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  • Title: The composition and organization of axonally transported proteins in the retinal ganglion cells of the guinea pig.
    Author: Levine J, Willard M.
    Journal: Brain Res; 1980 Jul 21; 194(1):137-54. PubMed ID: 6155179.
    Abstract:
    We labeled the proteins of guinea pig retinal ganglion cells with [35S]methionine and analyzed the axonally transported polypeptides by means of sodium dodecyl sulfate gel electrophoresis. Five groups of transported polypeptides could be distinguished by their characteristic times of initial appearance in segments of the axons of the retinal ganglion cells. The times of initial appearance of the groups corresponded to maximum transport velocities ranging from greater than 200 mm/day to 0.5 mm/day. We directly compared these transported polypeptides to polypeptides undergoing axonal transport in the retinal ganglion cells of the rabbit. Electrophoretically similar polypeptides were transported at the same relative velocities in the two animals. Our results lead to the following conclusions. (1) The basic composition and organization of axonally transported proteins is probably a general constant feature of mammalian retinal ganglion cells, implying that the correct organization is important for the proper functioning of these neurons. Therefore, the results obtained by the analysis of individual model systems should have general significance. (2) Four discontinuities in the transport process (in addition to the 5 discontinuities represented by the major transport groups) were revealed by a consideration of subtle differences between the rabbit and guinea pig, as well as differences in the rate of disappearance of label from individual polypeptides within each transport group. (3) The guinea pig should provide a useful model system for studying axonal transport, especially for immunological studies, since antibodies against axonally transported proteins of the guinea pig can be conveniently prepared in the rabbit. (4) While the structure (as reflected by electrophoretic mobility) of most major axonally transported polypeptides appears to be conserved over the evolutionary period (about 30 million years) separating two orders of mammals, the electrophoretic mobility of one neurofilament-associated polypeptide, H, was abnormally variant between the two species.
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