Introduction
As protein exists in every cell as a very important cellular component oddly for cell functioning, it is inevitable that cells will produce protein sum of money at some point of their life cycle. Protein aggregates apprize be in the form of amyloid (structured) or amorphous where under physiological conditions both are metabolically stable and insoluble. Normal unemphatic cells do not necessarily accumulate protein aggregates although the aggregates are act to be produced in the cells. This is because the cell has a quality determine mechanism which can suppress aggregates formation and more significantly selectively breaking down any misfolded proteins before an aggregate can be formed. However, a mutation in the special protein primary sequence or RNA modification of the protein which can be genetically or sporadically triggered can press forward protein aggregation process.
Misfolded proteins particularly the amyloid conformation accumulation is tightly associated with many neurodegenerative diseases as neurons are vulnerable to the adverse effectuate of abnormal protein folding which can initiate cell end signalling pathways. The common amyloid features of these neurodegenerative diseases imply the possibility of parallel therapeutics approaches in the management of these neurological disorders, based on normal cellular mechanisms of removing abnormal noxious proteins. Here, we will briefly review on some of the neurodegenerative disorders and their associated mechanisms of protein misfolding and aggregation and then focus on the Alzheimers disease as well as the cellular custodial mechanisms against abnormal protein aggregates with regards to therapeutic implications [1, 2, 3, 4].
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