Download Alterations in the Neuronal Cytoskeleton in Alzheimer by Steven S. M. Chin, Ronald K. H. Liem (auth.), George Perry PDF

By Steven S. M. Chin, Ronald K. H. Liem (auth.), George Perry (eds.)

The neuronal cytoskeleton is a posh constitution aware of either intrinsic and extrinsic elements. outlined populations of neurons within the brains of sufferers with Alzheimer and a number of other neurodegenerative illnesses comprise irregular filamentous accumulations which percentage parts with the cytoskeleton. even supposing there's a normal consensus that those irregular filaments do comprise cytoskeletal components, a lot debate continues to be relating to which cytoskeletal components are integrated and even if the cytoskeletal rearrangement is basic or secondary to different mobile adjustments. during this booklet those questions are addressed in a old perspect­ ive in mild of recent information that enables the reinterpretation of formerly said effects. Contributions are according to the various significant tech­ niques of recent biology together with biochemistry, molecular biology, electron microscopy and immunocytochemistry. within the view of the editor, this quantity is being written at a time while our figuring out of the cytopathology of Alzheimer ailment is relocating from predominantly descriptive to either analytical and mechanistic. i'm hoping that this contribution will offer impetus to hurry this transi­ tion. George Perry Cleveland, Ohio vii ACKNOWLEDGEMENT The aid of the Fidia Pharmaceutic company for the pc­ generated colour determine on web page sixty five is gratefully acknowledged.

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Extra resources for Alterations in the Neuronal Cytoskeleton in Alzheimer Disease

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J. Selkoe, Microtubule-associated protein tau (t) is a major antigenic component of paired helical filaments in Alzheimers disease. Proc Natl Acad Sci USA 83: 4044-4048 (1986). D. Cole, Phosphorylation affects the ability of tau protein to promote microtubule assembly. J BioI Chem. 259: 5301-5305 (1984). F. , Phosphorylation of tubulin by a calmodulin-dependent protein kinase. J BioI Chem. 261: 10332-10339 (1986). N. T. Bramblett, and M. Flavin, The sites at which brain microtubule-associated protein 2 is phosphorylated in vivo differ from those accessible to cAMP-dependent kinase in vitro.

136. 137. 138. 139. 140. 141. 142. 143. 22 Rendrickson AE, Cowan WM: Changes in the rate of axoplasmic transport during postnatal development of the rabbit's optic nerve and tract. Exp Neurol 30:403422, 1971 Willard M, Simon C: Modulations of neurofilament axonal transport during the development of rabbit retinal ganglion cells. Cell 35:551-559, 1983 Nixon RA, Logvinenko KB: Multiple fates of newly synthesized neurofilament proteins: Evidence for a stationary neurofilament network distributed nonuniformly along axons of retinal ganglion cell neurons.

Recently, it was reported that phosphorylated tau proteins are the major antigenic component of the paired helical filaments that characterize degenerative human neurons in Alzheimer's disease. 4 ,5,6 The enrichment in phosphorylated tau proteins seemed to be accompanied by an impoverishment in microtubules. It is significant, then, that Lindwall and Cole 7 found that phosphorylation of tau reduced its ability to promote microtubule assembly. Moreover, at high ratios of phosphorylated tau to tubulin, anomalies were reported in the turbidity assay for microtubule assembly, indicating aberrations in the structure of the tubulin polymers.

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