Cellular forms of the rat and human beta-amyloid precursor protein (BAPP).
Using synthetic peptide antisera generated against beta-amyloid precursor protein (BAPP) sequences we demonstrate that the newly synthesized BAPP appears as a 94 kDa peptide in rat brain RNA cell-free translates or polysome runoffs, while from similar human brain material we see two bands at 94 and 120 kDa. Immunoblots reveal likely post-translational modification of BAPP, and possibly an age-dependent, endogenous proteolysis of the protein in rat brain. On human brain immunoblots an unusual post-translational modification or possibly oligomerization of BAPP is seen, particularly in cortical regions.
Anderson
J
J
Fishberg Center for Neurobiology, Mount Sinai School of Medicine, New York, NY 10029.
Wallace
W
W
Snyder
S
S
Haroutunian
V
V
Roberts
J L
JL
Lieberburg
I
I
D000375:Aging / Q000378:metabolism*; D000682:Amyloid / Q000378:metabolism*; D016229:Amyloid beta-Peptides; D000818:Animals; D001921:Brain / Q000378:metabolism*; D006801:Humans; D007106:Immune Sera; D008970:Molecular Weight; D011498:Protein Precursors / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D051381:Rats; D011916:Rats, Inbred F344; D011919:Rats, Inbred Strains
D000682:Amyloid; D016229:Amyloid beta-Peptides; D007106:Immune Sera; D011498:Protein Precursors