Table 1.
M129V polymorphism distribution.
Table 2.
PrPC expression and processing depending on the M129V polymorphism.
Figure 1.
Analysis of PrPC glycosylation.
Immunoblots of PrPC glycoforms from the three PRNP codon 129 genotypes in PBMCs. Denatured lysates from 106 PBMCs were tested by Western Blot analysis using 4 antibodies to span the large PrP region: SAF32 (79–91), 8G8 (95–110), 3F4 (109–112) and PRI 917 (216–221). The 35–37 kDa band corresponds to the M.W. of the diglycosylated protein (D), while the 29–30 kDa and 27–28 kDa bands correspond to the M.W. of the monoglycosylated (M) and unglycosylated (U) proteins respectively. *: Non-specific signal.
Figure 2.
Immunoblots of truncated proteins from the three PRNP codon 129 genotypes in PBMCs. After PNGase treatment, denatured lysates from 106 PBMCs were tested by Western Blot analysis using 4 antibodies to span the large PrP region: SAF32 (79–91), 8G8 (95–110), 3F4 (109–112) and PRI 917 (216–221). The 27–28 kDa band corresponds to the M.W. of the unglycosylated Full-Length (F.L.) protein, while the bands near 20 kDa and 18 kDa correspond to the C2 and C1 fragments, respectively.
Figure 3.
Comparative biochemical analysis between brain and PBMCs.
A) Immunoblots of PrPC glycoforms from PBMCs and brain, Denatured lysates from 106 PBMCs and 10% brain were tested by Western Blot analysis using 2 antibodies: SAF32 (79–91), 3F4 (109–112). The 35–37 kDa band corresponds to the M.W. of the diglycosylated protein (D), while the 29–30 kDa and 27–28 kDa bands correspond to the M.W. of the monoglycosylated (M) and the unglycosylated (U) proteins, respectively. B) Immunoblots of truncated proteins from PBMCs and brain, After PNGase treatment, denatured lysates from 106 PBMCs and brain were tested by Western Blot analysis using 3F4 (109–112). The 27–28 kDa bands correspond to the M.W. of the unglycosylated Full-Length (F.L.) protein while the band near 20 kDa corresponds to the C2 fragment.