Large Amounts of Glutamine as the Cause of Disease Essay -- Biology Al

Neurodegenerative disorders such as Alzheimer's disease and Parkinson's disease are caused by the aggregation of abnormal proteins in neurons. An essential component of cellular function is the correct assimilation of proteins in the cell. Proteins fold into specific structures and then carry out cellular functions. However, when this folding process runs amuck, abnormal proteins are introduced into the cell. In neurodegenerative diseases, these protein aggregates are characterized by having genes which contain too many CAG trinucleotides repeats that encode for polyglutamine (polyQ). Having too much polyQ leads to the gene products being converted to a proteotoxic state. All in all, disruptions in protein folding lead to an overabundance of CAG repeats which results in an overproduction of polyQ which raises the toxicity of the cell to levels that effect the cell's functions. Through experimentation, this paper attempted to find the threshold for the number of CAG repeats that determines whether cellular function will be disrupted by the protein aggregates. Molecular genetic studies have already established than normal chromosomes (and genes) contain fewer than 30-34 CAG repeats. This paper attempted to prove that 35-40 CAG repeats results in cellular toxicity levels that severely disrupt cellular function. To address the connection between the CAG threshold (thus, the polyQ aggregation) and cellular toxicity, a species of worm, Caenorhabditis elegans, was used during experimentation. (C. elegans are good model organisms to study human neurodegenerative disease not only because C. elegans' neurons resemble vertebrate neurons at cellular and molecular levels, but also because many genes are conserved between worms and h... ... aggregation causes cell toxicity, or if the aggregates are a benign product of some other, yet unknown process that causes the detrimental effects. If future research reveals that glutamine aggregates promote cell toxicity, we can direct research on how to inhibit these aggregations to slow down or possibly reverse the course of the disease. 2.) How aging in the infected organism influences the progression of Huntington's disease: Experiments with C. elegans expressing the age-1 genetic mutation not only had an extended the lifespan, but also had a delayed onset of Huntington's disease. This suggests that a substance produced as an organism ages can catalyzes the toxicity of Huntington's disease. With this in mind, further research could hunt for what this aging-related catalyst is. Blocking this substance may slow down or halt the progression of the disease.