ABSTRACT
AMed or medin amyloid is the most common form of senile amyloid found with an occurrence of almost 100% in the population above fifty years of age. Medin is a 50-amino acid long internal fragment of the precursor protein lactadherin. Lactadherin is a 46 kD large protein composed of 364 amino acids. It contains three different domains; an EGF-like domain in the N-terminus and coagulation factor V- and VIII-like domains in the C-terminus. Uteri smooth muscle cells were cultured in 48-well-plates in 200 µl of Dulbecco’s modified eagle’s medium supplemented with 10% FBS, L-glutamine, and penicillin/streptomycin and incubated at 37°C in a 5% CO2 atmosphere. The morphology of uteri smooth muscle cells was greatly affected by medin. Cells in the control looked more healthy and were more homogenous. Degradation of the extracellular matrix components elastin and collagen has been implicated in many vascular diseases, such as aortic aneurysm and dissection.
