Halothane and Sevoflurane Decrease Norepinephrine-Stimulated Glucose Transport in Neonatal Cardiomyocyte

Kudoh, Akira; Matsuki, Akitomo

doi:10.1097/00000539-200011000-00021

Cited by 3 publications

(2 citation statements)

References 18 publications

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“…Wells containing medium but no cells served as blanks. Sevoflurane concentrations of 0.25 and 0.5 mM correspond to 0.3125 and 0.625 minimum alveolar concentrations (MAC), respectively [10]. These concentrations are lower than that of clinical usage.…”

Section: Methodsmentioning

confidence: 99%

Sevoflurane Stimulates MAP Kinase Signal transduction through the Activation of PKC .ALPHA. and .BETA.II in Fetal Rat Cerebral Cortex Cultured Neuron

Hasegawa

Takekoshi

Nagata

et al. 2006

Acta Histochem. Cytochem

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Protein kinase C (PKC) is a key enzyme that participates in various neuronal functions. PKC has also been identified as a target molecule for general anesthetic actions. Raf, mitogen-activated protein kinase (MEK) and extracellular signal-regulated kinase (ERK1/2) have been thought to be target effectors of PKC. In the present study, we attempted to evaluate the effect of sevoflurane on PKC/MAPK cascade signaling in cultured fetal rat cerebral cortex neurons, prepared from embryonic day 18 fetuses. The effects of sevoflurane on the translocation of 7 PKC isoforms (α, βI, βII, γ, δ, ɛ and ζ) were observed by immunoblotting using isoform-selective antibodies to PKCs. The treatment of neurons with sevoflurane induced the translocation of PKC α and PKC βII species from the cytosol to the membrane fraction, which indicated the activation of these PKC isoforms. In contrast, there was no clear change in the distribution of other PKC isoforms. We next examined whether the specific activation of PKC α and βII by sevoflurane could stimulate the MAP kinase signaling pathway in cultured neurons. Raf phosphorylation was increased by the administration of 0.25 mM sevoflurane. The phosphorylation of Raf proteins reached a maximum at 5–10 min. Subsequently, the phosphorylation of MEK proteins was increased at 10–15 min after sevoflurane treatments. That of ERK proteins was induced at 15–60 min. Moreover, the phosphorylation of ERK induced by sevoflurane was significantly decreased by the treatment of PKC inhibitor (staurosporine) and MEK inhibitor (PD98059). On the other hand, the contents of total Raf, MEK and ERK proteins were relatively constant at all times examined. To examine the localization of phosphorylated-ERK protein, immunohistochemical staining of sevoflurane-treated cultured neurons was performed. The phosphorylated-ERK proteins were markedly accumulated in both the cytosol of the cell body and the neurites in the neuronal cells with time after 0.25 mM sevoflurane-treatment. These results demonstrated that sevoflurane induced the phosphorylation of the MAP kinase cascade through the activation of the PKC α and PKC βII species.

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Section: Methodsmentioning

confidence: 99%

Sevoflurane Stimulates MAP Kinase Signal transduction through the Activation of PKC .ALPHA. and .BETA.II in Fetal Rat Cerebral Cortex Cultured Neuron

Hasegawa

Takekoshi

Nagata

et al. 2006

Acta Histochem. Cytochem

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“…Glucose represents the sole energy supply to the newborn heart in contrast to the adult heart, which depends mainly upon fatty acids as a source of energy. 15 This finding emphasizes the importance of avoiding hypoglycemia in pediatric patients in order to avoid myocardial depression. This is especially important when dealing with children who have impaired glucose homeostasis and are unable to utilize fatty acids as in the child presented in this report.…”

Section: Anesthetic Managementmentioning

confidence: 86%

The anesthetic management of ventricular septal defect (VSD) repair in a child with mitochondrial cytopathy

Farag

Argalious

Narouze

et al. 2002

Can J Anesth/J Can Anesth

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Endothelin‐1‐ and isoproterenol‐induced differential protein expression and signaling pathway in HL‐1 cardiomyocytes

Hong

Song

et al. 2010

Proteomics

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It is well known that the two chemical compounds endothelin-1 (ET-1) and isoproterenol (ISO) can individually induce cardiac hypertrophy through G protein-coupled receptors in cardiomyocytes. However, the cardiac hypertrophy signaling pathway activated by ET-1 and ISO is not well defined. Therefore, we investigated the protein expression profile and signaling transduction in HL-l cardiomyocyte cells treated with ET-1 and ISO. Following separation of the cell lysates by using 2-DE and silver staining, we identified 16 protein spots that were differentially expressed as compared to the controls. Of these 16 spots, three changed only after treatment with ET-1, whereas four changed only after treatment with ISO, suggesting that these two stimuli could induce different signaling pathways. In order to reveal the differences between ET-1- and ISO-induced signaling, we studied the different events that occur at each step of the signaling pathways, when selected biocomponents were blocked by inhibitors. Our results indicated that ET-1 and ISO used different pathways for phosphorylation of glycogen synthase kinase-3β (GSK3β). ET-1 mainly used the mitogen-activated protein kinase and phosphatidylinositol-3-kinase/AKT pathways to activate GSK3β, whereas under ISO stimulation, only the phosphatidylinositol-3-kinase/AKT pathway was required to trigger the GSK3β pathway. Furthermore, the strength of the GSK3β signal in ISO-induced cardiac hypertrophy was stronger than that in ET-1-induced cardiac hypertrophy. We found that these two agonists brought about different changes in the protein expression of HL-1 cardiomyocytes through distinct signaling pathways even though the destination of the two signaling pathways was the same.

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Halothane and Sevoflurane Decrease Norepinephrine-Stimulated Glucose Transport in Neonatal Cardiomyocyte

Cited by 3 publications

References 18 publications

Sevoflurane Stimulates MAP Kinase Signal transduction through the Activation of PKC .ALPHA. and .BETA.II in Fetal Rat Cerebral Cortex Cultured Neuron

Sevoflurane Stimulates MAP Kinase Signal transduction through the Activation of PKC .ALPHA. and .BETA.II in Fetal Rat Cerebral Cortex Cultured Neuron

The anesthetic management of ventricular septal defect (VSD) repair in a child with mitochondrial cytopathy

Endothelin‐1‐ and isoproterenol‐induced differential protein expression and signaling pathway in HL‐1 cardiomyocytes

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