Morphofunctional changes in goldfish Mauthner neurons after application of beta-amyloid.
The effects of applying aggregated beta-amyloid peptide fragment 25-35 on the three-dimensional structure and volume of Mauthner neurons (MN) and on motor asymmetry were assessed in goldfish using reconstructions based on serial histological sections. These experiments showed that the motor asymmetry of the fish was stable in the intact state and in controls and correlated tightly with structural asymmetry of neurons. beta-Amyloid produced large changes or inversion in motor asymmetry, which did not coincide with or even contradicted the structural asymmetry of MN. This occurred as a result of marked dystrophy or, conversely, hypertrophy of individual neurons and their individual dendrites, with changes in their proportions. It is suggested that the harmful action of beta-amyloid on MN structure and the discordant ("incorrect") behavior of the fish may result from mechanical deformation evoked by its tape-like fibrils. Overall, the results lead to the conclusion that MN provide a suitable system for studying the structural aspects of amyloidosis.
Kokanova
N A
NA
Neuron Ultrastructure Laboratory, Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Pushchino, Russia. kokanchik@rambler.ru
Mikhailova
G Z
GZ
Shtanchaev
R Sh
RSh
Tiras
N R
NR
Bezgina
E N
EN
Moshkov
D A
DA
D016229:Amyloid beta-Peptides / Q000502:physiology / Q000633:toxicity*; D000818:Animals; D007839:Functional Laterality; D006054:Goldfish; D009046:Motor Neurons / Q000187:drug effects* / Q000473:pathology; D009068:Movement / Q000187:drug effects*; D010446:Peptide Fragments / Q000502:physiology / Q000633:toxicity*
D016229:Amyloid beta-Peptides; D010446:Peptide Fragments; C074636:amyloid beta-protein (25-35)