Premium
Inhibition of glycogenolysis by 2,5‐anhydro‐D‐mannitol in isolated rat hepatocytes
Author(s) -
Stevens Hope C.,
Dills William L.
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80178-7
Subject(s) - phosphorolysis , glycogenolysis , glycogen phosphorylase , chemistry , glucagon , medicine , endocrinology , glycogen , mannitol , fructose , metabolite , galactose , biochemistry , biology , enzyme , purine nucleoside phosphorylase , purine , hormone
2,5‐Anhydro‐D‐mannitol, an analog of D‐fructofuranose, inhibited basal and glucagon‐stimulated glycogenolysis and glucose production in hepatocytes isolated from fed rats. Glucose formation from galactose was unaffected by the inhibitor. 2,5‐Anhydro‐D‐mannitol‐1‐phosphate inhibits phosphorylase a with a K i value of 2.4mM. This same phosphorylated metabolite accumulates to the extent of 9.2 μmol/g wet wt in treated hepatocytes suggesting that phosphorolysis is the locus of the inhibition of glucose production from glycogen. Our results suggest that 2,5‐anhydro‐D‐mannitol can be used to produce a model of hereditary fructose intolerance and that it merits further study as a hypoglycemic agent.