Electrophoretic Analysis of Axonally Transported Proteins in Toad Retinal Ganglion Cells

Publisher Website
Google Scholar
Abstract
To study changes in axonal transport in regenerating neurons, the composition and organization of polypeptides normally axonally transported in a neuronal system capable of regeneration, i.e., the retinal ganglion cells of the toad, B. marinus were studied. Proteins synthesized in the retina were labeled with 35S-methionine and 1-dimensional sodium dodecyl sulfate polyacrylamide gel electrophoresis was used to analyze labeled, transported proteins in tissues containing segments of the axons (the optic nerve, optic tract and optic tecta) of the retinal ganglion cells. The transported polypeptides could be divided into 5 groups according to their apparent transport velocities. Many of the polypeptides of each group were electrophoretically similar to polypeptides of corresponding groups previously described in rabbit and guinea pig retinal ganglion cells and in some cases, additional properties of the polypeptides indicated that the transported materials of the 2 vertebrate classes were homologous. The retinal ganglion cells of the toad B. marinus can be used as a model system to study changes in gene expression related to regeneration. The organization and many aspects of the composition of axonal transport in retinal ganglion cells evidently were conserved in animals as unrelated as amphibians and mammals.