Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0022116 (ischemia)
 91,303 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We immunohistochemically investigated the induction and localization of a low-molecular weight stress protein, HSP27, in the rat brain following 1 hr of middle cerebral artery occlusion in comparison with those of HSP70. The brains were perfusion-fixed after 4 h, 1 day, 3 days, 7 days, and 14 days of reperfusion. Frozen sections were then prepared and used for immunohistochemistry. In normal brains, we observed no immunoreactivities to HSP70 and HSP27. HSP70 was localized predominantly in neurons in areas peripheral to the ischemic center after 1 day and 3 days, and in endothelial cells and perivascular cells within the ischemic center after 1 day. In contrast, HSP27 was induced in microglia in the ischemic center after 4 h, and then in reactive astrocytes distributed widely in the ipsilateral hemisphere and in part of the contralateral hemisphere after 1 through 14 days. In the center of ischemia where infarction developed, only nonspecific staining was seen. Thus, the expression patterns of HSP70 and HSP27 were quite different with regard to cell type, distribution, and time course following focal cerebral ischemia. HSP70 may be a sensitive marker of acute neuronal stress in the penumbral areas, whereas HSP27, which was most prominently induced in reactive astrocytes in periischemic and remote areas, may be a component of glial reaction to injury.
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PMID:Immunohistochemical localization of the low molecular weight stress protein HSP27 following focal cerebral ischemia in the rat. 764 52

We report here the time-dependent expression of several classes of HSP mRNAs following focal cerebral ischemia in rats. HSP70, GRP78, HSP27, HSP90 and HSP47 have been reported to possess distinct functions under normal and/or stress conditions. These different classes of HSP mRNAs were differentially induced by ischemia, as determined by Northern blot analysis. Messenger RNAs of the HSP70 family proteins were induced within 4 h after ischemia and then rapidly decreased, whereas HSP27 and HSP47 mRNAs reached a maximum level of expression at 24 h and 48 h after ischemic treatment, respectively. In situ hybridization showed that the expression of inducible HSP70 mRNA was observed predominantly in regions adjacent to the ischemic core except during the early periods of ischemia. HSP27 mRNA was expressed over a broad area of the ipsilateral cerebral neocortex except for the ischemic center 24 h after ischemia. The unique induction kinetics for each HSP mRNA species may reflect their distinct roles in the brain during various physiological stresses. We will also discuss that stress proteins may be involved in the central nervous system after ischemia in two important aspects: early protection against stress and restoration of damaged lesions in the brain at later stages after ischemia.
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PMID:Differential induction of mRNA species encoding several classes of stress proteins following focal cerebral ischemia in rats. 795 88

Preconditioning the brain with sublethal cerebral ischemia induces tolerance to subsequent lethal periods of ischemia (ischemic tolerance). The purpose of this study is to investigate the role of low-molecular weight stress proteins, 27-kDa heat shock protein (HSP27) and alpha B crystallin, in ischemic tolerance. We measured the content of these proteins with enzyme immunoassay in the rat hippocampus and cerebral cortex following 6 min of ischemia with and without preconditioning with 3 min of ischemia and 3 days of reperfusion. We also visualized the localization of HSP27 immunohistochemically in comparison with that of HSP70. A 3-min period of ischemia caused a 2.4-fold increase in HSP27 content in the hippocampus after 3 days. Immunohistochemical localization of HSP27 was found in glial cells in all subregions of the hippocampus, whereas HSP70 immunostaining was seen only in CA1 pyramidal neurons. HSP27 content in the hippocampus decreased 2 h after 6 min of ischemia. HSP27 content progressively increased in the unpreconditioned hippocampus after 1 and 3 days, but returned to preischemic levels in the preconditioned hippocampus. HSP27 and HSP70 immunostaining was seen in CA1 pyramidal neurons after 1 day both with and without preconditioning. After 3 and 7 days, an intense HSP27 staining was observed in reactive glial cells in the CA1 without preconditioning, whereas the staining decreased in the preconditioned hippocampus. HSP70 staining was seen only in neurons at these time points. We observed no significant changes in HSP27 content in the cerebral cortex although neurons in the third and fifth layers were immunostained after 1 and 3 days. We observed no alterations in alpha B crystallin content after ischemia both in the hippocampus and the cortex. The present study demonstrated that cerebral ischemia induces HSP27 expression but not alpha B crystallin. Both HSP27 and HSP70 induction had a good temporal correlation with the induction of ischemic tolerance. However, different sites of action were suggested because the localization and cell types of HSP27 induction were quite different from those of HSP70 induction. The result suggests that it is unlikely that HSP27 is directly involved in the protection afforded by ischemic preconditioning.
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PMID:Induction of 27-kDa heat shock protein following cerebral ischemia in a rat model of ischemic tolerance. 813 Oct 73

Heat shock proteins (HSPs), which have been shown to be induced in the kidney by a variety of stress conditions, including ischemia, inflammation, oxidative stress, and toxin exposure, are believed to protect the cells from injury. In the present study, we demonstrated that administration of vasopressin i.v. to Wistar rats leads to HSP70 induction in the kidney. The effect was specific to the kidney (i.e., absent in brain, heart, lung, muscle, etc.) and selective for the HSP70 gene family (HSP27, HSP60, and HSP90 were not induced). Western blot analysis demonstrated that HSP70 protein expression peaked between 6 and 12 hours after vasopressin administration. Immunohistochemical staining revealed that induction was localized to renal tubule lining cells, with no expression seen in glomerular or interstitial regions. The elevated protein levels were preceded by the induction of HSP70 mRNA within 30 minutes after vasopression injection. The induction of HSP70 mRNA was associated with the activation of heat shock transcription factor 1 (HSF1), suggesting that the response was regulated at the level of transcription. This HSP70 expression was completely blocked in the presence of both a general vasopressin receptor antagonist (V1 and V2 receptors) and an antidiuretic antagonist (V2), but not in the presence of a vasopressor antagonist (V1). These observations could be significant for understanding the possible involvement of HSP70 in physiological processes of the kidney, as well as pathophysiologic conditions associated with either elevated or deficient levels of vasopressin.
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PMID:Vasopressin-induced heat shock protein expression in renal tubular cells. 856 80

Heat shock proteins present a complex family of proteins exerting chaperone-like activities that are classified according to their molecular weight. We especially explored protective functions of inducible heat shock protein 70, the mitochondrial heat shock protein 60 and 10, and the small heat shock proteins HSP27 and alphaB-crystallin against ischemic, reoxygenation-mediated injury using transgenic animals and hearts under in vivo conditions and in isolated cardiac myocyte-derived cells using adenoviral vectors. We noted with great interest that differential protective effects are exerted by specific hsps. For example, alpha-B-crystallin and constitutive hsp70 markedly protect microtubular structure in cardiac myocytes from ischemia-induced injury. Inducible hsp70, hsp60 and hsp10 when coexpressed, and hsp27 and alphaB-crystallin have an overall protective effect against ischemic injury as determined by the release of enzymes like creatine kinase and LDH. We did not note inflammatory or immune responses elicited by the expression of hsps in transgenic animals and cardiac myocytes. The specific cell types in which hsps are expressed may contribute to the protective effect of hsps versus their inflammatory and immunogenic effects when expressed in other cell types.
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PMID:Heat shock proteins and protection against ischemic injury. 1023 Oct 10

The small heat shock proteins alpha B crystallin and HSP27 exert a protective effect in response to simulated ischemia. A model is proposed whereby proteins not in their final folding state bind to the outside of the large oligomeric small heat shock protein complexes thus finding a safe haven during ischemia. After the ischemia is resolved, these proteins may be released and, with the help of HSP70, are shuttled to a productive refolding pathway resulting in proteins in their final folding state, which can assume their normal activity in cells recovered from ischemic injury.
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PMID:Small heat shock proteins and protection against injury. 1041 21

HSP27 and MKBP translocate from the cytosolic to myofibril fraction in ischemic rat heart as demonstrated by immunoblotting. Immunohistochemistry analysis showed that ischemia enhances the Z line labeling of HSP27 and MKBP. Two dimensional gel electrophoresis showed that ischemia increases the hyperphosphorylated form of HSP27. These data suggest that HSP27 and MKBP may be involved in the Z line protection against postischemic reperfusion injury.
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PMID:Translocation of HSP27 and MKBP in ischemic heart. 1053 52

Small heat shock proteins (sHSPs), a family of HSPs, are known to accumulate in the CNS, mainly in astrocytes, in several pathological conditions such as Alexander's disease, Alzheimer's disease, and Creutzfeldt-Jakob disease. sHSPs may act not only as molecular chaperones, protecting against various stress stimuli, but may also play a physiological role in regulating cell differentiation and proliferation. In the present study, we have demonstrated that transient focal ischemia in rats dramatically induced HSP27 but not alpha B-crystallin (alphaBC), both of which are members of sHSPs, in reactive astrocytes. In contrast, in vitro chemical ischemic stress induced both HSP27 and alphaBC in cultured glial cells to the same extent. Dibutyryl cAMP (dBcAMP) and isoproterenol, a beta-adrenergic receptor (betaAR) agonist, enhanced HSP27 expression but suppressed alphaBC, and changed the shape of the cells to a stellate form. dBcAMP and isoproterenol inhibited cell proliferation under normal conditions. An increase in betaAR-like immunoreactivity was also observed in reactive astrocytes in vivo. These results, together with recent findings that betaAR plays an important role in glial scar formation in vivo, raise the possibility that betaAR activation modulates sHSP expression after focal ischemia and is involved in the transformation of astrocytes to their reactive form.
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PMID:Differential expression of small heat shock proteins in reactive astrocytes after focal ischemia: possible role of beta-adrenergic receptor. 1055 86

We investigated the role of the 27-kDa heat shock protein (HSP27) in cardiac protection using Langendorff-perfused rat hearts. After preconditioning (a single episode of 5 min global ischemia followed by 5 min of reperfusion), HSP27 redistributed from the cytosol to the sarcomere and recovery of the contractile function, after 40 min of global ischemia and 50 min of reperfusion, was significantly enhanced. Both SB203580, a p38 MAP kinase inhibitor, and bisindolylmaleimide I, a protein kinase C inhibitor, prevented the effects of preconditioning. Both 2-chloro-N(6)-cyclopentyladenosine (adenosine A1 agonist) and anisomycin (activator of p38 MAP kinase and c-jun N-terminal kinase) mimicked preconditioning. These results suggest that activation of protein kinase C followed by activation of p38 MAP kinase elicits translocation of HSP27 to the sarcomere, a process which may be involved in the cardioprotective mechanism afforded by ischemic preconditioning in rat heart.
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PMID:Translocation of HSP27 to sarcomere induced by ischemic preconditioning in isolated rat hearts. 1069 90

alpha-Phenyl-N-tert-butylnitrone (PBN), a spin trap, is known as a protective agent against delayed-neuronal death after ischemia-reperfusion. To investigate this neuroprotective effect of PBN, we examined the effect of PBN on the mitogen-activated protein kinase (MAPK) signaling pathway and the expression of heat shock proteins (HSPs) in the gerbil hippocampus following transient (5 min) ischemia. Immunoblot analysis revealed that intraperitoneal (i. p.) injection of PBN (200 mg/kg) enhanced the activation of extracellular-response kinase (ERK) and suppressed the activation of stress-activated protein kinase/c-Jun N-terminal protein kinase (SAPK/JNK) and p38 mitogen-activated protein kinase (p38) at 6 h after ischemia. Elevated levels of HSP27 and HSP70 were seen at the same period. These data suggest that PBN protects against delayed-neuronal death not only by its inherent radical-trapping activity but also by regulating the MAPK pathway and up-regulating HSPs.
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PMID:Neuroprotective effect of alpha-phenyl-N-tert-butylnitrone in gerbil hippocampus is mediated by the mitogen-activated protein kinase pathway and heat shock proteins. 1071 91


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