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Förslaget inkom 2011-01-05

Unraveling the mystery of clinical variations in “Skellefteå-sjukan”

OBS! ANSÖKNINGSTIDEN FÖR DETTA EXJOBB HAR LÖPT UT.
Amyloidoses are a group of diseases where proteins are aggregated and form a matter called amyloid. This is deposited in tissues, which leads to a slow but progressive destruction of the tissue. Alzheimer’s disease, where the peptide A-beta is deposited as amyloid in the brain, is probably the most well known of the amyloid diseases, but many other peptides and proteins can also form amyloid.
In our group we work with systemic amyloidoses. This is a class of amyloid diseases where the proteins involved are deposited in large amounts throughout the body causing destruction of different organs, which eventually leads to death. I work with an inherited form that is caused by a mutation in the gene coding for transthyretin (TTR), a transporter protein circulating in the blood. The main feature of the disease is a slow degeneration of peripheral nerves, leading to severe disturbances of the sensory motor and autonomic systems, but inner organs are also commonly affected. Death occurs after 10-15 years. The specific clinical manifestations differ considerably between patients with different mutations but interestingly also between patients having the same mutation. The disease onset varies greatly as well; from 20 years of age up to any age. Our group is trying to figure out the reason behind such large differences in phenotype between patients.

Methods used are:
Common protein techniques like gel electrophoresis, western blotting,
mass spectrometry, protein purification methods and immunohistochemistry .


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