Fig. 9

Immunoblotting comparison of αsyn species in LBD and AD/ALB amygdala. High salt (HS) and SDS/urea fractions were obtained from the MTL of 5 LBD cases (lanes 1–5), 2 cases of AD/ALB (lanes 6–7), 2 non-synucleinopathy controls (lanes 8–9), and for one LBD case the amygdala was specifically isolated (lane 10). 20 μg of lysate for each case and fraction were subject to western blot analysis using a panel of 4 antibodies which are indicated. In the HS fraction, all antibodies predominantly revealed full-length (FL) αsyn in all cases. In the SDS/Urea fractions, monomeric FL αsyn is present in high amounts for 4/5 LBD cases (lanes 2, 3, 4, 5, and 10); 1 LBD and 1 AD/ALB case (lanes 1 and 7, respectively) have an intermediate amount of FL αsyn in this fraction and 1 AD/ALB case along with 2 controls (lanes 6, 8, and 9) have very little FL αsyn in this fraction. For the LBD cases, 2 prominent truncation bands are present for all antibodies except for C-terminal antibody 94-3A10 suggesting these are carboxy-truncated forms of αsyn (T1 and T2) in the SDS/urea fractions from the MTL in LBD but not controls or AD/ALB; the truncation bands are strongest in the LBD amygdala. Additional higher molecular mass bands are prominent in LBD cases (M1 and M2); these bands are less visible in AD/ALB or controls. The relative mobilities of molecular mass protein markers are identified on the left of the blots