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http://www.chemistry.ucsc.edu/~fink/200lecture/lecture17.htm
Here is some more information!
NEUROSCIENCE: NEURON INCLUSION BODIES AND DISEASE
The following points are made by Harry T. Orr (Nature 2004 431:747):
1) Neuropathologists have long known that some disorders are characterized by an abnormal accumulation of macromolecules inside cells. These "inclusion bodies" are found, for example, in the brains of patients suffering from Alzheimer's disease, prion diseases, amyotrophic lateral sclerosis (also known as Lou Gehrig's disease), Parkinson's disease, and a group of nine so-called polyglutamine diseases, of which Huntington's disease is the most widely known. The common factor in polyglutamine diseases is a genetic mutation that produces abnormal repeats of the amino-acid glutamine in the encoded protein, with more repeats being more pathogenic.
2) With the advent of studies by molecular geneticists and cell biologists, it became clear that, in the inherited forms of each of these diseases, inclusion bodies contain the protein encoded by the gene containing the disease-causing mutation. These observations reignited long-standing questions of whether and how the inclusions contribute directly to the disease process.(1) The debate has had especial intensity where polyglutamine diseases, and Huntington's disease in particular, are concerned(2,3). For the polyglutamine diseases, inclusion bodies containing mutant protein sprang to public attention in a series of papers(2-5) that appeared in 1997. In the case of Huntington's disease, the critical protein is called huntingtin (htt), and inclusions containing mutant htt are found at the major site of neurodegeneration, the medium spiny neurons in a brain region called the striatum.
3) Depending on the system and the manipulations performed, over the years the experimental evidence has been interpreted as showing that the inclusion bodies cause disease, protect against disease, or are simply incidental. The largest contingents are those who believe that inclusions are the major pathogenic species, owing to their ability to absorb other critical cellular proteins, and those who feel inclusions are protective, in that they sequester mutant protein out of harm's way. Resolution of this issue is necessary for many reasons, not least because many current studies aim to interfere with inclusion-body formation as a potential treatment for Huntington's disease and the other neurodegenerative disorders characterized by protein aggregates.
4) Arrasate et al(1) have devised a real-time technique for assessing the factors that affect the risk of neuron death in culture. They used a common model of Huntington's disease in which striatal neurons are transiently transfected with a pathogenic fragment of mutant htt (htt-exon1). They developed an automated microscopic system to simultaneously follow inclusion-body formation, the presence of diffuse htt and cell survival in the same neuron over a period of days. To visualize deposition of htt in transfected cells, they employed a construct of htt-exon1 fused with green fluorescent protein. As expected, inclusion bodies formed, in the nucleus and in the cytoplasm, and neurons died. However, inclusion-body formation actually prolonged survival and protected neurons, seemingly by reducing the amount of a toxic, diffusely distributed form of mutant htt.
References (abridged):
1. Arrasate, M., Mitra, S., Schweitzer, E. S., Segal, M. R. & Finkbeiner, S. Nature 431, 805-810 (2004)
2. Davies, S. W. et al. Cell 90, 537-548 (1997)
3. Paulson, H. L. et al. Neuron 19, 333-344 (1997)
4. Skinner, P. J. Nature 389, 971-974 (1997)
5. DiFiglia, M. et al. Science 277, 1990-1993 (1997)
