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Binding of S100 proteins to RAGE: an update.
Antibodies inhibit prion propagation and clear cell cultures of prion infectivity
It is shown that antibodies binding cell-surface PrPC inhibit PrPSc formation in a dose-dependent manner, and this observations support the use of antibodies in the prevention and treatment of prion diseases and identify a region of PrPC for drug targeting.
Novel aspects of calmodulin target recognition and activation.
The novel structures of CaM-target complexes discussed here demonstrate that this mechanism of activation may be less general than previously believed and seems to be not valid for the anthrax exotoxin, theCaM-regulated K+-channel and possibly also not for the Ca2+-pump.
S100B and S100A6 Differentially Modulate Cell Survival by Interacting with Distinct RAGE (Receptor for Advanced Glycation End Products) Immunoglobulin Domains*
- E. Leclerc, G. Fritz, M. Weibel, C. Heizmann, A. Galichet
- BiologyJournal of Biological Chemistry
- 26 October 2007
Comparison of the interaction of two S100 proteins, S100B and S100A6, with RAGE by in vitro assay and in culture of human SH-SY5Y neuroblastoma cells suggests that the receptor for advanced glycation end products (RAGE) plays important roles in mediating S100 protein-induced cellular signaling.
Trafficking of prion proteins through a caveolae-mediated endosomal pathway
It is proposed that this nonclassical endocytic pathway is likely to determine the subcellular location of PrPC conversion and was not observed for several other glycosylphosphatidyl inositol (GPI)-anchored proteins.
Structural and functional insights into RAGE activation by multimeric S100B
The structural and the binding data suggest that tetrameric S100B triggers RAGE activation by receptor dimerisation, which caused stronger activation of cell growth than S 100B dimer and promoted cell survival.
Measuring prions causing bovine spongiform encephalopathy or chronic wasting disease by immunoassays and transgenic mice
The CDI is capable of measuring the disease-causing PrP isoform (PrPSc) in bovine brainstems with a sensitivity similar to that of end-point titrations in transgenic mice expressing BoPrP, and was able to discriminate between PrPSc from BSE-infected cattle and Tg(BoPrP) mice as well as from chronic wasting disease -infected deer and elk.
Anti-DNA antibodies are a major component of the intrathecal B cell response in multiple sclerosis.
- R. Williamson, M. Burgoon, D. Burton
- Biology, MedicineProceedings of the National Academy of Sciences…
- 13 February 2001
It is found that high-affinity anti-DNA antibodies are a major component of the intrathecal IgG response in the patients with MS that the authors studied and indicates that anti- DNA antibodies may promote important neuropathologic mechanisms in chronic inflammatory disorders, such as MS and systemic lupus erythematosus.
The S100B/RAGE Axis in Alzheimer's Disease
The role of S100B/RAGE activation in Alzheimer's disease is discussed and the regulation of RAGE signaling by S 100B is complex and probably involves other ligands including the amyloid beta peptide, the Advanced Glycation Endproducts, or transtheyretin.
The extracellular region of the receptor for advanced glycation end products is composed of two independent structural units.
- Brian M. Dattilo, G. Fritz, E. Leclerc, C. V. Kooi, C. Heizmann, W. Chazin
- 18 May 2007
The results show that the V and C1 domains are not independent domains, but rather form an integrated structural unit and the implications are discussed with respect to models for RAGE signaling.