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Jessica Cardin, MS


The regulation of protein assembly and disassembly (protein flux) within the body has been a topic that has been studied extensively for the last 60 years. However, the majority of the research has been mostly focused on the rates of assembly (synthesis) and the related methodologies. Protein disassembly (degradation) is an equally viable research endeavor, as it is the other half of protein flux within tissues and whole body systems.

The body has many protein pools that are in constant flux and dysregulated degradation has been linked to many disease states, including Type II Diabetes, multiple forms of cancer, neurological degenerative disorders. Previous research has focused on either one of the two main systems for disassembly within the cell; the proteasome or the lysosome. 

However, the current body of work has neglected the synergy between these two cell structures and the potential for a mechanism that allows a cell to compensate when a proteolytic pathway is impaired or incapacitated. This pioneering research is important, as it will be the first to characterize the ability of the muscle cell to “shuttle” or partition protein disassembly between these two structures. Being able to comprehend how protein degradation works, as an entire system, will be invaluable for medical professionals to synthesize new treatments to combat the progression of diseases involving protein wasting. 

Sources:

        1. Schneider JL, and Cuervo AM. Autophagy and human disease: emerging themes. Current opinion in genetics & development 26: 16-23, 2014.

        2. Akin D, Wang SK, Habibzadegah-Tari P, Law B, Ostrov D, Li M, Yin X-M, Kim J-S, Horenstein N, and Dunn Jr WA. A novel ATG4B antagonist inhibits autophagy and has a negative impact on osteosarcoma tumors. Autophagy 10: 2021-2035, 2014.

        3. Altun M, Besche HC, Overkleeft HS, Piccirillo R, Edelmann MJ, Kessler BM, Goldberg AL, and Ulfhake B. Muscle wasting in aged, sarcopenic rats is associated with enhanced activity of the ubiquitin proteasome pathway. J Biol Chem 285: 39597-39608, 2010.

       4. Gasier HG, Riechman SE, Wiggs MP, Previs SF, and Fluckey JD. A comparison of 2H2O and phenylalanine flooding dose to investigate muscle protein synthesis with acute exercise in rats. American Journal of Physiology-Endocrinology and Metabolism 297: E252-E259, 2009.

       5. Nilsson MI, Greene NP, Dobson JP, Wiggs MP, Gasier HG, Macias BR, Shimkus KL, and Fluckey JD. Insulin resistance syndrome blunts the mitochondrial anabolic response following resistance exercise. American Journal of Physiology-Endocrinology and Metabolism 299: E466-E474, 2010.


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