Inhibition of gluconeogenesis and glycogenolysis by 2,5-anhydro-D-mannitol.

Hanson, Ronald L.; Ho, Robert S.; Wiseberg, J J; Simpson, Ronald C.; Younathan, Ezzat S.; Blair, James B.

doi:10.1016/s0021-9258(17)43644-1

Cited by 42 publications

(3 citation statements)

References 23 publications

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“…Finally, the present data corroborate our explanation of the mechanism of the hypoglycemic action of 2,5-anhydro-Dmannitol (Hanson et al, 1984). Riquelme et al (1984) reported that 2,5-anhydro-D-mannitol was phosphorylated to the 1-phosphate and the 1,6-bisphosphate esters in rat hepatocytes.…”

Section: Discussionsupporting

confidence: 91%

See 1 more Smart Citation

Stereospecificity of the fructose 2,6-bisphosphate site of muscle 6-phosphofructo-1-kinase

Kelley¹,

Voll²,

Voll³

et al. 1986

Biochemistry

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We explored the stereospecificity of the fructose 2,6-bisphosphate site of rabbit muscle 6-phosphofructo-1-kinase by determination of the activation constants (Ka) of several structurally locked analogues of this potent metabolic regulator. Under the assay conditions used, the Ka of fructose 2,6-bisphosphate was 0.12 microM. The most effective synthetic analogues and their Ka's were 2,5-anhydro-D-mannitol 1,6-bisphosphate (2.9 microM), 1,4-butanediol bisphosphate (6.6 microM), hexitol 1,6-bisphosphate (40 microM), and 2,5-anhydro-D-glucitol 1,6-bisphosphate (47 microM). Ten other bisphosphate compounds were much less effective as activators of the enzyme. These findings indicate that, unlike its active site, this allosteric site of 6-phosphofructo-1-kinase does not require the furanose ring. Its basic requirement seems to be a compound with two phosphate groups approximately 9 A apart. Although the free hydroxy groups of the activator do not seem to be essential, their presence enhances appreciably the affinity of the ligand for this regulatory site.

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Section: Discussionsupporting

confidence: 91%

“…Riquelme et al (1984) reported that 2,5-anhydro-D-mannitol was phosphorylated to the 1-phosphate and the 1,6-bisphosphate esters in rat hepatocytes. We have shown that the latter compound stimulates glycolysis and simultaneously inhibits both gluconeogenesis and glycogenolysis in the same system (Hanson et al, 1984).…”

Section: Discussionmentioning

confidence: 79%

Stereospecificity of the fructose 2,6-bisphosphate site of muscle 6-phosphofructo-1-kinase

Kelley¹,

Voll²,

Voll³

et al. 1986

Biochemistry

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show abstract

“…The differences between P1 and P2–P3 efflux suggest the former is trapped inside the cell, reflecting the metabolic involvement in probe uptake. With 2,5-anhydro- d -mannitol being a substrate for metabolic kinases, , it is plausible that due to the symmetry, the sugar provides a primary hydroxyl amenable to phosphorylation even after conjugation to the coumarin. The evident efflux measured for P2–P3 under the same conditions further highlighted the differences in the metabolic fate between the probes.…”

Section: Resultsmentioning

confidence: 99%

Discrimination of GLUTs by Fructose Isomers Enables Simultaneous Screening of GLUT5 and GLUT2 Activity in Live Cells

et al. 2023

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Facilitative carbohydrate transporters (GLUTs, SLC2 gene family) are transmembrane proteins transporting hexoses and other sugars based on cellular metabolic demands. While a direct link between GLUTs and metabolic disorders has framed them as important biological and medicinal targets, targeting disease-relevant GLUTs remains challenging. In this study, we aimed to identify substrate–GLUT interactions that would discriminate between major fructose transporters. We examined the uptake distribution for conformational and configurational isomers of fructose using the corresponding conformationally locked fluorescently labeled mimetics as probes for assessing GLUT preferences in real time. Through comparative analysis of the uptake of the probes in the yeast-based single GLUT expression systems and the multi-GLUT mammalian cell environment, we established the ability of fructose transporters to discriminate between fructose conformers and epimers. We demonstrated that recreating the conformational and configurational mixture of fructose with molecular probes allows for the specific probe distribution, with fructofuranose mimetic being taken up preferentially through GLUT5 and β-d-fructopyranose mimetic passing through GLUT2. The uptake of α-d-fructopyranose mimetic was found to be independent of GLUT5 or GLUT2. The results of this study provide a new approach to analyzing GLUT5 and GLUT2 activity in live cells, and the findings can be used as a proof-of-concept for multi-GLUT activity screening in live cells. The research also provides new knowledge on substrate–GLUT interactions and new tools for monitoring alterations in GLUT activities.

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On the inhibition of hepatic glycogenolysis by fructose. A31P-NMR study in perfused rat liver using the fructose analogue 2,5-anhydro-D-mannitol

Bruynseels¹,

Bergans²,

Gillis³

et al. 1999

NMR Biomed.

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Inhibition of gluconeogenesis and glycogenolysis by 2,5-anhydro-D-mannitol.

Cited by 42 publications

References 23 publications

Stereospecificity of the fructose 2,6-bisphosphate site of muscle 6-phosphofructo-1-kinase

Stereospecificity of the fructose 2,6-bisphosphate site of muscle 6-phosphofructo-1-kinase

Discrimination of GLUTs by Fructose Isomers Enables Simultaneous Screening of GLUT5 and GLUT2 Activity in Live Cells

On the inhibition of hepatic glycogenolysis by fructose. A31P-NMR study in perfused rat liver using the fructose analogue 2,5-anhydro-D-mannitol

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