The DOI matches its Crossref record; 108 of the 108 references it cites were found in a registry or an index.
New hepatic targets for glycaemic control in diabetes
Open accessAbstract
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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“serum from type 2 diabetic patients treated with glargine activates insulin receptors A and B similarly to NPH insulin and does not increase signalling through the IGF-1 receptor128.”
From Pathophysiology and treatment of type 2 diabetes: perspectives on the past, present, and future (2014) · cites this paper as [128]
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Pathophysiology and treatment of type 2 diabetes: perspectives on the past, present, and future
Kahn, S. E., Cooper, M. E., & Del Prato, S. (2014) · The Lancet · doi:10.1016/s0140-6736(13)62154-6 · Cited by 1,743
Management of type 2 diabetes: new and future developments in treatment
Tahrani, A. A., Bailey, C. J., Prato, S. D., & Barnett, A. H. (2011) · The Lancet · doi:10.1016/s0140-6736(11)60207-9 · Cited by 541
Islet G protein-coupled receptors as potential targets for treatment of type 2 diabetes
Åhrén, B. (2009) · Nature Reviews Drug Discovery · doi:10.1038/nrd2782 · Cited by 422
Glucokinase and molecular aspects of liver glycogen metabolism
Agius, L. (2008) · Biochemical Journal · doi:10.1042/bj20080595 · Cited by 407
Self-citationTargeting hepatic glucose metabolism in the treatment of type 2 diabetes
Rines, A. K., Sharabi, K., Tavares, C. D. J., & Puigserver, P. (2016) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2016.151 · Cited by 390
Metadata
- 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)
- 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
- 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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