Exjobbsförslag från företag
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Förslaget inkom 2006-10-13
Is medin amyloid the causing agent when the aorta breaks?
OBS! ANSÖKNINGSTIDEN FÖR DETTA EXJOBB HAR LÖPT UT.
Amyloidoses are protein conformation diseases, where the full-length protein or a peptide forms an insoluble beta-sheet structure aggregate. The aggregate is usually persistent and the accumulation increases over time, often resulting in destruction of the affected organ. Examples of amyloidoses are Alzheimer¿s disease, Diabetes type II and Creutzfeldt-Jacob¿s disease. Among other types of amyloid, our group focuses on the medin amyloid located in the media of the aorta. 97% of the population above 50 years of age are positive for medin. Medin is a 50-aa-long integral peptide of the full-length protein lactadherin. How medin is cleaved out from lactadherin or its effect in the aorta is still unknown. However, we work with the theory that medin amyloid is toxic to the smooth muscle cells of the aorta and because of this is involved in aortic aneurysm and dissection, two potentially lethal conditions that might result in rupture of the aorta.
We are planning to do a cytotoxic in vitro study with recombinant medin and cultured smooth muscle cells. If toxicity is seen the mechanism behind will be examined. Also lactadherin¿s effect in the aorta and how medin is formed will be investigated by different assays. Many functions have been assigned to lactadherin. It has been suggested to act as an inhibitor of coagulation, to be involved in apoptosis and to induce cell proliferation and migration.
Methods used, among others, will be protein purification with affinity chromatography and FPLC, cell culturing, SDS-PAGE, western blotting, different toxicity assays, immunohistochemistry and electron microscopy.
We welcome both 10- and 20-weeks students to our group and the interesting field of amyloidosis.
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