title: [Amyloid-like oligomers of presynaptic protein BASP1].
abstract: Brain protein BASP1 forms oligomers that resemble amyloid protein oligomers in some respects, including interaction with conformation-specific antibodies against amyloid oligomers. Aggregation-prone N-terminal myristoylated peptide myr-BASP1 (1-13) forms fibrillar aggregates of amyloid-like structure under physiological conditions in vitro, which is also the evidence of BASP1 similarity to amyloid proteins. Protein cross-linking by glutaraldehyde in situ demonstrated that BASP1 exists on the presynaptic membrane as lipid raft-associated oligomers. In addition, BASP1 is non-toxic to PC12 cells, when applied either as a monomer or oligomer. We conclude that BASP1 oligomer is a non-pathological physiologically relevant functional form of this protein.
authors.forename: O S
authors.initials: OS
authors.lastname: Vitiuk
authors.forename: N Ia
authors.initials: NIa
authors.lastname: Gil'iano
authors.forename: V V
authors.initials: VV
authors.lastname: Zakharov
mesh_terms: D000682:Amyloid / Q000737:chemistry / Q000378:metabolism; D000818:Animals; D001921:Brain / Q000378:metabolism*; D002148:Calmodulin-Binding Proteins / Q000737:chemistry / Q000378:metabolism*; D003598:Cytoskeletal Proteins / Q000737:chemistry / Q000378:metabolism*; D009419:Nerve Tissue Proteins / Q000737:chemistry / Q000378:metabolism*; D016716:PC12 Cells; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism*; D066329:Protein Aggregates; D051381:Rats
chemical_list: D000682:Amyloid; D002148:Calmodulin-Binding Proteins; D003598:Cytoskeletal Proteins; D009419:Nerve Tissue Proteins; D010446:Peptide Fragments; D066329:Protein Aggregates; C066853:Basp1 protein, rat