Catecholamine stimulation of ethanol oxidation by isolated rat hepatocytes

Ochs, Raymond S.; Lardy, Henry A.

doi:10.1016/0014-5793(81)80901-5

Cited by 17 publications

(2 citation statements)

References 16 publications

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“…In contrast, gluconeogenesis from sorbitol and glycerol is impaired in hepatocytes incubated in the absence of calcium (53,54). This is in agreement with the belief that cytosolic Ca 2 + stimulates transfer of reducing equivalents from cytosol to mitochondria by enhancing the glycerol 3-phosphate shuttle (55).…”

Section: Control By Acetyl-coasupporting

confidence: 80%

Gluconeogenesis and Related Aspects of Glycolysis

Hers¹,

Hue²

1983

Annu. Rev. Biochem.

516

259

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Section: Control By Acetyl-coasupporting

confidence: 80%

Gluconeogenesis and Related Aspects of Glycolysis

Hers¹,

Hue²

1983

Annu. Rev. Biochem.

516

259

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“…Addition of this hormone, too, accelerates flux through the glycerol 1-phosphate shuttle with glycerol as the substrate (Kneer et al, 1979). We have also found (results not shown) that glucose, like noradrenaline (Ochs & Lardy, 1981), accelerates ethanol oxidation for the same reason. Furthermore, noradrenaline, like glucose, stimulates glucose formation from 10 mM-pyruvate or 10 mMlactate plus 1 mM-pyruvate in the absence of an appreciable effect on pyruvate kinase and without a change in the cytosolic oxaloacetate concentration (Ochs & Lardy, 1983); this indicates that noradrenaline, too, must have activated both phosphoenolpyruvate carboxykinase and pyruvate carboxylase.…”

Section: Discussionsupporting

confidence: 58%

Stimulation by glucose of gluconeogenesis in hepatocytes isolated from starved rats

Rigoulet

Leverve

Plomp

et al. 1987

Biochemical Journal

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Control properties of the gluconeogenic pathway in hepatocytes isolated from starved rats were studied in the presence of glucose. The following observations were made. (1) Glucose stimulated the rate of glucose production from 20 mM-glycerol, from a mixture of 20 mM-lactate and 2 mM-pyruvate, or from pyruvate alone; no stimulation was observed with 20 mM-alanine or 20 mM-dihydroxyacetone. Maximal stimulation was obtained between 2 and 5 mM-glucose, depending on the conditions. At concentrations above 6 mM, gluconeogenesis declined again, so that at 10 mM-glucose the glucose production rate became equal to that in its absence. (2) With glycerol, stimulation of gluconeogenesis by glucose was accompanied by oxidation of cytosolic NADH and reduction of mitochondrial NAD+ and was insensitive to the transaminase inhibitor amino-oxyacetate; this indicated that glucose accelerated the rate of transport of cytosolic reducing equivalents to the mitochondria via the glycerol 1-phosphate shuttle. (3) With lactate plus pyruvate (10:1) as substrates, stimulation of gluconeogenesis by glucose was almost additive to that obtained with glucagon. From an analysis of the effect of glucose on the curves relating gluconeogenic flux and the steady-state intracellular concentrations of gluconeogenic intermediates under various conditions, in the absence and presence of glucagon, it was concluded that addition of glucose stimulated both phosphoenolpyruvate carboxykinase and pyruvate carboxylase activity.

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Thyroid Hormone and Dehydroepiandrosterone Permit Gluconeogenic Hormone Responses in Hepatocytes

Kneer

Lardy

2000

Archives of Biochemistry and Biophysics

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Catecholamine stimulation of ethanol oxidation by isolated rat hepatocytes

Cited by 17 publications

References 16 publications

Gluconeogenesis and Related Aspects of Glycolysis

Gluconeogenesis and Related Aspects of Glycolysis

Stimulation by glucose of gluconeogenesis in hepatocytes isolated from starved rats

Thyroid Hormone and Dehydroepiandrosterone Permit Gluconeogenic Hormone Responses in Hepatocytes

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