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The effects of protein oxidation, for example of methionine residues, are linked to many diseases, including those of protein misfolding, such as Alzheimer’s disease. Protein misfolding diseases are characterized by the accumulation of insoluble proteinaceous aggregates comprised mainly of amyloid fibrils. Amyloid-containing bodies known as corpora amylacea (CA) are also found in mammary secretory tissue, where their presence slows milk flow. The major milk protein κ-casein readily forms amyloid fibrils under physiological conditions. Milk exists in an extracellular oxidizing environment. Accordingly, the two methionine residues in κ-casein (Met95 and Met106) were selectively oxidized and the effects on the fibril-forming propensity, cellular toxicity, chaperone ability, and structure of κ-casein were determined. Oxidation resulted in an increase in the rate of fibril formation and a greater level of cellular toxicity. β-Casein, which inhibits κ-casein fibril formation in vitro, was less effective at supp...
| Authors: | Tomas Koudelka; Francis C. Dehle; Ian F. Musgrave; Peter Hoffmann; John A. Carver | |
| Journal: | Journal of Agricultural and Food Chemistry | |
| Year: | 2012 | |
| DOI: | 10.1021/jf205168t | |
| Publication date: | 11-04-2012 |
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Rohm and Haas Powder Coatings is delighted to announce that its Reading, Pennsylvania, facility is the first site in the world to receive the RCMS® Site Certification awarded by the American Chemical Council (ACC). When Raj Gupta, Chairman and CEO of Rohm and Haas Company, became Chairman ... more
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