Abstract
Neurodegenerative diseases (NDs) are characterized by the accumulation of misfolded proteins. The hallmarks of protein aggregation in NDs proceed with impairment in the mitochondrial function, besides causing an enhancement in endoplasmic reticulum (ER) stress, neuroinflammation and synaptic loss. As accumulation of misfolded proteins hampers normal neuronal functions, it triggers ER stress, which leads to the activation of downstream effectors formulating events along the signaling cascade—referred to as unfolded protein response (UPRER) —thereby controlling cellular gene expression. The absence of disease-modifying therapeutic targets in different NDs, and the exponential increase in the number of cases, makes it critical to explore new approaches to treating these devastating diseases. In one such approach, osmolytes (low molecular weight substances), such as taurine have been found to promote protein folding under stress conditions, thereby averting aggregation of the misfolded proteins. Maintaining the structural integrity of the protein, taurine-mediated resumption of protein folding prompts a shift in folding homeostasis more towards functionality than towards aggregation and degradation. Together, taurine enacts protection in NDs by causing misfolded proteins to refold, so as to regain their stability and functionality. The present study provides recent and useful insights into understanding the progression of NDs, besides summarizing the genetics of NDs in correlation with mitochondrial dysfunction, ER stress, neuroinflammation and synaptic loss. It also highlights the structural and functional aspects of taurine in imparting protection against the aggregation/misfolding of proteins, thereby shifting the focus more towards the development of effective therapeutic modules that could avert the development of NDs.
Highlights
The human brain is a complex organ of the human body, consisting of different cells, such as neurons, oligodendrocytes, microglia, astrocytes, etc., that work in a coordinated manner and regulate spatiotemporally
The present article contains recent and useful information pertaining to the etiology of neurodegenerative diseases (NDs) and factors that contribute to the development of NDs, together with the biology of taurine, a major cellular osmoprotectant that overcomes the toxicity that arises due to aggregation of misfolded proteins
The aggregation of misfolded proteins that leads to the generation of plaques, tangles, Lewy bodies, etc., and their deposition in different cell subsets of the brain and in the extracellular milieu, proceeds to the development of different NDs
Summary
The human brain is a complex organ of the human body, consisting of different cells, such as neurons, oligodendrocytes, microglia, astrocytes, etc., that work in a coordinated manner and regulate spatiotemporally. The underlying homeostasis network that regulates the complex architectural of the brain, being robust at the beginning (young age), shows a gradual decline in terms of functioning with age, thereby resulting in cognitive decline and, as such, development of a variety of neurodegenerative diseases (NDs) [1]. The absence of disease-modifying therapeutic targets in different NDs, and the exponential increase in the number of cases, makes it critical to explore new approaches to treating these devastating NDs. The present article contains recent and useful information pertaining to the etiology of NDs and factors that contribute to the development of NDs (in particular mitochondrial dysfunction, endoplasmic reticulum stress, neuroinflammation and synaptic loss, which progress to neuronal death), together with the biology of taurine, a major cellular osmoprotectant that overcomes the toxicity that arises due to aggregation of misfolded proteins. Taurine thereby imparts protection against oxidative stress, via regulation of protein folding/unfolding
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