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Protein Quality Control System in Neurodegeneration: a Healing Company Hard to Beat but Failure is Fatal

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Journal Mol Neurobiol
Date 2013 Feb 5
PMID 23378031
Citations 15
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Abstract

A common feature in most neurodegenerative diseases and aging is the progressive accumulation of damaged proteins. Proteins are essential for all crucial biological functions. Under some notorious conditions, proteins loss their three dimensional native conformations and are converted into disordered aggregated structures. Such changes rise into pathological conditions and eventually cause serious protein conformation disorders. Protein aggregation and inclusion bodies formation mediated multifactorial proteotoxic stress has been reported in the progression of Parkinson's disease (PD), Huntington's disease (HD), Alzheimer's disease (AD), amyotrophic lateral sclerosis (ALS) and Prion disease. Ongoing studies have been remarkably informative in providing a systematic outlook for better understanding the concept and fundamentals of protein misfolding and aggregations. However, the precise role of protein quality control system and precursors of this mechanism remains elusive. In this review, we highlight recent insights and discuss emerging cytoprotective strategies of cellular protein quality control system implicated in protein deposition diseases. Our current review provides a clear, understandable framework of protein quality control system that may offer the more suitable therapeutic strategies for protein-associated diseases.

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References
1.
Tibbles L, Woodgett J . The stress-activated protein kinase pathways. Cell Mol Life Sci. 1999; 55(10):1230-54. PMC: 11147067. DOI: 10.1007/s000180050369. View

2.
Liu J, Zheng H, Tang M, Ryu Y, Wang X . A therapeutic dose of doxorubicin activates ubiquitin-proteasome system-mediated proteolysis by acting on both the ubiquitination apparatus and proteasome. Am J Physiol Heart Circ Physiol. 2008; 295(6):H2541-50. PMC: 2654028. DOI: 10.1152/ajpheart.01052.2008. View

3.
Kraft C, Peter M, Hofmann K . Selective autophagy: ubiquitin-mediated recognition and beyond. Nat Cell Biol. 2010; 12(9):836-41. DOI: 10.1038/ncb0910-836. View

4.
Scheper G, van der Knaap M, Proud C . Translation matters: protein synthesis defects in inherited disease. Nat Rev Genet. 2007; 8(9):711-23. DOI: 10.1038/nrg2142. View

5.
Uversky V, Li J, Fink A . Trimethylamine-N-oxide-induced folding of alpha-synuclein. FEBS Lett. 2001; 509(1):31-5. DOI: 10.1016/s0014-5793(01)03121-0. View