Heat shock protein 70 in rat liver with necrosis and regeneration induced by thioacetamide.

Heat shock protein (hsp), which changes both its concentration and localization in reaction to stresses such as heating, ischemia, etc., is thought to protect protein structure and act as a chaperone in intracellular transportation. We examined one of the hsps, hsp 70, in rat liver with necrosis and regeneration produced by thioacetamide (TAA). Hsp 70 was determined by immunoblotting and detected histologically by immunostaining, using a specific antibody. Generally, hsp 70 moves from the cytosol to the nucleus, where it concentrates 15 min after TAA injection. After 15 min, hsp 70 was not detected in the nuclei of hepatocytes around the central vein, where the hepatocytes later became necrotic. However, hsp 70 immunostaining was increasingly strong in the nuclei of hepatocytes around the portal area, which did not become necrotic. These findings show that, in acute necrosis, hsp 70 seems to correlate with nuclear protection or with the transportation of some protein from the cytosol to the nucleus. Hepatocytes probably neither survive nor regenerate without hsp 70 in their nuclei.