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Protein degradation plays a critical role in synaptic plasticity, but the molecular mechanisms are not well understood. Previously we showed that proteasome inhibition enhances the early induction part of long-term synaptic plasticity for which protein synthesis is essential. In this study, we tested the effect of proteasome inhibition on protein synthesis using a chemically induced long-lasting synaptic plasticity (cLTP) in the murine hippocampus as a model system. Our metabolic labeling experiments showed that cLTP induction increases protein synthesis and proteasome inhibition enhances the amount of newly synthesized proteins. We then found that amyloid beta (Aβ), a peptide contributing to Alzheimer's pathology and impairment of synaptic plasticity, blocks protein synthesis increased by cLTP. This blockade can be reversed by prior proteasome inhibition. Thus, our work reveals interactions between protein synthesis and protein degradation and suggests a possible way to exploit protein degradation to rescue adverse Aβ effects on long-term synaptic plasticity.

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Medical imaging is a quickly growing industry where the need for highly efficient lossless compression algorithms is necessary in order to reduce storage space and transmission rates for the large, high resolution, medical images. Due to the fact that medical imagining cannot utilize lossy compression, in the event that vital information may be lost, it is imperative that lossless compression be used. While several authors have investigated lossless compression of medical images, the Burrows-Wheeler Transformation with an Inversion Coder (BWIC) has not been examined. Our investigation shows that BWIC runs in linear time and yields better compression rates than well-known image coders, such as JPEG-LS and JPEG-2000.