The Role of Hepatic Glucose-6-phosphatase in the Regulation of Carbohydrate Metabolism

Ashmore, James; Weber, George

doi:10.1016/s0083-6729(08)60269-1

Cited by 244 publications

(69 citation statements)

References 76 publications

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“…There have been some reports in the literature ind cating that glucocorticoids (dexamethasone) increase liver g ucose-6-phosphatase enzyme activity and others showing tlat it does not (e.g. [1,12,14,[22][23][24][25][26][27]). A simple explanation fi,r these apparently conflicting findings would be that the effect of dexamethasone also depends on the levels of other h )rmones like insulin and glucagon as illustrated in Table 1.…”

Section: Sehmoll Et Al/febs Letters 383 (1996) 6346mentioning

confidence: 99%

“…Glucose-6-phosphatase [EC 3.1.3.9] catalyses the hydrolysis ol glucose-6-phosphate to glucose [1,2]. This reaction is the terminal step of both gluconeogenesis and glycogen breakdown in liver.…”

Section: Introductionmentioning

confidence: 99%

“…Hepatic glucose-6-phosphatase enzyme activity [1,8], protein levels [8], and mRNA levels [9] all increase greatly in animal models of diabetes mellitus. Administration of glucocorticoids, insulin, thyroid hormone or glucagon to animals has been shown to alter glucose-6-phosphatase activity in microsomes [1,[10][11][12][13]. In addition, liver glucose-6-phosphatase enzyme activity, protein and mRNA levels are developmentally regulated in mammals [9,14,15].…”

Section: Introductionmentioning

confidence: 99%

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Cloning and sequencing of the 5′ region of the human glucose‐6‐phosphatase gene: transcriptional regulation by cAMP, insulin and glucocorticoids in H4IIE hepatoma cells

1996

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We have cloned and sequenced the first 1.2 kb of the 5' region of the human glucose-6-phosphatase gene. Transfection of H4IIE hepatoma cells with the 1.2 kb fragment fused to a luciferase reporter gene demonstrated both basal and hormone responsive luciferase activity. Dexamethasone increased and insulin decreased luciferase activity. Insulin and dibutyryl cyclic AMP both significantly decreased activity in the presence of de gamethasone.

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Section: Sehmoll Et Al/febs Letters 383 (1996) 6346mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Cloning and sequencing of the 5′ region of the human glucose‐6‐phosphatase gene: transcriptional regulation by cAMP, insulin and glucocorticoids in H4IIE hepatoma cells

1996

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“…de Duve et al (3), which mainly derives from the endoplasmic reticulum (ER) membranes (4). The latency of its activity, discovered in early studies (5,6), together with histochemical studies (7) indicated the compartmentation of the enzyme in the ER lumen. Consistent with this, more recent sequence information (8,9) revealed that mammalian glucose-6-phosphatases contain the carboxyl-terminal two-lysine retention motif by which transmembrane proteins are retained in the ER by retrieval from the Golgi (10,11).…”

mentioning

confidence: 99%

Demonstration of a Metabolically Active Glucose-6-phosphate Pool in the Lumen of Liver Microsomal Vesicles

Bánhegyi

Marcolongo

Fulceri

et al. 1997

Journal of Biological Chemistry

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Glucose-6-phosphate transport was investigated in rat or human liver microsomal vesicles using rapid filtration and light-scattering methods. Upon addition of glucose-6-phosphate, rat liver microsomes accumulated the radioactive tracer, reaching a steady-state level of uptake. In this phase, the majority of the accumulated tracer was glucose, but a significant intraluminal glucose-6-phosphate pool could also be observed. The extent of the intravesicular glucose pool was proportional with glucose-6-phosphatase activity. The relative size of the intravesicular glucose-6-phosphate pool (irrespective of the concentration of the extravesicular concentration of added glucose-6-phosphate) expressed as the apparent intravesicular space of the hexose phosphate was inversely dependent on glucose-6-phosphatase activity. The increase of hydrolysis by elevating the extravesicular glucose-6-phosphate concentration or temperature resulted in lower apparent intravesicular glucose-6-phosphate spaces and, thus, in a higher transmembrane gradient of glucose-6-phosphate concentrations. In contrast, inhibition of glucose-6-phosphate hydrolysis by vanadate, inactivation of glucose-6-phosphatase by acidic pH, or genetically determined low or absent glucose-6-phosphatase activity in human hepatic microsomes of patients suffering from glycogen storage disease type 1a led to relatively high intravesicular glucose-6-phosphate levels. Glucose-6-phosphate transport investigated by light-scattering technique resulted in similar traces in control and vanadate-treated rat microsomes as well as in microsomes from human patients with glycogen storage disease type 1a. It is concluded that liver microsomes take up glucose-6-phosphate, constituting a pool directly accessible to intraluminal glucose-6-phosphatase activity. In addition, normal glucose-6-phosphate uptake can take place in the absence of the glucose-6-phosphatase enzyme protein, confirming the existence of separate transport proteins.

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“…N. V S. Ramakrishna et al discovered an inhibitor4) of glucose-6-phosphate translocase in cultures of a microorganism, HIL-008003, (DSM 11641) which they called mumbaistatin (1). Although they succeeded in isolating the active principle, they were unable to determine the structure of this acid-labile compound,whose^-NMR spectrum contained relatively few signals.…”

mentioning

confidence: 99%

The Chemical Structure of Mumbaistatin, a Novel Glucose-6-phosphate Translocase Inhibitor Produced by Streptomyces sp. DSM 11641.

Vértesy¹,

Kurz²,

Paulus³

et al. 2001

J. Antibiot.

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The Role of Hepatic Glucose-6-phosphatase in the Regulation of Carbohydrate Metabolism

Cited by 244 publications

References 76 publications

Cloning and sequencing of the 5′ region of the human glucose‐6‐phosphatase gene: transcriptional regulation by cAMP, insulin and glucocorticoids in H4IIE hepatoma cells

Cloning and sequencing of the 5′ region of the human glucose‐6‐phosphatase gene: transcriptional regulation by cAMP, insulin and glucocorticoids in H4IIE hepatoma cells

Demonstration of a Metabolically Active Glucose-6-phosphate Pool in the Lumen of Liver Microsomal Vesicles

The Chemical Structure of Mumbaistatin, a Novel Glucose-6-phosphate Translocase Inhibitor Produced by Streptomyces sp. DSM 11641.

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