Localization of 70-kDa stress protein induction in gerbil brain after ischemia.
Induction of the 70-kDa heat shock protein, hsp70, has been demonstrated in brain following experimental stroke. In the present study, hsp70 was localized in gerbil brain at intervals after transient ischemia using a monoclonal antibody specific for stress-inducible forms of hsp70-related proteins. Induced immunoreactivity was found only in neurons, primarily in hippocampus, striatum, entorhinal cortex and some neocortical regions. Notably hsp70 accumulation was minimal in hippocampal CA1 neurons which die after brief ischemic episodes, but was most pronounced in dentate granule cells and CA3 neurons which are spared. The peak of CA3 immunoreactivity occurred at 48-h recirculation, at the onset of CA1 neuron loss at 2-4 days, demonstrating that hsp70 induction is also a component of this delayed hippocampal pathophysiology rather than a direct response to the metabolic disruption of the initial ischemic episode. These results suggest that hsp70 immunocytochemistry may serve as a marker for neuronal circuitry involved in proposed excitotoxic mechanisms after ischemia and other stresses. Control animals showed immunoreactivity in ependymal cells lining the ventricles, indicating a role for hsp70 in normal functioning of these specialized cells.
Vass
K
K
Laboratory of Neuropathology and Neuroanatomical Sciences, NINCDS, Bethesda, MD 20892.
Welch
W J
WJ
Nowak
T S
TS
D000818:Animals; D000911:Antibodies, Monoclonal; D002545:Brain Ischemia / Q000378:metabolism* / Q000473:pathology; D005260:Female; D005849:Gerbillinae; D006360:Heat-Shock Proteins / Q000378:metabolism*; D008970:Molecular Weight; D013997:Time Factors
D000911:Antibodies, Monoclonal; D006360:Heat-Shock Proteins