Abstract

Previous light microscopic immunocytochemical studies using two monoclonal antibodies that recognise alpha-tubulin (YOL/34 and YL1/2) but differ in their isotypic specificity have shown that the unmyelinated parallel fiber axons in the cerebellar cortex are labeled with only one of the antibodies (YOL/34). We now show that at 10 d postnatally the parallel fibers are labeled with both antibodies, and that during development YL1/2 (but not YOL/34) immunoreactivity disappears progressively from parallel fibers in the lower regions of the molecular layer upwards towards the external germinal layer. By approximately 28 d postnatally, the differential staining pattern of parallel fibers by the antibodies is established throughout the molecular layer. The time course, light microscopic, and ultrastructural staining distribution corresponds to a progressive change in alpha-tubulin immunoreactivity as the parallel fibers form synaptic contacts. This modification of alpha-tubulin (which was not observed in Purkinje cell dendrites or Bergmann glia) may be related to the formation of a basic isotype of alpha-tubulin within parallel fiber axons at maturation.

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