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Bladzijde 1 van 162 resultaten
Inhibition of nitric oxide synthase or cyclo-oxygenase pathways in organum vasculosum laminae terminalis attenuates interleukin-1 beta fever in rabbits.
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Fever was induced in rabbits by i.v. administration of lipopolysaccharide (LPS) or administration of interleukin-1 beta (IL-1 beta) into the organum vasculosum laminae terminalis (OVLT). Intra-OVLT injection of IL-1 receptor antagonist (IL-lra), 1 h before LPS or IL-1 beta injection, inhibited the
Heat shock protein 32/heme oxygenase-1 protects mouse Sertoli cells from hyperthermia-induced apoptosis by CO activation of sGC signalling pathways.
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Heat shock protein 32 (Hsp32)/heme oxygenase-1 (HO-1) may be a key enzyme for the protection of cells against stress. Its anti-apoptotic effect has been attributed to its product, carbon monoxide (CO), in many types of cells. However, whether its anti-apoptotic mechanism plays a role in Sertoli
Febrile seizure, but not hyperthermia alone, induces the expression of heme oxygenase-1 in rat cortex.
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BACKGROUND
Febrile seizure (FS) is the most common seizure disorders. Approximately one third of children with a febrile seizure have recurrent events. The mechanism of FS remains unclear. Heme oxygenase-1 (HO-1) is a member of the heat shock proteins family and can be induced in the brain by
Heme oxygenase-1 (Hsp32) is involved in the protection of small intestine by whole body mild hyperthermia from ischemia/reperfusion injury in rat.
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OBJECTIVE
The aim of the present study was to explore whether heme oxygenase-1 (HO-1) is involved in the hyperthermia-provided protection of the small intestine from ischemia/reperfusion injury in rats.
METHODS
Intestinal damage was induced in male Sprague-Dawley rats by clamping both the superior
Stress response of the rat testis: in situ hydridization and immunohistochemical analysis of heme oxygenase-1 (HSP32) induction by hyperthermia.
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By using in situ hybridization and immunohistochemistry, the distribution patterns of heme oxygenase (HO)-1 (HSP32) transcript and protein were studied, and their response to thermal stress was examined. And, by using an HO-1 cDNA probe and polyclonal antibody, the levels of HO-1 mRNA and protein in
Induction of heart heme oxygenase-1 (HSP32) by hyperthermia: possible role in stress-mediated elevation of cyclic 3':5'-guanosine monophosphate.
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Presently we have investigated the carbon monoxide generating capacity of the cardiovascular system under normal and stress conditions by examining the microsomal heme oxygenase system at the transcript, protein and activity levels; and have assessed response of heart nitric oxide (NO) synthase
Induction of heme oxygenase in rat hepatoma cells by exposure to heavy metals and hyperthermia.
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Treatment of rat hepatoma dRLh-84 cells with sodium arsenite, cadmium chloride and cobalt chloride resulted in marked induction of protein with a molecular mass of 32 kDa. To examine the possibility that the induced 32 kDa protein may be heme oxygenase, the enzyme activity was measured, and then the
Rapid induction of heme oxygenase 1 mRNA and protein by hyperthermia in rat brain: heme oxygenase 2 is not a heat shock protein.
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Catalytic activity of heme oxygenase (heme, hydrogen-donor:oxygen oxidoreductase, EC 1.14.99.3) isozymes, HO-1 and HO-2, permits production of physiologic isomers of bile pigments. In turn, bile pigments biliverdin and bilirubin are effective antioxidants in biological systems. In the rat brain we
Coordinated expression and mechanism of induction of HSP32 (heme oxygenase-1) mRNA by hyperthermia in rat organs.
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Heme oxygenase isozymes, HO-1 and HO-2, catalyze the cleavage of heme b (Fe-protoporphyrin-IX) at the alpha-meso carbon bridge to form the antioxidant, biliverdin IX alpha, and the putative cellular messenger, carbon monoxide. HO-1 is a heat shock (HSP32) or stress protein, while HO-2 is a
Role of the brain heme oxygenase-carbon monoxide pathway in stress fever in rats.
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This study was aimed at testing the hypothesis that the brain heme oxygenase (HO)-carbon monoxide (CO) pathway plays a role in stress fever. To this end, the effect of the HO inhibitor, zinc deuteroporphyrin 2,4-bis glycol (ZnDPBG), on restraint-induced fever was tested. Intracerebroventricular
Inhibition of Heme Oxygenase-1 enhances hyperthermia-induced autophagy and antiviral effect.
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Hyperthermia has been clinically utilized as an adjuvant therapy in the treatment of cervical carcinoma. However, thermotolerance induced by heme oxygenase-1 (HO-1), a stress-inducible cytoprotective protein, limits the efficacy of hyperthermic therapy, for which the exact mechanism remains unknown.
Regulation of inducible heme oxygenase and cyclooxygenase isozymes in a mouse model of spotted fever group rickettsiosis.
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Vascular endothelial cells (ECs) lining the blood vessels are the preferred primary targets of pathogenic Rickettsia species in the host. In response to oxidative stress triggered by infection, ECs launch defense mechanisms such as expression of heme oxygenase-1 (HO-1). Previous evidence from an
Effects of hyperthermia pretreatment on expression of heme oxygenase-1 and nitric oxide synthase in rats subjected to experimental anaphylactic shock.
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Previous studies have shown that hyperthermia pretreatment results in an attenuation of increased vascular leakage in rats subjected to experimental anaphylactic shock. It is known that both nitric oxide synthase (NOS) and heme oxygenase-1 (HO-1) play a role in the maintenance of microvascular
Heme oxygenase-1 induction by cobalt protoporphyrin enhances fever and inhibits pyrogenic tolerance to lipopolysaccharide.
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Heme oxygenase-1 (HO-1) is an enzyme that catalyzes degradation of the heme and regulates its availability for newly synthetized hemeproteins such as cyclooxygenases, NO synthases and cytochrome P450. Moreover, HO-1 activity modulates synthesis of cytokines and prostaglandins. All of these factors
Nitric oxide synthase-cyclo-oxygenase pathways in organum vasculosum laminae terminalis: possible role in pyrogenic fever in rabbits.
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1. Fever was induced in rabbits by administration of Escherichia coli endotoxin (lipopolysaccharide; LPS; 0.001-10 micrograms) into the organum vasculosum laminae terminalis (OVLT). Deep body temperature was evaluated over a period of 7 h. 2. The LPS-induced febrile response was mimicked by
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