Determination of Trends Underlying Aspartic Acid Isomerization in Intact Proteins Reveals Unusually Rapid Isomerization of Tau.
Abstract
Spontaneous chemical modifications in long-lived proteins can potentially change protein structure in ways that impact proteostasis and cellular health. For example, isomerization of aspartic acid interferes with protein turnover and is anticorrelated with cognitive acuity in Alzheimer's disease. However, few isomerization rates have been determined for Asp residues in intact proteins. To remedy this deficiency, we used protein extracts from SH-SY5Y neuroblastoma cells as a source of a complex, brain-relevant proteome with no baseline isomerization. Cell lysates were aged
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Research summary
The paper claims that aspartic acid isomerization in intact proteins occurs rapidly and may affect proteostasis and cognitive function in aging. This research is relevant as it investigates a biochemical modification that could influence the underlying mechanisms of aging and age-related diseases, particularly in the context of Alzheimer's disease.
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