Distributions of heat shock protein-70 mRNAs and heat shock cognate protein-70 mRNAs after transient global ischemia in gerbil brain

J. Kawagoe, Koji Abe, S. Sato, I. Nagano, S. Nakamura, K. Kogure

Research output: Contribution to journalArticle

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Abstract

Distributions of heat shock protein (HSP)-70 mRNAs and heat shock cognate protein (HSC)-70 mRNAs after 10 min of transient global ischemia were investigated in gerbil forebrain by in situ hybridization using cloned cDNA probes selective for the mRNAs. Expression of HSP70 immunoreactivity was also examined in the same brains. In hippocampal CA1 neuronal cells, in which only a minimal induction of immunoreactive HSP70 protein was found, the strong hybridization for HSP70 mRNA disappeared at around 2 days before the death of CA1 cells became evident. Furthermore, in hippocampal CA3 cells, a striking induction of HSP70 mRNA was sustained even at 2 days along with a prominent accumulation of HSP70 immunoreactivity. In contrast to the case of HSP70 mRNA, HSC70 mRNA was present in most neuronal cells, especially dense in CA3 cells, of the sham brain. A co-induction of HSP70 and HSC70 mRNAs was observed in several cell populations after the reperfusion with a peak at 8 h, although the magnitude of HSC70 mRNA induction was lower than that of HSP70 mRNA, particularly in CA1 cells. The expression of HSC70 mRNA in CA1 cells also disappeared at around 2 days. All the induced signals of HSP70 and HSC70 mRN As in other cell populations were diminished and returned to the sham level, respectively, by 7 days. These results are the first to show the time courses of distribution of HSP70 and HSC70 mRN As and the immunoreactive HSP70 protein in the same gerbil brain after ischemia. The results suggest that the weak induction of HSP70 protein in CA1 cells, which may relate to the vulnerability of this cell population, is due to both transittional and transcriptional deficits. The different roles inder normal condition and the cooperative role in the recovery process from ischemic injury between HSP70 and HSC70, and the involvement of HSC70 in CA1 cell death, are suggested.

Original languageEnglish
Pages (from-to)794-801
Number of pages8
JournalJournal of Cerebral Blood Flow and Metabolism
Volume12
Issue number5
Publication statusPublished - 1992
Externally publishedYes

Fingerprint

HSC70 Heat-Shock Proteins
HSP70 Heat-Shock Proteins
Gerbillinae
Ischemia
Messenger RNA
Brain
Cell Death
Population
Proteins
Prosencephalon
Brain Ischemia
Reperfusion
In Situ Hybridization

Keywords

  • Cerebral ischemia
  • Gerbil
  • Heat shock cognate protein
  • Heat shock protein
  • In situ hybridization

ASJC Scopus subject areas

  • Endocrinology
  • Neuroscience(all)
  • Endocrinology, Diabetes and Metabolism

Cite this

Distributions of heat shock protein-70 mRNAs and heat shock cognate protein-70 mRNAs after transient global ischemia in gerbil brain. / Kawagoe, J.; Abe, Koji; Sato, S.; Nagano, I.; Nakamura, S.; Kogure, K.

In: Journal of Cerebral Blood Flow and Metabolism, Vol. 12, No. 5, 1992, p. 794-801.

Research output: Contribution to journalArticle

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abstract = "Distributions of heat shock protein (HSP)-70 mRNAs and heat shock cognate protein (HSC)-70 mRNAs after 10 min of transient global ischemia were investigated in gerbil forebrain by in situ hybridization using cloned cDNA probes selective for the mRNAs. Expression of HSP70 immunoreactivity was also examined in the same brains. In hippocampal CA1 neuronal cells, in which only a minimal induction of immunoreactive HSP70 protein was found, the strong hybridization for HSP70 mRNA disappeared at around 2 days before the death of CA1 cells became evident. Furthermore, in hippocampal CA3 cells, a striking induction of HSP70 mRNA was sustained even at 2 days along with a prominent accumulation of HSP70 immunoreactivity. In contrast to the case of HSP70 mRNA, HSC70 mRNA was present in most neuronal cells, especially dense in CA3 cells, of the sham brain. A co-induction of HSP70 and HSC70 mRNAs was observed in several cell populations after the reperfusion with a peak at 8 h, although the magnitude of HSC70 mRNA induction was lower than that of HSP70 mRNA, particularly in CA1 cells. The expression of HSC70 mRNA in CA1 cells also disappeared at around 2 days. All the induced signals of HSP70 and HSC70 mRN As in other cell populations were diminished and returned to the sham level, respectively, by 7 days. These results are the first to show the time courses of distribution of HSP70 and HSC70 mRN As and the immunoreactive HSP70 protein in the same gerbil brain after ischemia. The results suggest that the weak induction of HSP70 protein in CA1 cells, which may relate to the vulnerability of this cell population, is due to both transittional and transcriptional deficits. The different roles inder normal condition and the cooperative role in the recovery process from ischemic injury between HSP70 and HSC70, and the involvement of HSC70 in CA1 cell death, are suggested.",
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