Aggregation and toxicity

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  • Susan L.Lindquist*† and Steven Henikoff‡ *Whitehead Institute for Biomedical Research, Massachusetts Institute of Technology, Cambridge, MA 02142; and ‡The Fred Hutchinson Cancer Research Center, Seattle, WA 98109 Over the past half-century, the central dogma, in which DNA makes RNA makes protein, has dominated thinking in biology, with continuing refinements in understanding of DNA inheritance, gene expression, and macromolecular interactions. However, we have also witnessed the elucidation of epigenetic phenomena that violate conventional notions of inheritance.

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  • Amyloid-b(Ab) aggregation and amyloid formation are key pathological features of Alzheimer’s disease, and are considered to be two of the major contributing factors to neurodegeneration and dementia. Identification of small molecule inhibitors that are orally available, have low toxicity and high central nervous system bioavailability is one approach to the potential development of a disease-modifying treatment for Alzheimer’s disease.

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  • Our setup allows us to disentan- gle the implications of these two alternative pricing mechanisms that are standard in the open-economy macro literature. In our model, di®erent assumptions regarding the pricing decisions of ¯rms are virtually inconsequential for the properties of aggregate variables, other than the terms of trade. In particular, the real exchange rate and the international relative price of ¯nal tradable goods behave similarly across the two price setting regimes.

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  • Stages of neutrophil development shown schematically. G-CSF (granulocyte colony-stimulating factor) and GM-CSF (granulocytemacrophage colony-stimulating factor) are critical to this process. Identifying cellular characteristics and specific cell-surface markers are listed for each maturational stage. Figure 61-3 Neutrophil band with Döhle body. The neutrophil with a sausage-shaped nucleus in the center of the field is a band form.

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  • Alzheimer’s disease (AD) is an age-related, progressive degenerative dis-order that is characterized by synapse and neuron loss in the brain and the accumulation of protein-containing deposits (referred to as ‘senile plaques’) and neurofibrillary tangles. Insoluble amyloid b-peptide (Ab) fibrillar aggregates found in extracellular plaques have long been thought to cause the neurodegenerative cascades of AD.

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  • A yeast model was generated to study the mechanisms and phenotypical repercussions of expression of a-synuclein as well as the coexpression of protein tau. The data show that aggregation ofa-synuclein is a nucleation– elongation process initiated at the plasma membrane. Aggregation is con-sistently enhanced by dimethyl sulfoxide, which is known to increase the level of phospholipids and membranes in yeast cells.

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  • Yadav et al. (2007) studied on fertilizer industrial discharge showed that some components in the discharge may interact with each other and produce toxic to aquatic organisms. For instance, the interaction between dissolved oxygen and ammonia changed the respiratory physiology in fresh water fish. In addition, results showed that the toxicity of the effluent in fish depends on concentration and duration of exposure.

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  • Pesticide risk assessments cover all endpoints of concern. OPP updates risk assessment methods as science evolves or new information becomes available, and has worked to improve protection of children’s health. There has been an increased emphasis on toxic effects unique to children. OPP requires advanced toxicity testing to assess possible effects on the fetus and developing young, including developmental neurotoxicity and reproductive studies.

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  • All combined or “synthetic” measures which try to measure environmental and economic changes in one indicator can be dismissed as over-simplistic. Beyond this, however, there is also the serious question of how meaningful it is to try to produce an estimate of national sustainability rather than assess the benefits and impacts of particular activities within a country.

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  • Human stefin B, from the family of cystatins, is used as a model amyloido-genic protein in studies of the mechanism of amyloid fibril formation and related cytotoxicity. Interaction of the protein’s prefibrillar oligo-mers⁄aggregates with predominantly acidic phospholipid membranes is known to correlate with cellular toxicity.

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  • After the successful cloning of the first gene for a polyglutamine disease in 1991, the expanded polyglutamine tract in the nine polyglutamine disease proteins became an obvious therapeutic target. Early hypotheses were that misfolded, precipitated protein could be a universal pathogenic mechanism. However, new data are accumulating on Huntington’s disease and other polyglutamine diseases that appear to contradict the toxic aggregate hypothesis.

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  • The amyloidbpeptide (Ab) with 39–42 residues is the major component of amyloid plaques found in brains of Alzheimer’s disease patients, and solu-ble oligomeric peptide aggregates mediate toxic effects on neurons. The Ab aggregation involves a conformational change of the peptide structure to b-sheet.

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  • Protein aggregation is central to most neurodegenerative diseases, as shown by familial case studies and by animal models. A modified ‘amyloid cas-cade’ hypothesis for Alzheimer’s disease states that prefibrillar oligomers, also called amyloid-b-derived diffusible ligands or globular oligomers, are the responsible toxic agent. It has been proposed that these oligomeric spe-cies, as shown for amyloid-b, b2 -microglobulin or prion fragments, exert toxicity by forming pores in membranes, initiating a cascade of detrimental events for the cell. ...

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  • Beta-amyloid (1–40) (Abeta), the main component of senile plaques seen in the brains of Alzheimer’s disease patients, was found to be toxic both as fibrils and smaller soluble globular aggregates. The hydrolytic properties of Abeta, a new biochemical activity described previously [Brzyska M, Bacia A & Elbaum D (2001)Eur J Biochem268, 3443–3454], may contribute to its overall toxicity.

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