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

Neurodegenerative disorders such as Alzheimers affection and Parkinsons disease atomic number 18 caused by the aggregation of antidromic proteins in neurons. An essential region of cellular function is the correct assimilation of proteins in the cell. Proteins fold into particularized structures and then carry out cellular functions. However, when this folding procedure runs amuck, abnormal proteins are introduced into the cell. In neurodegenerative diseases, these protein aggregates are characterized by having genes which contain too legion(predicate) 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.Through experimentation, this paper attempt to find the threshold fo r the number of CAG repeats that determines whether cellular function will be disrupted by the protein aggregates. Molecular genetic studies have already completed 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 confederacy between the CAG threshold (thus, the polyQ aggregation) and cellular toxicity, a species of worm, Caenorhabditis elegans, was used during experimentation. (C. elegans are proper model organisms to study human neurodegenerative disease not only because C. elegans neurons jibe vertebrate neurons at cellular and molecular levels, still also because umteen 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 aggr egates promote cell toxicity, we can sway research on how to inhibit these aggregations to slow down or perhaps reverse the course of the disease.2.) How aging in the infected organism influences the procession 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, further research could draw for what this aging-related catalyst is. Blocking this substance may slow down or halt the progression of the disease.