution of S100b (beta beta), S100a0 (alpha alpha) is mainly present in human skeletal and heart muscles at the level of 1-2 micrograms/mg of soluble protein and is universally distributed at high levels in skeletal and heart muscles of various mammals [8].

Biological context of S100b

• The mouse Mif gene maps to the middle region of chromosome 10, between Bcr and S100b, which have been mapped to human chromosomes 22q11 and 21q22.3, respectively [9].
• Cells expressing the pan-neuronal markers, neurofilament-M and Hu, or the glial marker, S100b, were observed undergoing mitosis [10].

Anatomical context of S100b

• At postnatal day 0, fewer than 5% and 10% of cells in myenteric ganglia of the small and large intestine, respectively, were neither PGP9.5(+) nor S100b(+) [2].
• MATERIALS AND METHODS: Isolated human pancreatic islets were treated for 24 h with HG (25 mmol/l) or with S100b (5 mg/l), a specific ligand for the AGE-specific receptor [7].
• S-100 proteins (S-100 a and S-100 b) were specifically abundant in nerve tissues [11].

Associations of S100b with chemical compounds

• Moreover, addition of citrate, a potent ligand for trivalent cations, resulted in a significant withdrawal in mAb recognition of aluminium which was previously bound to either CaM or S100b proteins [12].

Other interactions of S100b

• These results suggest that a predominant form of S100 protein in human myocardial cells is not S100a (alpha beta) or S100b (beta beta), but S100a0 (alpha alpha) [13].

References