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

Neurode generative disorders such as Alzheimers disease and Parkinsons 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 by 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 cells functions. finished experimentation, this paper attempted to find the threshold for the number of CAG repeats that deter mines 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 data link 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 non 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 auspicious product of some other, yet unknown process that causes the detrimental effects. If future research reveals that glutamine aggregates promote cell toxicity, we can d irect research on how to prevent these aggregations to slow down or possibly reverse the course of the disease.2.) How aging in the infected organism influences the progression of Huntingtons diseaseExperiments with C. elegans expressing the age-1 genetic mutation not only had an extended the lifespan, but also had a delayed onset of Huntingtons disease. This suggests that a substance produced as an organism ages can catalyzes the toxicity of Huntingtons disease. With this in mind, except research could hunt for what this aging-related catalyst is. Blocking this substance may slow down or halt the progression of the disease.