BASPl - an Axon Terminal Protein Forming Amyloid-Like Oligomers

摘要

Brain protein BASP1 forms oligomers similar to amyloid protein oligomers in terms of a series of parameters, including the interaction with conformation-specific antibodies to amyloid oligomers. The N-terminal myristylated peptide myr-BASPl(l-13), responsible for protein aggregation, forms fibrils of amyloid structure in physiological conditions in vitro, which is also evidence of similarity between BASP1 and amyloid proteins. Glutaraldehyde linking studies showed that BASP1 is present on presynaptic membranes in the rat brain as oligomers. In addition, BASP1 oligomers were not toxic to PC12 cells. These data provide evidence that BASP1 oligomers can be regarded as the nonpathological functional form of this protein.