Cited by 171Diabetes Treatment and ManagementMetabolism, Diabetes, and CancerPancreatic function and diabetes

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New hepatic targets for glycaemic control in diabetes

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Agius, Loranne·2007·Best Practice & Research Clinical Endocrinology & Metabolism

DOI 10.1016/j.beem.2007.09.001

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Abstract

Type-2 diabetes is associated with impaired glucose clearance by the liver in the postprandial state, and with elevated glucose production in the post-absorptive state. New targets within the liver are currently being investigated for development of antihyperglycaemic drugs for type-2 diabetes. They include glucokinase, which catalyses the first step in glucose metabolism, the glucagon receptor, and enzymes of gluconeogenesis and/or glycogenolysis such as glucose 6-phosphatase, fructose 1,6-bisphosphatase and glycogen phosphorylase. Preclinical studies with candidate drugs on animal models or cell-based assays suggest that these targets have the potential for pharmacological glycaemic control. Data from clinical studies is awaited. Further work is required for better understanding of the implications of targeting these sites in terms of possible side-effects or tachyphylaxis. The advantage of combined targeting of two or more sites within the liver for minimizing side-effects and tachyphylaxis caused by single-site targeting is discussed.

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BindingDB Entry 50030938: Synthesis and glycogen phosphorylase inhibitory activity of N-(beta-D-glucopyranosyl)amides possessing 1,4-benzodioxane moiety.
BindingDB (2010) · UC San Diego · doi:10.7270/q22807pv
BindingDB Entry 50027183: Novel design principle validated: glucopyranosylidene-spiro-oxathiazole as new nanomolar inhibitor of glycogen phosphorylase, potential antidiabetic agent.
BindingDB (2010) · UC San Diego · doi:10.7270/q2571btv
BindingDB Entry 50043205: TBA
BindingDB (2014) · UC San Diego · doi:10.7270/q2x068fd
BindingDB Entry 50045311: Structure based inhibitor design targeting glycogen phosphorylase B. Virtual screening, synthesis, biochemical and biological assessment of novel N-acyl-ß-d-glucopyranosylamines.
BindingDB (2016) · UC San Diego · doi:10.7270/q2ks6t58
BindingDB Entry 50047056: Glucose-derived spiro-isoxazolines are anti-hyperglycemic agents against type 2 diabetes through glycogen phosphorylase inhibition.
BindingDB (2017) · UC San Diego · doi:10.7270/q2qr500m
BindingDB Entry 50031075: Synthesis of 1-(D-glucopyranosyl)-1,2,3-triazoles and their evaluation as glycogen phosphorylase inhibitors.
BindingDB (2010) · UC San Diego · doi:10.7270/q2jq114d
BindingDB Entry 50018710: Current anti-diabetic agents and their molecular targets: A review.
BindingDB (2024) · UC San Diego · doi:10.7270/q29z9940
BindingDB Entry 50047111: 4(5)-Aryl-2-C-glucopyranosyl-imidazoles as New Nanomolar Glucose Analogue Inhibitors of Glycogen Phosphorylase.
BindingDB (2017) · UC San Diego · doi:10.7270/q2w37z56
BindingDB Entry 50039916: The binding of C5-alkynyl and alkylfurano[2,3-d]pyrimidine glucopyranonucleosides to glycogen phosphorylase b: synthesis, biochemical and biological assessment.
BindingDB (2013) · UC San Diego · doi:10.7270/q2vx0hkh
BindingDB Entry 2669: Naturally Occurring Pentacyclic Triterpenes as Inhibitors of Glycogen Phosphorylase: Synthesis, Structure-Activity Relationships, and X-ray Crystallographic Studies.
BindingDB (2008) · UC San Diego · doi:10.7270/q2wq0233
BindingDB Entry 50043341: Synthesis, enzyme kinetics and computational evaluation of N-(ß-D-glucopyranosyl) oxadiazolecarboxamides as glycogen phosphorylase inhibitors.
BindingDB (2014) · UC San Diego · doi:10.7270/q2bc410f
BindingDB Entry 50044205: New synthesis of 3-(ß-D-glucopyranosyl)-5-substituted-1,2,4-triazoles, nanomolar inhibitors of glycogen phosphorylase.
BindingDB (2015) · UC San Diego · doi:10.7270/q2zp47n4
BindingDB Entry 50048176: Synthetic, enzyme kinetic, and protein crystallographic studies of C-ß-d-glucopyranosyl pyrroles and imidazoles reveal and explain low nanomolar inhibition of human liver glycogen phosphorylase.
BindingDB (2018) · UC San Diego · doi:10.7270/q2tt4sxg
BindingDB Entry 50030415: Synthesis and structure-activity relationships of C-glycosylated oxadiazoles as inhibitors of glycogen phosphorylase.
BindingDB (2010) · UC San Diego · doi:10.7270/q2q52ppv
BindingDB Entry 50011192: Structural Specificity of Flavonoids in the Inhibition of Human Fructose 1,6-Bisphosphatase.
BindingDB (2021) · UC San Diego · doi:10.7270/q2zw1qh2
BindingDB Entry 50049015: Discovery of new nanomolar inhibitors of GPa: Extension of 2-oxo-1,2-dihydropyridinyl-3-yl amide-based GPa inhibitors.
BindingDB (2019) · UC San Diego · doi:10.7270/q2gf0wr2

Authors: Agius, L.
Affiliations: Newcastle University (GB)
Corresponding author: Agius, Loranne
ORCID: Agius, Loranne
Venue: Best Practice & Research Clinical Endocrinology & Metabolism
Publisher: Elsevier BV
Published: 2007-12
Volume: 21
Issue: 4
Pages: 587-605
ISSN: 1521-690X (ISSN-L)
DOI: 10.1016/j.beem.2007.09.001
OpenAlex: W2132179056
Cited by: 155
References: 107
Citations by year: 2026: 3 · 2025: 5 · 2024: 5 · 2023: 3 · 2022: 3 · 2021: 3 · 2020: 11 · 2019: 2 · 2018: 10 · 2017: 10 · 2016: 10 · 2015: 13 · 2014: 10 · 2013: 12 · 2012: 16
FWCI: 1.91
Type: journal article
Language: en
Open access: green
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
Locations: Best Practice & Research Clinical Endocrinology & Metabolism (publishedVersion)
PubMed (publishedVersion)
Newcastle University ePrints (Newcastle Univesity)
Topics: Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Diabetes Treatment and Management
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Pancreatic function and diabetes
Keywords: type 2 diabetes, hepatic glucose metabolism, antidiabetic drugs, glucokinase, glucagon receptor, gluconeogenesis, glycogenolysis, glucose-6-phosphatase, fructose-1,6-bisphosphatase, glycogen phosphorylase, tachyphylaxis, adverse drug reactions
MeSH terms: Animals, Binding Sites, Blood Glucose, Diabetes Mellitus, Type 2, Enzyme Inhibitors, Glucagon, Glucokinase, Gluconeogenesis, Glucose-6-Phosphatase, Fructose-Bisphosphatase, Humans, Hypoglycemic Agents, Liver, Glycogen Phosphorylase

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New hepatic targets for glycaemic control in diabetes

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