Abstract

The heat shock transcription factor HSF1 mediates the induction of heat shock genes in response to temperature elevation and other traumatic events. The induced hsps play roles in cellular repair and protective mechanisms. Immunocytochemistry revealed that in the unstressed rat, HSF1 was already prepositioned in the nucleus at abundant levels in both neuronal and glial cell types. Following a fever-like temperature, glial cells rapidly induced hsp70 whereas populations of large neurons did not. The lack of hsp70 induction in these neurons in vivo did not appear to be due to deficiencies in levels of nuclear HSF1. During postnatal development of the cerebellum, levels of HSF1 increased progressively from day 1 to 30. Members of the hsp gene set are also constitutively expressed in the unstressed animal and play roles as molecular chaperones. HSF2, which has been proposed as a developmental regulator of constitutive heat shock gene expression, demonstrated a developmental alteration in cellular localization, namely a nuclear distribution in neurons at postnatal day 2 and a cytoplasmic localization at day 30. During postnatal development the overall levels of neural HSF2 declined. This profile showed no obvious correlation with previously observed levels of constitutive hsp expression during postnatal neural development.

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