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Query: UMLS:C0022116 (ischemia)
 91,303 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Thresholds of induction of heat shock protein (HSP) 70 and heat shock cognate protein (HSC) 70 mRNAs after transient global ischemia in gerbil brain were investigated by in situ hybridization using cloned cDNA probes selective for each mRNA species. In sham control brain, HSP70 mRNA was little present, while HSC70 mRNA was present in most cell populations. A 0.5-min occlusion of bilateral common carotid arteries did not affect the amount of HSP70 and HSC70 mRNAs. The selective induction of HSC70 mRNA was observed in dentate granule cells at 1 h, and in most cells of hippocampus especially dentate gyrus at 3 h after 1 min of ischemia when induction of HSP70 mRNA was not evident in the identical brain. The selective induction diminished by 2 days. However, after 2 min of ischemia, HSP70 and HSC70 mRNAs were induced together in hippocampal cells from 1 h of the reperfusion, and the co-induction prolonged in CA1 cells until 2 days. Body temperatures monitored at rectum increased after the reperfusion with a peak at 30 min. The degree of increase of the body temperature was significantly higher in the case after 2-min ischemia than in the cases after 0.5- and 1-min ischemia. Although HSP70 and HSC70 mRNAs are generally co-induced in stressful conditions, our results suggest the different thresholds of the induction between HSP70 and HSC70 mRNAs after transient brain ischemia. The selective induction of HSC70 mRNA which is not accompanied by the induction of HSP70 mRNA may relate to the differences of the duration of ischemia and the degree of the increase of body temperature after ischemia.
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PMID:Different thresholds of HSP70 and HSC70 heat shock mRNA induction in post-ischemic gerbil brain. 129 Oct 30

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 mRNAs 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 mRNAs and the immunoreactive HSP70 protein in the same gerbil brain after ischemia.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Distributions of heat shock protein-70 mRNAs and heat shock cognate protein-70 mRNAs after transient global ischemia in gerbil brain. 150 43

The distribution of heat shock protein (HSP) 70 and heat shock cognate protein (HSC) 70 mRNA after 30 min of middle cerebral artery (MCA) occlusion was investigated in rat brain by in situ hybridization using cloned cDNA probes selective for the mRNAs. While HSP70 mRNA was hardly present at caudate and dorsal hippocampal levels of the sham brain this mRNA was greatly induced in cells of the MCA territory 1 h after reperfusion. Although the maximum amount of induced HSP70 mRNA in the caudate was much smaller than that in the cortex the maximum induction in the caudate (3 h) preceded that in the cortex (8 h). In contrast to the case of HSP70 mRNA, HSC70 mRNA was present in most cells of the sham brain, and was especially dense in hippocampal CA3 cells. Further induction of HSC70 mRNA was observed after reperfusion in the same cell populations, as in the case of HSP70 mRNA. HSC70 mRNA levels were significantly reduced in the caudate at 8 h when small amounts of HSP70 mRNA were still elevated. In the ipsilateral granule cells of the dentate gyrus and hippocampal CA3 cells a slight but significant induction of HSC70 mRNA was observed from 1 h to 1 day, while obvious induction of HSP70 mRNA never occurred. All the induced signals of HSP70 and HSC70 mRNA were diminished or returned to the sham level by 7 days, except for HSC70 mRNA in the caudate. These results are the first observations of the distribution of HSP70 and HSC70 mRNA after transient focal ischemia of rat brain.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Distributions of heat shock protein (HSP) 70 and heat shock cognate protein (HSC) 70 mRNAs after transient focal ischemia in rat brain. 152 56

Hyperthermia induces the synthesis of the 71-kDa heat-shock protein (heat-shock response) in all rat tissues, including heart. We examined whether induction of the heat-shock response alters the response of isolated hearts to ischemia and reperfusion. Anesthetized male rats were pretreated with 15 min of hyperthermia (42 degrees C) and then recovered for 0, 24, 48, 96, or 192 h. Hearts were isolated from control and hyperthermia-treated rats and retrogradely perfused. Greatest recovery occurred in 48-h postheat-shock hearts; after 30 min of reperfusion there was a 38, 62, and 62% recovery of force, +dF/dt, and -dF/dt, respectively, and 17, 36, and 30% recovery, respectively, for the control hearts. Creatine kinase efflux during reperfusion was reduced by 75% for 24-h postheat-shock hearts. The antioxidative enzyme catalase was increased 24, 48, and 96 h posthyperthermia. Treatment of rats with 3-amino-1,2,4-triazole (1 g/kg body wt), which irreversibly inactivates catalase, 30 min before isolation of hearts, abolished the hyperthermia-induced enhancement of postischemic recovery. These results show a strong relationship between the acquisition and decay of the enhanced postischemic ventricular recovery and the hyperthermic induction of the heat-shock response indicated by the accumulation of heat-shock protein HSP71 (mol mass 71 kDa) and the increase in catalase activity.
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PMID:Acquisition and decay of heat-shock-enhanced postischemic ventricular recovery. 238 21

We examined rat kidneys for serial expressions of two major heat-shock proteins (HSPs), HSP73 and HSP90, after 60 min of unilateral renal ischemia up to day 28. Immunohistochemical studies showed that HSP73 and HSP90 were rapidly induced in the cytoplasm of injured epithelial cells of the S3 segment of proximal tubules and were again induced in the cytoplasm of regenerative cells in this segment from day 3. In epithelial cells of the Henle's loops, HSP90 was also induced in the cytoplasm of both injured and regenerative cells, but HSP73 was not induced in this portion. Furthermore, a transient accumulation of HSP73 into the nucleus was observed in epithelial cells of papillary collecting ducts shortly after ischemia. Serial immunoblot analysis of isotonic buffer extractable fractions from ischemic kidneys revealed the induction of both HSP73 and HSP90 in the degenerative and regenerative phases: the maximal inductions in the two phases were at 3-6 and on days 5-7, respectively. These results demonstrate that HSP73 and HSP90 are induced in injured tubular epithelial cells with a regional heterogeneity during the degenerative and regenerative phases after renal ischemia and suggest that these HSPs are involved in the process of postischemic cellular recovery.
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PMID:Induction of heat-shock proteins HSP73 and HSP90 in rat kidneys after ischemia. 756 12

Induction of heat shock protein (HSP) 70 and heat shock cognate protein (HSC) 70 mRNAs, and immunoreactivity for HSP70 were investigated in rat hippocampus after transient global ischemia with in situ hybridization and immunohistochemistry. In sham control brain, HSP70 mRNA was scarcely present, while HSC70 mRNA was expressed in most neuronal cells. After 20 min of transient four-vessel occlusion (4VO), ischemia-resistant hippocampal CA3 cells consistently induced HSP70 mRNA along with further HSC70 mRNA. The resistant dentate granule (DG) cells continuously induced HSC70 mRNA even after the great reduction of HSP70 mRNA. In contrast, in ischemia-vulnerable CA1 cells, a relatively lower level of HSC70 mRNA induction than the level of HSP70 mRNA induction was observed. The vulnerable CA1 cells produced a prominent HSP70 immunoreactivity. These results suggest that the vulnerability of the CA1 cells after transient ischemia may not be explained only by the ability of HSP70 induction, but may be related to the imbalance of HSP70 and HSC70 mRNA inductions.
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PMID:Regional difference of HSP70 and HSC70 heat shock mRNA inductions in rat hippocampus after transient global ischemia. 768 48

Vulnerability of aged hearts to ischemia may be due to defects in protective mechanisms provided by heat shock proteins (HSPs). To determine whether there is a defect in the induction of HSPs by ischemia in old hearts, HSP72 and HSP73 (inducible and constitutive HSP70, respectively) mRNA induction was examined in young (2-mo-old; n = 36) and old (18-mo-old; n = 32) rat hearts. Transient (10- or 20-min) ischemia was applied by tightening a snare placed around left coronary arterial branches 3 days before examination to avoid the effect of operation on induction. HSP72 mRNA was induced markedly in young hearts after 10-min ischemia, peaked at 2 h, but was induced only slightly in old hearts. HSP73 mRNA was also induced in young hearts, peaked at 4 h, but was not induced in old hearts. The mRNAs were markedly induced in old hearts as well after 20-min ischemia, which was accompanied by the induction of HSP72 protein. Thus the age-related modulation of HSP72 and HSP73 mRNAs suggests a defective sensing mechanism for ischemia in old hearts.
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PMID:Diminished heat shock protein 70 mRNA induction in aged rat hearts after ischemia. 797 10

Inductions of mRNAs for heat shock protein (HSP) 70 and heat shock cognate protein (HSC) 70 were examined in the cerebral cortex, cerebellum, heart, lung, kidney, and liver of gerbils after a 10-min transient forebrain ischemia. HSP70 mRNA was normally expressed in a small amount in the cerebellum, lung, and kidney, but was not expressed in the heart or liver in a detectable amount. A very small amount of HSP70 mRNA was also present in the cerebral cortex. HSC70 mRNA was normally present in all the organs examined with a variety in the amount. Eight hours after the cerebral ischemia, the level of HSP70 mRNA increased in the cerebral cortex, lung, and kidney. HSC70 mRNA levels also increased in all the organs. However, the increase of HSC70 mRNA was remarkable in the heart. Transient cerebral ischemia caused subsequent hyperthermia. Treatment of gerbils with an artificial hyperthermia without cerebral ischemia increased the HSP70 and HSC70 mRNA levels as well. However, the HSC70 mRNA level in the heart after cerebral ischemia was much higher than that in the case with hyperthermic treatment. These results suggest that HSC70 mRNA was preferentially induced in the heart after transient forebrain ischemia that was not only due to the subsequent hyperthermia.
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PMID:Preferential expression of HSC70 heat shock mRNA in gerbil heart after transient brain ischemia. 826 47

To evaluate the mechanism of tolerance to ischemia, inductions of heat shock protein (HSP) 70 and heat shock cognate protein (HSC) 70 mRNAs in gerbil hippocampus were compared with in situ hybridization between cases of a single 3.5-min period of forebrain ischemia and a 3.5-min period of ischemia 2 days after 2-min pretreatment with ischemia. Immunohistochemistry for HSP70 protein and morphological studies were also performed in the same brains up to 7 days after the reperfusion. Following a single 3.5-min period of ischemia, HSP70 and HSC70 mRNAs were induced in all hippocampal cells. However, the hippocampal CA1 cells produced only a minimum of HSP70 protein, and the cells were almost lost by 7 days. Following 3.5 min of ischemia after 2-min pretreatment, large populations of the CA1 cells survived at 7 days. The peak time of the HSP70 and HSC70 mRNA induction shifted to an earlier period of reperfusion in all hippocampal cells as compared with the case of a single episode of ischemia. The peak of HSP70 and HSC70 mRNA induction shifted from 1 day to 3 h in the CA1 cells. The CA1 cells produced strongly immunoreactive HSP70 from 3 hr to 2 days. These results suggest that pretreatment with an initial period of ischemia (for 2 min) accelerated HSP70 and HSC70 gene expression at the transcriptional level, ameliorated the translational disturbance of HSP70 mRNA to protein, and saved the CA1 cells from subsequent lethal ischemia (for 3.5 min). These changes of heat shock gene expression might play important roles in the acquisition of ischemic tolerance of hippocampal CA1 neurons.
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PMID:Acceleration of HSP70 and HSC70 heat shock gene expression following transient ischemia in the preconditioned gerbil hippocampus. 836 Feb 84

The effect of bifemelane hydrochloride (BFH) on the induction of heat shock protein (HSP) 70 and heat shock cognate protein (HSC) 70 mRNAs after transient global ischemia in gerbil brain was investigated by in situ hybridization using cloned cDNA probes selective for each mRNA species. Following 3.5 min of ischemia, HSP70 and HSC70 mRNAs were induced in all hippocampal cells. The CA1 cells were almost lost by 7 days. Treatment with BFH twice before and after ischemia (total 60 mg/kg, i.p.) reduced the induction of HSP70 and HSC70 mRNAs both at 8 h and 1 day of the reperfusion, and about half of the CA1 cells survived at 7 days. Thus, the reduction of HSP70 and HSC70 mRNA inductions after ischemia may suggest that BFH reduced intra- and/or post-ischemic stress, and protected CA1 cells from ischemic damage.
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PMID:Reduction of HSP70 and HSC70 mRNA inductions by bifemelane hydrochloride after transient ischemia in gerbil brain. 836 50


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