Accumulation of misfolded proteins is a hallmark in the pathogenesis of many disorders, including common neurodegenerative diseases such as Alzheimer’s disease, Parkinson’s disease, Huntington’s disease and Amyotrophic Lateral Sclerosis.
The presence of this abnormal protein accumulation has been correlated with the activation of a stress signaling pathway emerging from the endoplasmic reticulum, a cellular reaction named the “Unfolded Protein Response” (UPR).
The proper folding of proteins is vital for cellular function and survival. Perturbation of protein folding may cause accumulation of unfolded or misfolded proteins in the lumen, resulting in the development of pathogenic states.
This dysfunction could be due to genetic polymorphisms or mutations or also be caused by environmental stress to induce age-related diseases, Example of such diseases include but are not restricted to: Alzheimer’s Parkinson’s, Charcot-Marie-Tooth or retinitis pigmentosa, type II Diabetes, and some forms of cancer.