Cellular and molecular pathology in alzheimer's disease

Crutcher, Keith A.; Anderton, Brian H.; Barger, Steven W.; Ohm, Thomas G.; Snow, Alan D.

doi:10.1002/hipo.1993.4500030730

Cited by 48 publications

(1 citation statement)

References 181 publications

(151 reference statements)

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“…Thus one dominant question has been whether tau-based pathologies are primary independent lesions of AD, are secondary to amyloid plaque formation, or are formed via a cellular defect common to APP and tau protein processing. The reader is referred to several recent reviews concerning the molecular biology of AD for more complete information concerning the roles of APP and related presenilin genes [5,[8][9][10][11][12][13].…”

Section: Introductionmentioning

confidence: 99%

Regulated phosphorylation and dephosphorylation of tau protein: effects on microtubule interaction, intracellular trafficking and neurodegeneration

Billingsley

Kincaid

1997

Biochemical Journal

411

231

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This review attempts to summarize what is known about tau phosphorylation in the context of both normal cellular function and dysfunction. However, conceptions of tau function continue to evolve, and it is likely that the regulation of tau distribution and metabolism is complex. The roles of microtubule-associated kinases and phosphatases have yet to be fully described, but may afford insight into how tau phosphorylation at the distal end of the axon regulates cytoskeletal-membrane interactions. Finally, lipid and glycosaminoglycan modification of tau structure affords yet more complexity for regulation and aggregation. Continued work will help to determine what is causal and what is coincidental in Alzheimer's disease, and may lead to identification of therapeutic targets for halting the progression of paired helical filament formation.

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Section: Introductionmentioning

confidence: 99%

Regulated phosphorylation and dephosphorylation of tau protein: effects on microtubule interaction, intracellular trafficking and neurodegeneration

Billingsley

Kincaid

1997

Biochemical Journal

411

231

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Neural membrane phospholipids in alzheimer disease

et al. 1995

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Phospholipids form the backbone of neural membranes, providing fluidity and permeability. Two plasma membrane fractions, one from synaptosomes (SPM), the other from glial and neuronal cell bodies (PM), were prepared from different regions of autopsied Alzheimer disease (AD) brains. Corresponding fractions were prepared from age-matched control brains. All fractions from AD brains showed significantly lower levels of ethanolamine glycerophospholipids and significantly higher levels of serine glycerophospholipids than the control brain. No differences were observed in phosphatidylcholine levels among these membranes. These results suggest that altered phospholipid composition of plasma membranes may be involved in the abnormal signal transduction and neurodegeneration in AD.

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The transentorhinal cortex of the African green monkey: a combined light- and electron-microscopic study of calcium-binding protein containing neurons

Smaluhn

Plaschke

Léránth

et al. 2000

Anatomy and Embryology

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The transentorhinal cortex (TEC) is a primate-specific transition zone between the entorhinal allocortex and the temporal isocortex. Neurons in the lamina pre-alpha of TEC are known to be the first to develop intraneuronal changes in the course of Alzheimer's disease. In order to shed light on this important feature, we studied as yet unknown morphological and neurochemical characteristics of the TEC of the African green monkey (Cercopithecus aethiops sabaeus). Using light- and electron-microscopic immunocytochemistry, the distribution and morphology of neurons containing calcium-binding proteins were described and compared with those in the adjacent cortices. Light-microscopic analysis revealed that parvalbumin-containing neurons were distributed in all cortical layers. Calbindin-containing cells were fewer but also present in each layer. Calretinin-containing neurons were largely confined to the upper layers of the TEC. All three types of neuron showed pyramidal-like, multipolar and bipolar shapes; their dendrites were smooth or beaded. Ultrastructural studies revealed immunopositive somata with infolded nuclei and large amounts of cytoplasm. The somata were only sparsely innervated by symmetric synapses. Immunopositive dendrites were almost exclusively covered with immunonegative axon terminals establishing symmetric and asymmetric synapses. Immunopositive terminals established symmetric contacts with immunonegative dendrites and somata. Only occasionally, could synaptic contacts between immunopositive pre- and postsynaptic structures be observed. The comparison of neurons in the TEC and adjacent cortices revealed no striking differences. In summary, the morphological and neurochemical characteristics of TEC neurons as analyzed in our study do not provide an explanation for the early onset of neurodegenerative changes in the TEC.

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Cellular and molecular pathology in alzheimer's disease

Cited by 48 publications

References 181 publications

Regulated phosphorylation and dephosphorylation of tau protein: effects on microtubule interaction, intracellular trafficking and neurodegeneration

Regulated phosphorylation and dephosphorylation of tau protein: effects on microtubule interaction, intracellular trafficking and neurodegeneration

Neural membrane phospholipids in alzheimer disease

The transentorhinal cortex of the African green monkey: a combined light- and electron-microscopic study of calcium-binding protein containing neurons

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