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Glycogen phosphorylase inhibition improves beta cell function
Author(s) -
Nagy Lilla,
Márton Judit,
Vida András,
Kis Gréta,
Bokor Éva,
Kun Sándor,
Gönczi Mónika,
Docsa Tibor,
Tóth Attila,
Antal Miklós,
Gergely Pál,
Csóka Balázs,
Pacher Pal,
Somsák László,
Bai Péter
Publication year - 2018
Publication title -
british journal of pharmacology
Language(s) - Uncategorized
Resource type - Journals
SCImago Journal Rank - 2.432
H-Index - 211
eISSN - 1476-5381
pISSN - 0007-1188
DOI - 10.1111/bph.13819
Subject(s) - glycogen , glycogen phosphorylase , glycogen synthase , medicine , glycogenesis , endocrinology , insulin , glycogen debranching enzyme , glycogen branching enzyme , beta cell , glycolysis , biology , phosphorylase kinase , carbohydrate metabolism , chemistry , metabolism , islet
Glycogen phosphorylase (GP) is the key enzyme for glycogen degradation. GP inhibitors (GPi-s) are glucose lowering agents that cause the accumulation of glucose in the liver as glycogen. Glycogen metabolism has implications in beta cell function. Glycogen degradation can maintain cellular glucose levels, which feeds into catabolism to maintain insulin secretion, and elevated glycogen degradation levels contribute to glucotoxicity. The purpose of this study was to assess whether influencing glycogen metabolism in beta cells by GPi-s affects the function of these cells.