ubiquinone and gadolinium-chloride

ubiquinone has been researched along with gadolinium-chloride* in 1 studies

Other Studies

1 other study(ies) available for ubiquinone and gadolinium-chloride

Article	Year
Acceleration of hepatocellular energy by idebenone during early reperfusion after cold preservation ameliorates heat shock protein 70 gene expression in a pig liver model. Transplantation, 1997, Sep-27, Volume: 64, Issue:6 Heat shock proteins (HSPs) are induced in the liver after warm ischemia/reperfusion and are thought to be markers of hepatocellular injury and oxidative stress.. The influence of variable periods of cold storage followed by reperfusion on the expression of HSP70 was studied in the isolated perfused pig liver. Organs were harvested and stored in histidine-tryptophan-ketoglutarate solution at 4 degrees C and then perfused (210 min) in a closed water bath (38 degrees C), which subjects the liver to fluctuating outer pressure. The role of energy depletion, reactive oxygen intermediates, Kupffer cells, and circulating leukocytes in HSP70 expression was determined.. HSP70 expression was not detectable in liver tissue before explantation or before reperfusion by Northern blot analysis using a pig HSP70 gene probe. HSP70 expression was observed after reperfusion depending on cold storage time. Kinetics of HSP70 expression monitored by reverse transcriptase polymerase chain reaction showed a rapid increase of mRNA within 1 hr, which was closely associated with delayed recovery of hepatocellular energy charge, as assessed by the ketone body ratio. The inactivation of Kupffer cells, the presence or absence of leukocytes, and the suppression of oxidative stress with the antioxidant idebenone, given during reperfusion, had no influence. However, feeding the animals with idebenone over 7 days before explantation led to a faster recovery of ketone body ratio, paralleled by a substantial suppression of HSP70 expression.. Our data show that HSP70 expression during reperfusion is mainly dependent on the preceding cold storage time and the consecutive delayed recovery of the hepatocellular energy charge. Topics: Animals; Base Sequence; Benzoquinones; Cold Temperature; Conserved Sequence; DNA Primers; Energy Metabolism; Female; Gadolinium; Glucose; HSP70 Heat-Shock Proteins; Hypertonic Solutions; Ischemia; Ketone Bodies; Kinetics; Kupffer Cells; Liver; Male; Mannitol; Organ Preservation; Polymerase Chain Reaction; Potassium Chloride; Procaine; Reperfusion; RNA, Messenger; Swine; Transcription, Genetic; Ubiquinone	1997

Article

Year

Acceleration of hepatocellular energy by idebenone during early reperfusion after cold preservation ameliorates heat shock protein 70 gene expression in a pig liver model.

Transplantation, 1997, Sep-27, Volume: 64, Issue:6

Heat shock proteins (HSPs) are induced in the liver after warm ischemia/reperfusion and are thought to be markers of hepatocellular injury and oxidative stress.. The influence of variable periods of cold storage followed by reperfusion on the expression of HSP70 was studied in the isolated perfused pig liver. Organs were harvested and stored in histidine-tryptophan-ketoglutarate solution at 4 degrees C and then perfused (210 min) in a closed water bath (38 degrees C), which subjects the liver to fluctuating outer pressure. The role of energy depletion, reactive oxygen intermediates, Kupffer cells, and circulating leukocytes in HSP70 expression was determined.. HSP70 expression was not detectable in liver tissue before explantation or before reperfusion by Northern blot analysis using a pig HSP70 gene probe. HSP70 expression was observed after reperfusion depending on cold storage time. Kinetics of HSP70 expression monitored by reverse transcriptase polymerase chain reaction showed a rapid increase of mRNA within 1 hr, which was closely associated with delayed recovery of hepatocellular energy charge, as assessed by the ketone body ratio. The inactivation of Kupffer cells, the presence or absence of leukocytes, and the suppression of oxidative stress with the antioxidant idebenone, given during reperfusion, had no influence. However, feeding the animals with idebenone over 7 days before explantation led to a faster recovery of ketone body ratio, paralleled by a substantial suppression of HSP70 expression.. Our data show that HSP70 expression during reperfusion is mainly dependent on the preceding cold storage time and the consecutive delayed recovery of the hepatocellular energy charge.

Topics: Animals; Base Sequence; Benzoquinones; Cold Temperature; Conserved Sequence; DNA Primers; Energy Metabolism; Female; Gadolinium; Glucose; HSP70 Heat-Shock Proteins; Hypertonic Solutions; Ischemia; Ketone Bodies; Kinetics; Kupffer Cells; Liver; Male; Mannitol; Organ Preservation; Polymerase Chain Reaction; Potassium Chloride; Procaine; Reperfusion; RNA, Messenger; Swine; Transcription, Genetic; Ubiquinone

1997