D. Dewar et Da. Dawson, CHANGES OF CYTOSKELETAL PROTEIN IMMUNOSTAINING IN MYELINATED FIBER TRACTS AFTER FOCAL CEREBRAL-ISCHEMIA IN THE RAT, Acta Neuropathologica, 93(1), 1997, pp. 71-77
Breakdown of the cytoskeleton has been proposed to be a central event
in the evolution of ischaemic brain damage. Alterations in the immunos
taining of cytoskeletal proteins, particularly microtubule-associated
protein (MAP) 2, have been suggested to be sensitive markers of ischae
mic damage in the somatodendritic compartment. However, axons are also
subjected to the adverse conditions created by an ischaemic challenge
, but MAP2 is not located in the axonal compartment. The purpose of th
e present study was to examine immunostaining of beta-tubulin, MAP1a a
nd MAP5, all of which are located in axons as well as perikarya, speci
fically in myelinated fibre tracts in rats subjected to unilateral mid
dle cerebral artery (MCA) occlusion. In sham-operated control rats imm
unostaining of all three antibodies in myelinated fibre tracts had a s
mooth, regular appearance. Two hours after MCA occlusion there were st
riking changes in the patterns of immunostaining of all three antibodi
es in myelinated fibre tracts within the MCA territory. These were par
ticularly noticeable in beta-tubulin- and MAP5-stained sections where
the pattern in white matter had a rough, globular appearance. This pat
tern was accentuated at 6 h after MCA occlusion and the presence of ''
bulb-like'' profiles in white matter tracts was notable particularly i
n the MAPS-stained sections. Thus, the changes in the patterns of stai
ning at 2 h after MCA occlusion may represent the early stages of axon
al disconnection, and immunostaining of microtubular proteins may repr
esent a sensitive method to assess ischaemically induced damage to mye
linated fibre tracts.