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- W2499940618 abstract "Publisher Summary This chapter examines the S100b calcium-binding properties and Ca2+-dependent interactions with the microtubule associated with tau proteins. The S100b protein is mainly located in the cytosol of glial cells and might be secreted from glial cells. A neurite extension factor that corresponds to a disulfide form of S100b has been purified from chicken embryo cerebral cortical neurons. The Ca2+-binding properties of S100 are surveyed and Ca2+ dependent interactions of S100b with the neuronal microtubule associated tau proteins are demonstrated. The S100b protein, like calmodulin, induces total disassembly of microtubules at mM Ca2+ concentrations and does so with even higher efficiency than calmodulin does. It is demonstrated that purified tubulin did not bind to S100-Sepharose columns whether or not Ca 2+ was present, suggesting that S100 protein might bind to microtubule components other than tubulin. An S100b-Sepharose column was first equilibrated with 50 mM Tris, 100 mM NaCI, 0.5 mM CaCl2, buffer pH 7.3. Complex formation of tau with Sb was confirmed when it was discovered that S100b inhibited the calcium/ phospholipid-dependent phosphorylation of tau proteins by protein kinase C by interacting with the substrate rather than with the kinase." @default.
- W2499940618 created "2016-08-23" @default.
- W2499940618 creator A5023208717 @default.
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- W2499940618 date "1987-01-01" @default.
- W2499940618 modified "2023-10-16" @default.
- W2499940618 title "S100b PROTEIN: CALCIUM-BINDING PROPERTIES AND CA2+-DEPENDENT INTERACTIONS WITH THE MICROTUBULE ASSOCIATED TAU PROTEINS: S100b REGULATES TAU PHOSPHORYLATION BY PROTEIN KINASE C11Supported by grants from Institut National de la Santé et de la Recherche Medicale, NIH Grants EHS-ES-01896, GMS-20338 and by the Agricultural Research Station." @default.
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- W2499940618 doi "https://doi.org/10.1016/b978-0-12-521040-9.50096-6" @default.
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