TY - JOUR
T1 - Intracellular localization of constitutive and inducible heat shock protein 70 in rat liver after in vivo heat stress
AU - Čvoro, Aleksandra
AU - Korać, Aleksandra
AU - Matić, Gordana
PY - 2004
Y1 - 2004
N2 - The level and intracellular redistribution of the two nucleo-cytoplasmic members of 70 kDa heat shock protein family (constitutive, Hsc70 or Hsp73, and inducible, Hsp72) were studied in rat liver during a 24-h period after exposure of the animals to 41 °C whole body hyperthermic stress. The examined proteins were detected in the liver cytosol and nuclei by Western blotting and immunohistochemical staining of paraffin sections, as well as by immnocytochemical staining of isolated nuclear smears. All three techniques applied were based on the use of monoclonal antibodies recognizing both constitutive and inducible Hsp70 isoforms or only the inducible isoform, and gave consistent results. The exposure of the animals to in vivo heat stress was shown to induce the synthesis of otherwise non-existing Hsp72, rendering Hsc70 level unchanged in comparison to unstressed controls. However, immediately after the stress the intracellular redistribution of Hsc70, i.e. its nuclear accumulation, was observed. The maximal level of Hsp70 both in the cytoplasm and in the nuclei was registered 5 h after the stress, which coincided with the maximal level of Hsp72 induction. The alterations in the level and intracellular distribution of examined proteins were still noticeable 24 h after the stress. The results of this study could shed some more light on, as yet uncertain, differences between cellular functions of these two proteins, as well as on the role of the constitutive form under normal and stress conditions.
AB - The level and intracellular redistribution of the two nucleo-cytoplasmic members of 70 kDa heat shock protein family (constitutive, Hsc70 or Hsp73, and inducible, Hsp72) were studied in rat liver during a 24-h period after exposure of the animals to 41 °C whole body hyperthermic stress. The examined proteins were detected in the liver cytosol and nuclei by Western blotting and immunohistochemical staining of paraffin sections, as well as by immnocytochemical staining of isolated nuclear smears. All three techniques applied were based on the use of monoclonal antibodies recognizing both constitutive and inducible Hsp70 isoforms or only the inducible isoform, and gave consistent results. The exposure of the animals to in vivo heat stress was shown to induce the synthesis of otherwise non-existing Hsp72, rendering Hsc70 level unchanged in comparison to unstressed controls. However, immediately after the stress the intracellular redistribution of Hsc70, i.e. its nuclear accumulation, was observed. The maximal level of Hsp70 both in the cytoplasm and in the nuclei was registered 5 h after the stress, which coincided with the maximal level of Hsp72 induction. The alterations in the level and intracellular distribution of examined proteins were still noticeable 24 h after the stress. The results of this study could shed some more light on, as yet uncertain, differences between cellular functions of these two proteins, as well as on the role of the constitutive form under normal and stress conditions.
KW - Hsc70
KW - Hsp70
KW - Hsp72
KW - Rat liver
KW - in vivo heat stress
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U2 - 10.1023/B:MCBI.0000044312.59958.c8
DO - 10.1023/B:MCBI.0000044312.59958.c8
M3 - Article
C2 - 15543931
AN - SCOPUS:16644385833
VL - 265
SP - 27
EP - 35
JO - Molecular and Cellular Biochemistry
JF - Molecular and Cellular Biochemistry
SN - 0300-8177
IS - 1-2
ER -