Aggregation of misfolded proteins is a hallmark of many neurodegenerative diseases, such as Alzheimer’s disease, Parkinson’s disease, amyotrophic lateral sclerosis and polyglutamine (polyQ) diseases. Clearance of misfolded proteins in the cell relies on the ubiquitin-proteasome system (UPS) and the autophagy-lysosome system. Since their discoveries, the UPS and autophagy were once thought to be independent of each other in terms of components, mechanisms and substrate selectivity. The UPS was believed to be responsible for degrading soluble proteins, whereas autophagy for degrading insoluble protein aggregates. However, recent studies have demonstrated that the insoluble protein aggregates may not be cytotoxic. By contrast, after deaggregation, multimers and microaggregates may still be present in the cell causing cytotoxicity. The UPS is incapable of degrading these soluble and semi-soluble species, and the vital task of degradation these toxic species rests upon the autophagy-lysos...
Cervical intraepithelial neoplastic grads1 were studied by flexible endoscopy obtaining five images: First image obtaining using white light the second and third image obtaining by blue, green narrow band image respectively by the special technique of endoscopy the fourth image was obtaining after that acetic acid was applied lastly, the iodine stain is applied and the fifth image was recorded after end of examination the five image were recorded and reviewed to be studied in correlation with cytology and histopathology results to be obtaining accurate diagnosis for CIN1. Go through link for full article ↡ https://medwinpublishers.com/AABSc/AABSc16000127.pdf