Proteiinikertymiä

Proteiinikertymiä, often translated as protein aggregates or inclusions, are abnormal accumulations of misfolded proteins within or outside cells. These structures can form in various tissues and are implicated in the pathogenesis of numerous neurodegenerative diseases, such as Alzheimer's disease, Parkinson's disease, and Huntington's disease. The aggregation process typically begins with a misfolding event, where a protein adopts an incorrect three-dimensional structure. This aberrant conformation can expose hydrophobic regions, promoting interactions with other misfolded proteins. Over time, these interactions lead to the formation of oligomers, protofibrils, and eventually larger, insoluble aggregates. The exact mechanisms by which these protein deposits cause cellular dysfunction and death are complex and vary depending on the specific protein involved. However, proposed mechanisms include disruption of cellular transport, induction of oxidative stress, impairment of protein degradation pathways, and excitotoxicity. The presence and type of proteiinikertymiä are often used as diagnostic markers for specific diseases. Research into understanding the formation, toxicity, and clearance of these aggregates is a major focus in the field of neurodegenerative disease research, with the goal of developing therapeutic strategies to prevent or reverse their formation.