ArticleArchives of biochemistry and biophysics2007
Biphasic effect of extra-reticular Mg2+ on hepatic G6P transport and hydrolysis.
Article in Archives of biochemistry and biophysics, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
5 citing papers in PubMed, 11 citations in OpenAlex.
- Low Hepatic MgJournal of Metabolic Syndrome · 2014Article
- Reduced cellular Mg²⁺ content enhances hexose 6-phosphate dehydrogenase activity and expression in HepG2 and HL-60 cells.Archives of biochemistry and biophysics · 2014Article
- Acute effect of ethanol on hepatic reticular G6Pase and Ca2+ pool.Alcoholism, clinical and experimental research · 2013Article
- Cellular magnesium homeostasis.Archives of biochemistry and biophysics · 2011Review
- Enhanced glucose 6-phosphatase activity in liver of rats exposed to Mg(2+)-deficient diet.Archives of biochemistry and biophysics · 2011Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Magnesium ions (Mg(2+)) play a key role in regulating hepatic cellular functions and enzymatic activities. In the present study, we report a concentration-dependent effect of cytosolic Mg(2+) on G6P and pyrophosphate (PPi) transport and hydrolysis in digitonin-permeabilized rat hepatocytes. The stimulatory effect of Mg(2+) on G6P is specific but biphasic, with a maximal effect at a concentration of 0.25 mM, whereas the effect on PPi increases in a dose-dependent manner. Both effects can be abolished by addition of EDTA to the system. Addition of taurocholate, histone-2A, alamethicin or A23187 to the incubation system results in a marked decrease in the Mg(2+) concentration present within the endoplasmic reticulum lumen. Under these conditions, the stimulatory effect of extra-reticular Mg(2+) on G6P transport and hydrolysis is abolished. Taken together, these data suggest that cytosolic Mg(2+) stimulates G6P transport by acting at the level of the substrate binding site of the G6Pase enzymatic complex or the surrounding phospholipid environment. The effect, which is lost when G6P has readily access to the ER lumen, requires physiological endoplasmic reticulum Mg(2+) content.
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Registered trials
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