Author: "Aine McKillop" - Searchworks@Jio Institute Digital Library Search Results

40 results on '"Aine McKillop"'

1. Zinc-induced activation of GPR39 regulates glucose homeostasis through glucose-dependent insulinotropic polypeptide secretion from enteroendocrine K-cells

Author: Aine McKillop, Peter R. Flatt, Brian M Moran, Yasser Abdel-Wahab, and Michael G Miskelly
Subjects: 0301 basic medicine, medicine.medical_specialty, Chemistry, Insulin, medicine.medical_treatment, Clinical Biochemistry, Incretin, 030209 endocrinology & metabolism, Enteroendocrine cell, medicine.disease, Biochemistry, Glucagon, 03 medical and health sciences, 030104 developmental biology, 0302 clinical medicine, Endocrinology, Internal medicine, Diabetes mellitus, Knockout mouse, medicine, Glucose homeostasis, Receptor, Molecular Biology
Abstract: The role of Zn2+-sensing receptor GPR39 on glucose homeostasis and incretin regulation was assessed in enteroendocrine L- and K-cells. Anti-hyperglycaemic, insulinotropic and incretin secreting properties of Zn2+ were explored in normal, diabetic and incretin receptor knockout mice. Compared to intraperitoneal injection, oral administration of Zn2+ (50 μmol/kg body weight) with glucose (18 mmol/kg) in lean mice reduced the glycaemic excursion by 25–34% (p p p p 2+ lowered glucose by 24–31% (p p 2+ reduced glucose by 15–28% (p p p 2+ had no effect on responses of glucose-dependent insulinotropic polypeptide (GIP) receptor knockout mice. Consistent with this, Zn2+ had no effect on circulating total GLP-1 whereas GIP release was stimulated by 26% (p 2+ had a direct effect on GIP secretion from pGIPneo STC-1 cells, increasing GIP secretion by 1.3-fold. GPR39 is expressed on intestinal L- and K-cells, and stimulated GIP secretion plays an integral role in mediating enhanced insulin secretion and glucose tolerance following oral administration of Zn2+. This suggests development of potent and selective GPR39 agonists as a therapeutic approach for diabetes.
Published: 2019
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2. Development and characterisation of novel, enzymatically stable oxytocin analogues with beneficial antidiabetic effects in high fat fed mice

Author: Aine McKillop, Nigel Irwin, Andrew McCloskey, Peter R. Flatt, R. Charlotte Moffett, and Shruti Mohan
Subjects: 0301 basic medicine, Blood Glucose, Male, medicine.medical_treatment, Type 2 diabetes, Oxytocin, Biochemistry, chemistry.chemical_compound, Mice, 0302 clinical medicine, Insulin Secretion, Insulin, geography.geographical_feature_category, Protein Stability, Islet, Female, Beta cell, Oligopeptides, medicine.drug, Half-Life, medicine.medical_specialty, Biophysics, 030209 endocrinology & metabolism, Diet, High-Fat, Diabetes Mellitus, Experimental, 03 medical and health sciences, Islets of Langerhans, In vivo, Internal medicine, medicine, Animals, Hypoglycemic Agents, Obesity, Molecular Biology, Triglycerides, geography, Triglyceride, Cholesterol, HDL, Cholesterol, LDL, medicine.disease, Glucagon, 030104 developmental biology, Endocrinology, chemistry, Diabetes Mellitus, Type 2, Insulin Resistance, Energy Intake, Hormone
Abstract: Background There is growing evidence to support beneficial effects of the hypothalamic synthesised hormone, oxytocin, on metabolism. However, the biological half-life of oxytocin is short and receptor activation profile unspecific. Methods We have characterised peptide-based oxytocin analogues with structural modifications aimed at improving half-life and receptor specificity. Following extensive in vitro and in vivo characterisation, antidiabetic efficacy of lead peptides was examined in high fat fed (HFF) mice. Results Following assessment of stability against enzymatic degradation, insulin secretory activity, receptor activation profile and in vivo bioactivity, analogues 2 N (Ac-C ˂YIQNC >PLG-NH2) and D7R (( d -C)YIQNCYLG-NH2) were selected as lead peptides. Twice daily injection of either peptide for 22 days reduced body weight, energy intake, plasma glucose and insulin and pancreatic glucagon content in HFF mice. In addition, both peptides reduced total- and LDL-cholesterol, with concomitant elevations of HDL-cholesterol, and D7R also decreased triglyceride levels. The two oxytocin analogues improved glucose tolerance and insulin responses to intraperitoneal, and particularly oral, glucose challenge on day 22. Both oxytocin analogues enhanced insulin sensitivity, reduced HOMA-IR and increased bone mineral density. In terms of pancreatic islet histology, D7R reversed high fat feeding induced elevations of islet and beta cell areas, which was associated with reductions in beta cell apoptosis. Islet insulin secretory responsiveness was improved by 2 N, and especially D7R, treatment. Conclusion Novel, enzymatically stable oxytocin analogues exert beneficial antidiabetic effects in HFF mice. General significance These observations emphasise the, yet untapped, therapeutic potential of long-acting oxytocin-based agents for obesity and type 2 diabetes.
Published: 2020

3. Development of novel ligands for peptide GPCRs

Author: Finbarr O'Harte, Brian M Moran, and Aine McKillop
Subjects: 0301 basic medicine, endocrine system, Incretin, 030209 endocrinology & metabolism, Peptide, Ligands, Incretins, Glucagon-Like Peptide-1 Receptor, Receptors, G-Protein-Coupled, 03 medical and health sciences, chemistry.chemical_compound, 0302 clinical medicine, Insulin-Secreting Cells, Free fatty acid receptor 1, Drug Discovery, Animals, Humans, Hypoglycemic Agents, Pancreatic polypeptide, G protein-coupled receptor, Pharmacology, chemistry.chemical_classification, Fatty Acids, digestive, oral, and skin physiology, GPR120, Oxyntomodulin, 030104 developmental biology, Diabetes Mellitus, Type 2, chemistry, Biochemistry, Drug Design, Peptide YY, Peptides, hormones, hormone substitutes, and hormone antagonists
Abstract: Incretin based glucagon-like peptide-1 receptor (GLP-1R) agonists which target a G-protein coupled receptor (GPCR) are currently used in the treatment of type 2 diabetes. This review focuses on GPCRs from pancreatic β-cells, including GLP-1, glucose-dependent insulinotropic polypeptide (GIP), glucagon, somatostatin, pancreatic polypeptide (PP), cholecystokinin (CCK), peptide YY (PYY), oxyntomodulin (OXM) and ghrelin receptors. In addition, fatty acids GPCRs are thought to have an increasing role in regulating peptide secretions namely short fatty acids GPCR (GPR41, GPR43), medium chain fatty acid GPCR (GPR84), long chain fatty acid GPCR (GPR40, GPR120) and cannabinoid-like GPCR (GPR55, GPR119). Several pre-clinical and clinical trials are currently ongoing in peptide GPCR based therapies, including dual and triple agonist peptides which activate two or more GPCRs simultaneously.
Published: 2016
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4. Metabolic effects of orally administered small-molecule agonists of GPR55 and GPR119 in multiple low-dose streptozotocin-induced diabetic and incretin-receptor-knockout mice

Author: Aine McKillop, Brian M Moran, Noella Gormley, Yasser Abdel-Wahab, and Peter R. Flatt
Subjects: Male, 0301 basic medicine, medicine.medical_specialty, Endocrinology, Diabetes and Metabolism, G-protein-coupled receptors, Incretin, Biology, Glucose homeostasis, Incretins, Streptozocin, Article, Diabetes Mellitus, Experimental, Receptors, G-Protein-Coupled, Eating, Mice, 03 medical and health sciences, Abnormal cannabidiol, Insulin-Secreting Cells, Internal medicine, Diabetes mellitus, Multiple low-dose streptozotocin, Internal Medicine, medicine, Animals, Beta cell regeneration, Fatty acid agonists, Receptors, Cannabinoid, Mice, Knockout, Insulin secretion, Diabetes, Resorcinols, medicine.disease, Streptozotocin, Peptide Fragments, Pyrimidines, 030104 developmental biology, GPR119, Endocrinology, GPR55, Ethanolamines, Knockout mouse, Insulin Resistance, medicine.drug
Abstract: Aims/hypothesis Abnormal cannabidiol (Abn-CBD) and AS-1269574 are potent selective agonists for GPR55 and GPR119, respectively. The present study evaluated the actions and ability of these small-molecule agonists to counteract experimental diabetes in mice. Methods Diabetes was induced in NIH Swiss mice by five consecutive daily intraperitoneal injections of 40 mg/(kg body weight) streptozotocin. Diabetic mice received daily oral administration of Abn-CBD or AS-1269574 (0.1 μmol/kg) or saline vehicle (0.9% wt/vol. NaCl) over 28 days. Body weight, food intake, fluid intake, plasma glucose, insulin, glucose tolerance, insulin release, lipid profile and pancreatic morphology were examined. Mechanism of action of agonists was assessed in acute studies using incretin-receptor-knockout mice. Results Abn-CBD and AS-1269574 decreased plasma glucose (20–26%, p
Published: 2016
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5. Pharmacological potential of novel agonists for FFAR4 on islet and enteroendocrine cell function and glucose homeostasis

Author: Andrew McCloskey, Peter R. Flatt, Aine McKillop, and M.G. Miskelly
Subjects: Blood Glucose, Male, Agonist, medicine.drug_class, Enteroendocrine Cells, medicine.medical_treatment, Pharmaceutical Science, Incretin, Enteroendocrine cell, 02 engineering and technology, Pharmacology, 030226 pharmacology & pharmacy, Diabetes Mellitus, Experimental, Receptors, G-Protein-Coupled, Mice, 03 medical and health sciences, 0302 clinical medicine, Glucagon-Like Peptide 1, Insulin-Secreting Cells, Animals, Homeostasis, Hypoglycemic Agents, Insulin, Medicine, Glucose homeostasis, Secretion, Sulfonamides, geography, Aniline Compounds, geography.geographical_feature_category, business.industry, 021001 nanoscience & nanotechnology, Islet, Glucose, Diabetes Mellitus, Type 2, Sitagliptin, 0210 nano-technology, business, medicine.drug
Abstract: Background To investigate the metabolic effects of FFAR4-selective agonists on islet and enteroendocrine cell hormone release and the combined therapeutic effectiveness with DPP-IV inhibitors. Methods Insulinotropic activity and specificity of FFAR4 agonists were determined in clonal pancreatic BRIN-BD11 cells. Expression of FFAR4 was assessed by qPCR and western blotting following agonist treatment in BRIN-BD11 cells and by immunohistochemistry in mouse islets. Acute in-vivo effects of agonists was investigated after intraperitoneal (i.p.) or oral administration in lean and HFF-obese diabetic mice. Results GSK137647 (10–11–10–4 M) and Compound-A (10–10–10–4 M) stimulated insulin secretion at 5.6 mM (p Conclusions Specific FFAR4 agonism improves glucose tolerance through insulin and incretin secretion, with enhanced DPP-IV inhibition in combination with Sitagliptin. General significance These findings have for the first time demonstrated that selective FFAR4 activation regulates both islet and enteroendocrine hormone function with agonist combinational therapy, presenting a promising strategy for the treatment of type-2-diabetes.
Published: 2020
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6. GPR39 receptors and actions of trace metals on pancreatic beta cell function and glucose homoeostasis

Author: Brian M Moran, Yasser Abdel-Wahab, Aine McKillop, Srividya Vasu, and Peter R. Flatt
Subjects: inorganic chemicals, 0301 basic medicine, medicine.medical_specialty, Endocrinology, Diabetes and Metabolism, medicine.medical_treatment, 030209 endocrinology & metabolism, Biology, Cell Line, Receptors, G-Protein-Coupled, Mice, 03 medical and health sciences, 0302 clinical medicine, Endocrinology, In vivo, Insulin-Secreting Cells, Internal medicine, Glucose Intolerance, Cyclic AMP, Internal Medicine, medicine, Animals, Homeostasis, Insulin, Receptor, Cytotoxicity, Pancreatic islets, General Medicine, Trace Elements, Glucose, 030104 developmental biology, medicine.anatomical_structure, Hyperglycemia, Second messenger system, Calcium, Intracellular
Abstract: G-protein-coupled receptor 39 (GPR39) has been implicated in glucose homoeostasis, appetite control and gastrointestinal tract function.This study used clonal BRIN-BD11 cells and mouse pancreatic islets to assess the insulin-releasing actions of trace metals believed to act via GPR39, and the second messenger pathways involved in mediating their effects. Micromolar concentrations of Zn(2+), Cu(2+), Ni(2+) and Co(2+) were examined under normoglycaemic and hyperglycaemic conditions. Mechanistic studies investigated changes of intracellular Ca(2+), cAMP generation and assessment of cytotoxicity by LDH release. Cellular localisation of GPR39 was determined by double immunohistochemical staining.All trace metals (7.8-500 µmol/l) stimulated insulin release with Cu(2+) being the most potent in isolated islets, with an EC50 value of 87 μmol/l. Zn(2+) was the most selective with an EC50 value of 125 μmol/l. Enhancement of insulin secretion was also observed with Ni(2+) (179 μmol/l) and Co(2+) (190 μmol/l). These insulin-releasing effects were confirmed using clonal BRIN-BD11 cells which exhibited enhanced intracellular Ca(2+) (p 0.05-p 0.001) and cAMP generation (p 0.05-p 0.001) in response to trace metals. Oral administration of Zn(2+), Ni(2+) and Cu(2+) (50 µmol/kg together with 18 mmol/kg glucose) decreased the glycaemic excursion (p 0.05-p 0.01) and augmented insulin secretion (p 0.05-p 0.01) in NIH Swiss mice.This study has demonstrated the presence of GPR39 and the insulinotropic actions of trace metals on BRIN-BD11 cells and pancreatic beta cells, together with their antihyperglycaemic actions in vivo. These data suggest that development of agonists capable of specifically activating GPR39 may be a useful new therapeutic approach for diabetes management.
Published: 2015
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7. Tissue expression of DPP-IV in obesity-diabetes and modulatory effects on peptide regulation of insulin secretion

Author: Claire L. Stevenson, Brian M Moran, Aine McKillop, Yasser Abdel-Wahab, and Peter R. Flatt
Subjects: 0301 basic medicine, Blood Glucose, medicine.medical_specialty, animal structures, Physiology, Dipeptidyl Peptidase 4, 030209 endocrinology & metabolism, Peptide, Type 2 diabetes, Diet, High-Fat, Biochemistry, Dipeptidyl peptidase, 03 medical and health sciences, Cellular and Molecular Neuroscience, Islets of Langerhans, Mice, 0302 clinical medicine, Endocrinology, Insulin resistance, Glucagon-Like Peptide 1, Internal medicine, Diabetes mellitus, Insulin Secretion, medicine, Animals, Humans, Hypoglycemic Agents, Insulin, Obesity, chemistry.chemical_classification, geography, Dipeptidyl-Peptidase IV Inhibitors, geography.geographical_feature_category, biology, Chemistry, medicine.disease, Islet, Enzyme assay, Metformin, 030104 developmental biology, Glucose, Diabetes Mellitus, Type 2, Gene Expression Regulation, biology.protein, Insulin Resistance
Abstract: Dipeptidyl peptidase type 4 (DPP-4) inhibitors represent an important class of glucose-lowering drug for type 2 diabetes. DPP-4 enzyme activity has been observed to be significantly altered in type 2 diabetes. Here, the role of DPP-4 was examined in a high fat fed (HFF) mouse model of insulin resistance. HFF mice had an increased bodyweight (p .01), were hyperglycaemic (p .01) and hyperinsulinaemic (p .05). Compared to normal diet, HFF mice exhibited increased plasma DPP-4 activity (p .01). Tissue distribution patterns in lean and HFF mice demonstrated highest levels of DPP-4 activity in lung (20-26 μmol/min/mg protein) and small intestine (13-14 μmol/min/mg protein), and lowest activity in the spleen (3.8 μmol/min/mg protein). Modulation of DPP-4 activity by high fat feeding was observed in several tissues with increases in the lung (p .05), liver (p .05), kidney (p .05) and pancreas (p .05). With a high fat diet, DPP-4 gene expression was upregulated in the liver (p .001) and downregulated in the pancreas (p 0.001) and small intestine (p .001). Immunohistochemical analysis revealed increased DPP-4 immunostaining localised primarily in the pancreatic islets of HFF mice (p .01) with no change in islet GLP-1 expression. Treatment of HFF mice with metformin for 21-days resulted in inhibition of circulating DPP-4 activity (p .05), decreased blood glucose (p .05) and increased GLP-1 gene expression (p .001). These data indicate that DPP-4 is modulated in a tissue specific manner and is dependent on physiological conditions such as hyperglycaemia and insulin resistance, suggesting a significant role in disorders such as diabetes.
Published: 2017

8. Evaluation of the insulin-releasing and glucose-lowering effects of GPR120 activation in pancreaticβ-cells

Author: Brian M Moran, Yasser Abdel-Wahab, Peter R. Flatt, and Aine McKillop
Subjects: Blood Glucose, Agonist, medicine.medical_specialty, Docosahexaenoic Acids, medicine.drug_class, Endocrinology, Diabetes and Metabolism, medicine.medical_treatment, Cell Line, Diabetes Mellitus, Experimental, Receptors, G-Protein-Coupled, Mice, Endocrinology, Insulin-Secreting Cells, Internal medicine, Insulin Secretion, Cyclic AMP, Internal Medicine, medicine, Animals, Hypoglycemic Agents, Insulin, Cellular localization, geography, geography.geographical_feature_category, Dose-Response Relationship, Drug, business.industry, Pancreatic islets, alpha-Linolenic Acid, GPR120, Islet, Immunohistochemistry, Eicosapentaenoic acid, medicine.anatomical_structure, Eicosapentaenoic Acid, Docosahexaenoic acid, Female, business
Abstract: Aims To assess the potency and selectivity of various GPR120 agonists and to determine the cellular localization of GPR120 in clonal β-cells and pancreatic islets. Methods Insulin secretion and alterations in intracellular Ca2+ and cAMP response to glucose and GPR120 agonists, including endogenous agonists α-linolenic acid (ALA), docosahexaenoic acid (DHA), eicosapentaenoic acid (EPA) and a synthetic analogue (GW-9508), were examined using clonal pancreatic BRIN-BD11 cells, mouse pancreatic islets and in vivo studies using NIH Swiss mice. Cytotoxicity was assessed by lactate dehydrogenase release. Cellular localization of GPR120 was explored by double-staining immunohistochemistry. Results The most potent and selective GPR120 agonist tested was ALA (half maximum effective concentration 1.2 × 10−8 mol/l) with a maximum stimulation of insulin secretion of 53% at 10−4 mol/l (p
Published: 2014
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9. Evidence for inhibitory autocrine effects of proinsulin C-peptide on pancreaticβ-cell function and insulin secretion

Author: Aine McKillop, Yasser Abdel-Wahab, Ming T. Ng, and Peter R. Flatt
Subjects: medicine.medical_specialty, Endocrinology, Diabetes and Metabolism, Pancreatic islets, Insulin, medicine.medical_treatment, Biology, Peptide hormone, Endocrinology, medicine.anatomical_structure, Tolbutamide, Internal medicine, Internal Medicine, medicine, Diazoxide, Secretion, Autocrine signalling, Proinsulin, medicine.drug
Abstract: AIMS: Autocrine and paracrine regulatory mechanisms ensure integrated secretion of islet hormones that respond efficiently to changes in metabolic need. As proinsulin C-peptide exerts various biological effects and binds to cell membranes including insulin-secreting β cells, its physiological role in insulin release was examined.METHODS: Insulin releasing activity of human and rat C-peptides were studied in the clonal pancreatic cell line, BRIN-BD11, with findings substantiated using isolated islets and in vivo studies employing SWISS TO mice.RESULTS: Acute exposure of clonal β cells to human C-peptide resulted in concentration-dependent inhibitory effects on insulin secretion at 5.6 mM (p < 0.05-p < 0.001) and 16.7 mM (p < 0.01-p < 0.001) glucose. At physiologically relevant intra-islet concentrations (10(-9) -10(-6) M), C-peptide suppressed the insulin-secretory responses to a range of secretagogues acting at different points in the β cell stimulus-secretion coupling pathway including alanine (p < 0.05), Ca(2+) (p < 0.001), arginine (p < 0.05), tolbutamide (p < 0.001), glucagon-like peptide 1 (GLP-1) (p < 0.001), isobutylmethylxanthine (IBMX) (p < 0.01) and KCl (p < 0.05). Similar results were obtained using isolated mouse pancreatic islets. Human C-peptide (3 × 10(-7) M, p < 0.001), somatostatin-14 (3 × 10(-7) M, p < 0.01) and diazoxide (300 µM, p < 0.001) reduced both alanine and glucose-stimulated insulin release by 43, 25 and 48%, respectively. The effects of human C-peptide were reproduced using rat C-peptide I and II. C-peptide also inhibited in vivo glucose-stimulated insulin release and impaired glucose tolerance in mice.CONCLUSIONS: C-peptide is a biologically active endogenous peptide hormone that exerts inhibitory autocrine effects on pancreatic β-cell function. Mechanisms involving the activation of K(+) channels and a distal effect downstream of increased cytoplasmic Ca(2+) appear to be implicated in the inhibition of insulin secretion.
Published: 2014
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10. An evaluation of resource development and dissemination activities designed to promote problem-based learning at the University of Ulster

Author: Jacqueline M. McCormack, Catherine J. Hack, Sandra Sweetman, and Aine McKillop
Subjects: Cooperative learning, Instructional design, business.industry, Teaching method, Education, Engineering management, Resource (project management), Problem-based learning, Resource development, ComputingMilieux_COMPUTERSANDEDUCATION, Mathematics education, The Internet, Psychology, business, Curriculum
Abstract: The transition from traditional instruction to a problem-based approach to learning requires many changes for educators and for students. The aim of this project was to develop an online problem-based learning (PBL) resource centre to provide academic staff from across the University with support in incorporating PBL in their curriculum design. The resultant interactive resource centre (pbLRC) provides guidance and information on designing PBL. Within the pbLRC there are links to student-centred resources and a facility for sharing case studies. A range of dissemination activities, including workshops, seminars and the establishment of a PBL network, have been used to promote the use of the pbLRC. This paper describes the development of the pbLRC and evaluates its impact and the approaches taken to embedding PBL in academic practice across the University of Ulster.
Published: 2013
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11. Evaluation of the insulin releasing and antihyperglycaemic activities of GPR55 lipid agonists using clonal beta-cells, isolated pancreatic islets and mice

Author: Aine McKillop, Yasser Abdel-Wahab, Brian M Moran, and Peter R. Flatt
Subjects: Pharmacology, Agonist, medicine.medical_specialty, medicine.drug_class, medicine.medical_treatment, Pancreatic islets, Insulin, Biology, Endocannabinoid system, Endocrinology, medicine.anatomical_structure, In vivo, Internal medicine, medicine, Glucose homeostasis, Cannabinoid, Cellular localization
Abstract: Background and Purpose G-protein coupled receptor (GPR)55 is a novel lipid sensing receptor activated by both cannabinoid endogenous ligands (endocannabinoids) and other non-cannabinoid lipid transmitters. This study assessed the effects of various GPR55 agonists on glucose homeostasis. Experimental Approach Insulin secretion and changes in intracellular Ca2+ and cAMP in response to glucose and a range of GPR55 agonists [endogenous ligands (OEA, PEA), chemically synthetic cannabidiol (CBD) analogues (Abn-CBD, 0–1602), an analogue of rimonabant (AM-251) and antagonist (CBD)] were investigated in clonal BRIN-BD11 cells and mouse pancreatic islets. Cytotoxicity was assessed by LDH release, cellular localization by double-staining immunohistochemistry and in vivo effects assessed in mice. Key Results The most potent and selective GPR55 agonist was the synthetic CBD analogue, Abn-CBD (pEC50 10.33), maximum stimulation of 67% at 10−4 mol·L−1 (P < 0.001) in BRIN-BD11 cells. AM-251 (pEC50 7.0), OEA (pEC50 7.0), 0–1602 (pEC50 7.3) and PEA (pEC50 6.0) stimulated insulin secretion. Results were corroborated by islet studies, with no cytotoxic effects. Concentration-dependent insulin secretion by GPR55 agonists was glucose-sensitive and accompanied by elevations of [Ca2+]i (P < 0.01–P < 0.001) and cAMP (P < 0.05–P < 0.01). GPR55 agonists exhibited insulinotropic and glucose lowering activity in vivo. GPR55 was expressed on BRIN-BD11 cells and confined to islet beta cells with no distribution on alpha cells. Conclusion and Implications These results demonstrate GPR55 is distributed in pancreatic beta cells and is a strong activator of insulin secretion, with glucose-lowering effects in vivo. Development of agents agonizing the GPR55 receptor may have therapeutic potential in the treatment of type 2 diabetes.
Published: 2013
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12. Emerging Applications of Metabolomic and Genomic Profiling in Diabetic Clinical Medicine

Author: Aine McKillop and Peter R. Flatt
Subjects: Blood Glucose, medicine.medical_specialty, Endocrinology, Diabetes and Metabolism, 030209 endocrinology & metabolism, Genomics, Genome-wide association study, Review, Computational biology, Disease, Antioxidants, 03 medical and health sciences, Diabetes mellitus genetics, 0302 clinical medicine, Metabolomics, Adipokines, Diabetes mellitus, Internal medicine, Diabetes Mellitus, Internal Medicine, medicine, Humans, Insulin, Genetic Predisposition to Disease, Genotyping, 030304 developmental biology, Genetic association, Glycated Hemoglobin, Inflammation, Metabolic Syndrome, Advanced and Specialized Nursing, 0303 health sciences, Reviews/Commentaries/ADA Statements, business.industry, Histocompatibility Antigens Class II, Alanine Transaminase, gamma-Glutamyltransferase, medicine.disease, 3. Good health, Oxidative Stress, C-Reactive Protein, Diabetes Mellitus, Type 1, Endocrinology, Diabetes Mellitus, Type 2, business, Biomarkers, Genome-Wide Association Study
Abstract: Clinical and epidemiological metabolomics provides a unique opportunity to look at genotype-phenotype relationships as well as the body\x{2019}s responses to environmental and lifestyle factors. Fundamentally, it provides information on the universal outcome of influencing factors on disease states and has great potential in the early diagnosis, therapy monitoring, and understanding of the pathogenesis of disease. Diseases, such as diabetes, with a complex set of interactions between genetic and environmental factors, produce changes in the body\x{2019}s biochemical profile, thereby providing potential markers for diagnosis and initiation of therapies. There is clearly a need to discover new ways to aid diagnosis and assessment of glycemic status to help reduce diabetes complications and improve the quality of life. Many factors, including peptides, proteins, metabolites, nucleic acids, and polymorphisms, have been proposed as putative biomarkers for diabetes. Metabolomics is an approach used to identify and assess metabolic characteristics, changes, and phenotypes in response to influencing factors, such as environment, diet, lifestyle, and pathophysiological states. The specificity and sensitivity using metabolomics to identify biomarkers of disease have become increasingly feasible because of advances in analytical and information technologies. Likewise, the emergence of high-throughput genotyping technologies and genome-wide association studies has prompted the search for genetic markers of diabetes predisposition or susceptibility. In this review, we consider the application of key metabolomic and genomic methodologies in diabetes and summarize the established, new, and emerging metabolomic and genomic biomarkers for the disease. We conclude by summarizing future insights into the search for improved biomarkers for diabetes research and human diagnostics.
Published: 2011
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13. Insulinotropic actions of nateglinide in type 2 diabetic patients and effects on dipeptidyl peptidase-IV activity and glucose-dependent insulinotropic polypeptide degradation

Author: John R. Lindsay, Aine McKillop, Brian D. Green, Finbarr O'Harte, Nicola A. Duffy, Steven Patterson, P. M. Bell, and Peter R. Flatt
Subjects: Male, medicine.medical_specialty, Pyrrolidines, Dipeptidyl Peptidase 4, Phenylalanine, Endocrinology, Diabetes and Metabolism, medicine.medical_treatment, Blood sugar, Adamantane, Nateglinide, Gastric Inhibitory Polypeptide, Type 2 diabetes, chemistry.chemical_compound, Endocrinology, Cyclohexanes, Internal medicine, Diabetes mellitus, Insulin Secretion, Nitriles, medicine, Humans, Insulin, Vildagliptin, Dipeptidyl-Peptidase IV Inhibitors, C-peptide, business.industry, General Medicine, Middle Aged, medicine.disease, Postprandial, Diabetes Mellitus, Type 2, chemistry, Female, business, medicine.drug
Abstract: BackgroundNateglinide restores early-phase insulin secretion to feeding and reduces postprandial hyperglycaemia in type 2 diabetes. This study evaluated the effects of nateglinide on dipeptidyl peptidase-IV (DPP-IV) activity and glucose-dependent insulinotropic polypeptide (GIP) degradation.Research design and methodsBlood samples were collected from type 2 diabetic subjects (n=10, fasting glucose 9.36±1.2 mmol/l) following administration of oral nateglinide (120 mg) 10 min prior to a 75 g oral glucose load in a randomised crossover design.ResultsPlasma glucose reached 18.2±1.7 and 16.7±1.7 mmol/l at 90 min in control and placebo groups (PPPPPin vitro. Comparison of in vitro inhibition of DPP-IV by nateglinide and vildagliptin revealed IC50 values of 17.1 and 2.1 μM respectively.ConclusionsAlthough considerably less potent than specified DPP-IV inhibitors, the possibility that some of the beneficial actions of nateglinide are indirectly mediated through DPP-IV inhibition and increased bioavailability of GIP and other incretins merits consideration.
Published: 2009
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14. Effect of RU486 on Hepatic and Adipocyte Gene Expression Improves Diabetes Control in Obesity-type 2 Diabetes

Author: Victor A. Gault, Norma Frizzell, Peter R. Flatt, AI Taylor, and Aine McKillop
Subjects: Blood Glucose, Male, medicine.medical_specialty, Adipose Tissue, White, Endocrinology, Diabetes and Metabolism, Clinical Biochemistry, Mice, Obese, Adipose tissue, Type 2 diabetes, White adipose tissue, Biology, Biochemistry, Drug Administration Schedule, Mice, chemistry.chemical_compound, Endocrinology, Glucocorticoid receptor, Diabetes mellitus, Internal medicine, Adipocyte, Adipocytes, medicine, Animals, Insulin, Obesity, RNA, Messenger, Pancreas, Triglycerides, Epididymis, Glucose tolerance test, medicine.diagnostic_test, Body Weight, Biochemistry (medical), Fasting, Feeding Behavior, General Medicine, Glucose Tolerance Test, medicine.disease, Mifepristone, Diabetes Mellitus, Type 2, Gene Expression Regulation, Liver, chemistry, Glycogenesis, hormones, hormone substitutes, and hormone antagonists
Abstract: Cortisol has wide-ranging actions, namely in gluconeogenesis and glycogenesis and exerts its effects through the glucocorticoid receptor. In the present study, we examined effects of glucocorticoid receptor blockade on type 2 diabetes control using the antagonist, RU486. Obese diabetic mice received daily injections of vehicle or RU486 over 28 days. Food intake, body weight, and plasma glucose were measured frequently. At 28 days, glucose tolerance, insulin sensitivity, and plasma triglycerides were assessed. Epididymal white adipose tissue and liver were excised for measurement of gene expression. Daily administration of RU486 had no effect on body weight or food intake, but plasma glucose concentrations were significantly lowered (1.4-1.6-fold; p
Published: 2009
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15. Recent Developments in the Search for Biomarkers for the Diagnosis and Monitoring of Diabetes

Author: Peter R. Flatt and Aine McKillop
Subjects: Endocrinology, Diabetes and Metabolism, Systems biology, Biochemistry (medical), Amylin, General Medicine, Disease, Biology, Proteomics, Bioinformatics, medicine.disease, Metabolomics, Insulin resistance, Glycation, Diabetes mellitus, Drug Discovery, medicine, Immunology and Allergy
Abstract: In the fields of genomic, proteomic and metabolomic technologies many advances have been made in the past few years for the early diagnosis and monitoring of diseases such as diabetes mellitus. As diabetes is afflicting affluent and developing societies throughout the world and is fuelled by aging demographics and the recent increase of obesity and related insulin resistance, there is a clear need to discover effective agents for diagnosing the disease and controlling glycaemic status. Biological markers such as peptides, proteins, metabolites, nucleic acids and polymorphisms have been proposed as novel exciting biomarkers. Patents have been filed demonstrating altered levels of proteins such as pancreatic polypeptide in beta cell failure and fibronectin in insulin resistance. Much interest has focused on the potential of glycosylated proteins such as glycated insulin, glycosylated amylin, C-terminally truncated form of the receptor for advanced glycation end-products, and glycated LDL antibodies. The emergence of genomic analysis is now complemented by systems biology and computational methods that can unravel large amounts of heterogeneous genetic and genomic information to produce meaningful results. Many patents have been filed that claim to estimate the susceptibility or predisposition of metabolic disease such as diabetes. New genomic technologies such as transcriptional profiling and proteomics have been shown to be significant in identifying and validating biomarkers, and systems biology has shown great promise in unravelling the complexities of genomic, proteomic and metabolomic technologies.
Published: 2008
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16. Sub-chronic administration of the 11β-HSD1 inhibitor, carbenoxolone, improves glucose tolerance and insulin sensitivity in mice with diet-induced obesity

Author: Victor A. Gault, Aine McKillop, AI Taylor, Nigel Irwin, and Peter R. Flatt
Subjects: Blood Glucose, Male, medicine.medical_specialty, medicine.medical_treatment, Clinical Biochemistry, Carbenoxolone, Adipose tissue, Type 2 diabetes, Biology, Biochemistry, Eating, Mice, Receptors, Glucocorticoid, Insulin resistance, Glucocorticoid receptor, Internal medicine, 11-beta-Hydroxysteroid Dehydrogenase Type 1, medicine, Animals, Insulin, Obesity, Molecular Biology, Saline, Reverse Transcriptase Polymerase Chain Reaction, Body Weight, Glucose Tolerance Test, medicine.disease, Dietary Fats, Endocrinology, Metabolic control analysis, Insulin Resistance, Corticosterone, medicine.drug
Abstract: We have examined the metabolic effects of daily administration of carbenoxolone (CBX), a naturally occurring 11β-hydroxysteroid dehydrogenase (11β-HSD1) inhibitor, in mice with high fat diet-induced insulin resistance and obesity. Eight-week-old male Swiss TO mice placed on a synthetic high fat diet received daily intraperitoneal injections of either saline vehicle or CBX over a 16-day period. Daily administration of CBX had no effect on food intake, but significantly lowered body weight (1.1- to 1.2-fold) compared to saline-treated controls. Non-fasting plasma glucose levels were significantly decreased (1.6-fold) by CBX treatment on day 4 and remained lower throughout the treatment period. Circulating plasma corticosterone levels were not significantly altered by CBX treatment. Plasma glucose concentrations of CBX-treated mice were significantly reduced (1.4-fold) following an intraperitoneal glucose load compared with saline controls. Similarly, after 16-day treatment with CBX, exogenous insulin evoked a significantly greater reduction in glucose concentrations (1.4- to 1.8-fold). 11β-HSD1 gene expression was significantly down-regulated in liver, whereas glucocorticoid receptor gene expression was increased in both liver and adipose tissue following CBX treatment. The reduced body weight and improved metabolic control in mice with high fat diet-induced obesity upon daily CBX administration highlights the potential value of selective 11β-HSD1 inhibition as a new route for the treatment of type 2 diabetes and obesity.
Published: 2008
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17. G protein-coupled receptors: signalling and regulation by lipid agonists for improved glucose homoeostasis

Author: Peter R. Flatt, Aine McKillop, and Brian M Moran
Subjects: 0301 basic medicine, Blood Glucose, Gs alpha subunit, biology, Endocrinology, Diabetes and Metabolism, Gi alpha subunit, GPR120, General Medicine, Lipids, Receptors, G-Protein-Coupled, 03 medical and health sciences, 030104 developmental biology, Endocrinology, Gq alpha subunit, Biochemistry, Free fatty acid receptor 1, Internal Medicine, biology.protein, cAMP-dependent pathway, Animals, Homeostasis, Humans, Protein kinase A, G protein-coupled receptor, Signal Transduction
Abstract: G protein-coupled receptors (GPCRs) play a pivotal role in cell signalling, controlling many processes such as immunity, growth, cellular differentiation, neurological pathways and hormone secretions. Fatty acid agonists are increasingly recognised as having a key role in the regulation of glucose homoeostasis via stimulation of islet and gastrointestinal GPCRs. Downstream cell signalling results in modulation of the biosynthesis, secretion, proliferation and anti-apoptotic pathways of islet and enteroendocrine cells. GPR40 and GPR120 are activated by long-chain fatty acids (>C12) with both receptors coupling to the Gαq subunit that activates the Ca(2+)-dependent pathway. GPR41 and GPR43 are stimulated by short-chain fatty acids (C2-C5), and activation results in binding to Gαi that inhibits the adenylyl cyclase pathway attenuating cAMP production. In addition, GPR43 also couples to the Gαq subunit augmenting intracellular Ca(2+) and activating phospholipase C. GPR55 is specific for cannabinoid endogenous agonists (endocannabinoids) and non-cannabinoid fatty acids, which couples to Gα12/13 and Gαq proteins, leading to enhancing intracellular Ca(2+), extracellular signal-regulated kinase 1/2 (ERK) phosphorylation and Rho kinase. GPR119 is activated by fatty acid ethanolamides and binds to Gαs utilising the adenylate cyclase pathway, which is dependent upon protein kinase A. Current research indicates that GPCR therapies may be approved for clinical use in the near future. This review focuses on the recent advances in preclinical diabetes research in the signalling and regulation of GPCRs on islet and enteroendocrine cells involved in glucose homoeostasis.
Published: 2015

18. Activation of GPR120 by lipid agonists modulates glucagon secretion in pancreatic islets and improves glucose tolerance in mice

Author: Peter R. Flatt, Noella Gormley, and Aine McKillop
Subjects: medicine.medical_specialty, Endocrinology, medicine.anatomical_structure, Chemistry, Pancreatic islets, Internal medicine, medicine, Glucagon secretion, GPR120
Published: 2015
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19. Meal-dependent Regulation of Circulating Glycated Insulin in Type 2 Diabetic Subjects

Author: Peter R. Flatt, John R. Lindsay, KI Mahood, Finbarr O'Harte, Aine McKillop, S Au, and P. M. Bell
Subjects: Blood Glucose, Male, medicine.medical_specialty, Time Factors, Endocrinology, Diabetes and Metabolism, medicine.medical_treatment, Clinical Biochemistry, Type 2 diabetes, Biochemistry, Enteral administration, Endocrinology, Insulin resistance, Insulin-Secreting Cells, Internal medicine, medicine, Homeostasis, Humans, Insulin, Glucose homeostasis, Meal, C-Peptide, business.industry, Biochemistry (medical), General Medicine, Carbohydrate, medicine.disease, Parenteral nutrition, Diabetes Mellitus, Type 2, Food, Female, business
Abstract: There is mounting evidence that elevated circulating concentrations of glycated insulin play a role in insulin resistance in type 2 diabetes. This study evaluated the secretion of glycated insulin in response to enteral stimulation in type 2 diabetic subjects. Following a mixed meal (450 kcal; 44 % carbohydrate; 40 % fat; 16 % protein), glycated insulin rose 10-fold to peak (60 min) at 104.5 +/- 25.0 pmol/l (p0.001), representing 22 % total circulating insulin. The response paralleled early rises in insulin and C-peptide, which peaked at 90 min and were more protracted. Maximum glucose concentrations were observed at 50 min. These data indicate that type 2 diabetic subjects exhibit a rapid meal-induced release of glycated insulin from readily releasable pancreatic beta-cell stores, which might contribute to impaired glucose homeostasis following enteral nutrition.
Published: 2006
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20. Meal-induced 24-hour profile of circulating glycated insulin in type 2 diabetic subjects measured by a novel radioimmunoassay

Author: Mark Mooney, Aine McKillop, Peter R. Flatt, Patrick M. Bell, John R. Lindsay, and Finbarr O'Harte
Subjects: Blood Glucose, Male, medicine.medical_specialty, Glycosylation, Endocrinology, Diabetes and Metabolism, medicine.medical_treatment, Radioimmunoassay, Enzyme-Linked Immunosorbent Assay, Type 2 diabetes, Eating, Endocrinology, Internal medicine, Blood plasma, Intermittent fasting, medicine, Homeostasis, Humans, Insulin, Pancreatic hormone, Morning, Meal, business.industry, Middle Aged, Postprandial Period, medicine.disease, Circadian Rhythm, Diet, Diabetes Mellitus, Type 2, Basal (medicine), Female, business
Abstract: Increasing evidence supports a role for glycated insulin in the insulin-resistant state of type 2 diabetes. We measured 24-hour profiles of plasma glycated insulin, using a novel radioimmunoassay (RIA), to evaluate the effects of meal stimulation and intermittent fasting on circulating concentrations of plasma glycated insulin in type 2 diabetes. Patients (n = 6; hemoglobin A(1c) [HbA(1c)], 7.2% +/- 0.6%; fasting plasma glucose, 7.4 +/- 0.7 mmol/L; body mass index [BMI], 35.7 +/- 3.5 kg/m(2); age, 56.3 +/- 4.4 years) were admitted for 24 hours and received a standardized meal regimen. Half-hourly venous samples were taken for plasma glycated insulin, glucose, insulin, and C-peptide concentrations between 8 Am and midnight and 2-hourly overnight. The mean plasma glycated insulin concentration over 24 hours was 27.8 +/- 1.2 pmol/L with a mean ratio of insulin:glycated insulin of 11:1. Circulating glucose, insulin, C-peptide, and glycated insulin followed a basal and meal-related pattern with most prominent increments following breakfast, lunch, and evening meal, respectively. The mean concentrations of glycated insulin during the morning, afternoon, evening, and night-time periods were 24.4 +/- 2.5, 28.7 +/- 2.3, 31.1 +/- 2.1, and 26.2 +/- 1.5 pmol/L, respectively, giving significantly higher molar ratios of insulin:glycated insulin of 18.0:1, 14.2:1, and 12.7:1 compared with 7.01 at night (P < 0.01 to P < 0.001). These data demonstrate that glycated insulin circulates at relatively high concentrations in type 2 diabetes with a diurnal pattern of basal and meal-stimulated release. A higher proportion of glycated insulin circulates at night suggestive of differences in metabolic clearance compared with native insulin. (C) 2003 Elsevier Inc. All rights reserved.
Published: 2003
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21. Evaluation of the site(s) of glycation in human proinsulin by ion-trap LCQ electrospray ionization mass spectrometry

Author: Peter R. Flatt, Angela Meade, Finbarr O'Harte, and Aine McKillop
Subjects: endocrine system, Glycosylation, Time Factors, Protein Conformation, Physiology, Electrospray ionization, Molecular Sequence Data, Clinical Biochemistry, Peptide, Mass spectrometry, Biochemistry, Mass Spectrometry, Dithiothreitol, Cellular and Molecular Neuroscience, chemistry.chemical_compound, Endocrinology, Glycation, Humans, Amino Acid Sequence, Peptide sequence, Chromatography, High Pressure Liquid, Proinsulin, chemistry.chemical_classification, Binding Sites, Chromatography, Molecular Structure, Chemistry, Peptide Fragments, hormones, hormone substitutes, and hormone antagonists
Abstract: The glycation of beta cell proteins is known to occur under hyperglycemic states. The site(s) of glycation in human proinsulin was investigated following exposure to a hyperglycemic environment under reducing conditions in vitro. Proinsulin and glycated proinsulin were separated by reversed-phase high-performance liquid chromatography (R-P-HPLC) and identified using LCQ ion-trap electrospray ionization mass spectrometry. This revealed a major peak (>70% total) of monoglycated proinsulin (M-r 9552.2 Da), a second peak (approximately 27%) of nonglycated proinsulin (M-r 9389.8 Da), and a third minor peptide peak (approximately 3%) corresponding to diglycated proinsulin (M-r 9717.9 Da). Following reduction of disulphide bridges with dithiothreitol, intact peptides were incubated with endoproteinase Glu-C to release nine daughter fragments for LC-MS analysis. This strategy revealed an N-terminal fragment of monoglycated proinsulin Phe(1) Glu(13), which contained a single glucitol adduct (M-r 1642.0 Da). A similar treatment of small amounts of purified diglycated proinsulin revealed a fragment with Phe(1)-Glu(13) linked by a disulphide bridge to Gln(70)-Glu(82) containing two glucitol adducts (M-r 3292.7 Da). In summary, these studies indicate that the major site of glycation in proinsulin, like insulin, is the amino terminal Phe(1) residue. However, small amounts of diglycated proinsulin occur naturally, involving an additional site of glycation located between Gln(70) and Glu(82). (C) 2002 Elsevier Science B.V. All rights reserved.
Published: 2003
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22. Demonstration of increased concentrations of circulating glycated insulin in human Type 2 diabetes using a novel and specific radioimmunoassay

Author: Aine McKillop, John R. Lindsay, Peter R. Flatt, P. M. Bell, Finbarr O'Harte, and Mark Mooney
Subjects: Glycation End Products, Advanced, Male, medicine.medical_specialty, Glycosylation, Endocrinology, Diabetes and Metabolism, medicine.medical_treatment, Radioimmunoassay, Serum albumin, Type 2 diabetes, Human type, Glycation, Internal medicine, Diabetes mellitus, Internal Medicine, medicine, Humans, Insulin, Glycated Serum Albumin, Serum Albumin, biology, business.industry, Middle Aged, medicine.disease, Specific radioimmunoassay, Endocrinology, Diabetes Mellitus, Type 2, biology.protein, Female, Glycated insulin, business
Abstract: Glycation of insulin, resulting in impaired bioactivity, has been shown within pancreatic beta cells. We have used a novel and specific radioimmunoassay to detect glycated insulin in plasma of Type 2 diabetic subjects.Blood samples were collected from 102 Type 2 diabetic patients in three main categories: those with good glycaemic control with a HbA(1c) less than 7%, moderate glycaemic control (HbA(1c) 7-9%) and poor glycaemic control (HBA(1c) greater than 9%). We used 75 age- and sex-matched non-diabetic subjects as controls. Samples were analysed for HbA(1c), glucose and plasma concentrations of glycated insulin and insulin.Glycated insulin was readily detected in control and Type 2 diabetic subjects. The mean circulating concentration of glycated insulin in control subjects was 12.6+/-0.9 pmol/l ( n=75). Glycated insulin in the good, moderate and poorly controlled diabetic groups was increased 2.4-fold ( p0.001, n=44), 2.2-fold ( p0.001, n=41) and 1.1-fold ( n=17) corresponding to 29.8+/-5.4, 27.3+/-5.7 and 13.5+/-2.9 pmol/l, respectively.Glycated insulin circulates at noticeably increased concentrations in Type 2 diabetic subjects.
Published: 2003
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23. Demonstration of Glycated Insulin in Human Diabetic Plasma and Decreased Biological Activity Assessed by Euglycemic-Hyperinsulinemic Clamp Technique in Humans

Author: Patrick M. Bell, Christopher R. Barnett, Helene McNulty, M. Ivan Wiggam, AC Boyd, C. N. Ennis, Finbarr O'Harte, Mark Mooney, Peter R. Flatt, Jane T. McCluskey, Aine McKillop, Raymond Gamble, Brian Sheridan, John R. Lindsay, and Steven J. Hunter
Subjects: Blood Glucose, Male, Spectrometry, Mass, Electrospray Ionization, medicine.medical_specialty, Glycosylation, Endocrinology, Diabetes and Metabolism, Glucose uptake, medicine.medical_treatment, CHO Cells, Type 2 diabetes, Binding, Competitive, Cricetinae, Hyperinsulinism, Internal medicine, Diabetes mellitus, Blood plasma, Internal Medicine, medicine, Animals, Humans, Insulin, Lipolysis, Chromatography, High Pressure Liquid, Pancreatic hormone, Glycated Hemoglobin, Chemistry, Glucose clamp technique, medicine.disease, Endocrinology, Diabetes Mellitus, Type 2, Glucose Clamp Technique
Abstract: The presence and biological significance of circulating glycated insulin has been evaluated by high-pressure liquid chromatography (HPLC), electrospray ionization mass spectrometry (ESI-MS), radioimmunoassay (RIA), receptor binding, and hyperinsulinemic-euglycemic clamp techniques. ESI-MS analysis of an HPLC-purified plasma pool from four male type 2 diabetic subjects (HbA(1c) 8.1 +/- 0.2%, plasma glucose 8.7 +/- 1.3 mmol/l [means +/- SE]) revealed two major insulin-like peaks with retention times of 14-16 min. After spectral averaging, the peak with retention time of 14.32 min exhibited a prominent triply charged (M+3H)(3+) species at 1,991.1 m/z, representing monoglycated insulin with an intact M(r) of 5,970.3 Da. The second peak (retention time 15.70 min) corresponded to native insulin (M(r) 5,807.6 Da), with the difference between the two peptides (162.7 Da) representing a single glucitol adduct (theoretical 164 Da). Measurement of glycated insulin in plasma of type 2 diabetic subjects by specific RIA gave circulating levels of 10.1 +/- 2.3 pmol/l, corresponding to approximately 9% total insulin. Biological activity of pure synthetic monoglycated insulin (insulin B-chain Phe(1)-glucitol adduct) was evaluated in seven overnight-fasted healthy nonobese male volunteers using two-step euglycemic-hyperinsulinemic clamps (2 h at 16.6 micro g x kg(-1) x min(-1), followed by 2 h at 83.0 micro g x kg(-1) x min(-1); corresponding to 0.4 and 2.0 mU x kg(-1) x min(-1)). At the lower dose, the exogenous glucose infusion rates required to maintain euglycemia during steady state were significantly lower with glycated insulin (P < 0.01) and approximately 70% more glycated insulin was required to induce a similar rate of insulin-mediated glucose uptake. Maximal responses at the higher rates of infusion were similar for glycated and control insulin. Inhibitory effects on endogenous glucose production, insulin secretion, and lipolysis, as indicated by measurements of C-peptide, nonesterified free fatty acids, and glycerol, were also similar. Receptor binding to CHO-T cells transfected with human insulin receptor and in vivo metabolic clearance revealed no differences between glycated and native insulin, suggesting that impaired biological activity is due to a postreceptor effect. The present demonstration of glycated insulin in human plasma and related impairment of physiological insulin-mediated glucose uptake suggests a role for glycated insulin in glucose toxicity and impaired insulin action in type 2 diabetes.
Published: 2003
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24. Evaluation of Glycated Insulin in Diabetic Animals Using Immunocytochemistry and Radioimmunoassay

Author: Patrick Harriott, Peter R. Flatt, Finbarr O'Harte, Mark Mooney, and Aine McKillop
Subjects: Male, medicine.medical_specialty, Glycosylation, Hydrocortisone, medicine.medical_treatment, Radioimmunoassay, Biophysics, Mice, Obese, Biochemistry, Eating, Mice, Insulin resistance, Glycation, Internal medicine, Diabetes mellitus, Diabetes Mellitus, medicine, Animals, Insulin, Rats, Wistar, Pancreas, Molecular Biology, Chemistry, Pancreatic islets, Cell Biology, medicine.disease, Immunohistochemistry, Rats, Glucose, Endocrinology, medicine.anatomical_structure, medicine.drug
Abstract: Glycated insulin was evaluated in plasma and biological tissues of diabetic animal models by immuno. cytochemistry (ICC) and a novel radioimmunoassay. Glycated insulin circulated at 0.10 +/-0.04 ng/ml and 2.20 +/-0.14 ng/ml in lean and diabetic obese (ob/ob) mice, corresponding to 12.5 and 9.8% total plasma insulin, respectively. The concentration of glycated insulin was elevated 22-fold in obese mice compared to controls (P
Published: 2001
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25. Structure, antihyperglycemic activity and cellular actions of a novel diglycated human insulin

Author: P Hojrup, Yasser Abdel-Wahab, Aine McKillop, J M Conlon, Christopher R. Barnett, Peter R. Flatt, Finbarr O'Harte, AC Boyd, and Helene McNulty
Subjects: Blood Glucose, Male, medicine.medical_specialty, Glycosylation, Physiology, medicine.medical_treatment, Mice, Inbred Strains, Deoxyglucose, Biochemistry, Mass Spectrometry, Mice, Cellular and Molecular Neuroscience, Endocrinology, Glycation, Internal medicine, Mole, medicine, Animals, Humans, Insulin, Glucose homeostasis, Amino Acids, Chromatography, High Pressure Liquid, Glycoproteins, Edman degradation, Chemistry, Serine Endopeptidases, Biological Transport, Muscle, Smooth, Liter, Glucose, Hyperglycemia, Blood sugar regulation, Digestion, Glycogen, Injections, Intraperitoneal
Abstract: Udgivelsesdato: 2000-Oct Human insulin was glycated under hyperglycemic reducing conditions and a novel diglycated form (M(r) 6135.1 Da) was purified by RP-HPLC. Endoproteinase Glu-C digestion combined with mass spectrometry and automated Edman degradation localized glycation to Gly(1) and Phe(1) of the insulin A- and B-chains, respectively. Intraperitoneal (i.p.) administration of diglycated insulin to mice alone or in combination with glucose (7 nmol/kg) resulted in a 43-61% and 11-34% reduction in glucose lowering activity, respectively, compared with native insulin. Consistent with these findings, diglycated insulin (10(-9) to 10(-7) mol/liter) was 22-38% less effective (P < 0.001) than native insulin in stimulating glucose uptake, glucose oxidation and glycogen production in isolated mouse abdominal muscle.
Published: 2000
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26. Production and characterization of specific antibodies for evaluation of glycated insulin in plasma and biological tissues

Author: AC Boyd, Mark Mooney, Aine McKillop, Janie McCluskey, Finbarr O'Harte, and Peter R. Flatt
Subjects: Male, medicine.medical_specialty, Endocrinology, Diabetes and Metabolism, medicine.medical_treatment, Guinea Pigs, Radioimmunoassay, Sensitivity and Specificity, Diabetes Mellitus, Experimental, Epitopes, Islets of Langerhans, Endocrinology, Glycation, Diabetes mellitus, Internal medicine, medicine, Animals, Insulin, Rats, Wistar, Chromatography, High Pressure Liquid, Proinsulin, Antiserum, biology, Chemistry, Immune Sera, medicine.disease, Rats, Polyclonal antibodies, Antibody Formation, biology.protein, Immunization, Rabbits, Carrier Proteins, Keyhole limpet hemocyanin
Abstract: Previous studies have shown that glycation of insulin occurs in pancreatic beta-cells under conditions of hyperglycaemia and that the site of glycation is the N-terminal Phe(1) of the insulin B-chain. To enable evaluation of glycated insulin in diabetes, specific antibodies were raised in rabbits and guinea-pigs by using two synthetic peptides (A: Phe-Val-Asn-Gln-His-Leu-Cys-Tyr, and B: Phe-Val-Asn-Gln-His-Leu-Tyr-Lys) modified by N-terminal glycation and corresponding closely to the N-terminal sequence of the glycated human insulin B-chain. For immunization, the glycated peptides were conjugated either to keyhole limpet haemocyanin or ovalbumin using glutaraldehyde, m-maleimidobenzoyl-N-hydroxysuccinimide ester or 1-ethyl-3-(3-dimethylamino propyl) carbodiimide hydrochloride. Antibody titration curves, obtained using I(125)-tyrosylated tracer prepared from glycated peptide A, revealed high-titre antisera in five groups of animals immunized for 8-28 weeks. The highest titres were observed in rabbits and guinea-pigs immunized with peptide B coupled to ovalbumin using glutaraldehyde. Under radioimmunoassay conditions, these antisera exhibited effective dose (median) (ED(50)) values for glycated insulin of 0.3-15 ng/ml and 0.9-2.5 ng/ml respectively, with negligible cross-reactivity against insulin or other islet peptides. The degree of cross-reaction with glycated proinsulin was approximately 50%. Glycated insulin in plasma of control and hydrocortisone-treated diabetic rats measured using rabbit 3 antiserum (1:10 000 dilution; sensitivity
Published: 2000
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27. Activation of GPR119 by fatty acid agonists augments insulin release from clonal β-cells and isolated pancreatic islets and improves glucose tolerance in mice

Author: Yasser Abdel-Wahab, Brian M Moran, Aine McKillop, and Peter R. Flatt
Subjects: Agonist, medicine.medical_specialty, Pancreatic Polypeptide-Secreting Cells, medicine.drug_class, Pyridones, medicine.medical_treatment, Clinical Biochemistry, Oleic Acids, Biology, Biochemistry, Cell Line, Receptors, G-Protein-Coupled, Oleoylethanolamide, chemistry.chemical_compound, Mice, Structure-Activity Relationship, Internal medicine, Insulin-Secreting Cells, Insulin Secretion, medicine, Glucose homeostasis, Animals, Insulin, Receptor, Molecular Biology, Glucose tolerance test, Oxadiazoles, medicine.diagnostic_test, Dose-Response Relationship, Drug, Pancreatic islets, Fatty Acids, Glucose Tolerance Test, Endocrinology, medicine.anatomical_structure, Pyrimidines, chemistry, Ethanolamines, Endocannabinoids
Abstract: G-protein coupled receptor 119 (GPR119) is emerging as a potential target for the treatment of type 2 diabetes with beneficial effects on glucose homeostasis. This study assessed the insulin-secreting properties of various GPR119 agonists and the distribution of GPR119 in pancreatic islets. Endogenous ligands [oleoylethanolamide (OEA), palmitoylethanolamine (PEA)] and chemically synthetic analogues (AS-1269574, PSN-375963) were investigated in clonal BRIN-BD11 cells and mouse pancreatic islets. Secondary messenger assays such as intracellular Ca2+ and cAMP in response to agonists at normoglycaemic and hyperglycaemic conditions were assessed. Cytotoxicity was assessed by LDH release. AS-1269574 was the most potent and selective agonist tested in isolated islets, with an EC50 value of 9.7×10-7 mol/l, enhancing insulin release maximally by 63.2%. Stimulation was also observed with GPR119 ligands; OEA (3.0×10-6 mol/l; 37.5%), PSN-375963 (2.4×10-6 mol/l; 28.7%) and PEA (1.2×10-6 mol/l; 22.2%). Results were corroborated by studies using BRIN-BD11 cells, which revealed augmentation of intracellular Ca2+ and cAMP. Both OEA and AS-1269574 enhanced insulin release and improved glucose tolerance in vivo in NIH Swiss mice. These results demonstrate the cellular localisation of GPR119 on islet cells (β and pancreatic polypeptide cells), its activation of the β-cell stimulus-secretion coupling pathway and glucose lowering effects in vivo.
Published: 2013

28. Evaluation of the degradation and metabolic effects of the gut peptide xenin on insulin secretion, glycaemic control and satiety

Author: Victor A. Gault, Nigel Irwin, Peter R. Flatt, Steven Patterson, AI Taylor, and Aine McKillop
Subjects: Blood Glucose, medicine.medical_specialty, Endocrinology, Diabetes and Metabolism, medicine.medical_treatment, Enteroendocrine cell, Type 2 diabetes, Biology, Xenin, Satiety Response, Cell Line, Gastrointestinal Hormones, Eating, Mice, Endocrinology, In vivo, Internal medicine, Insulin-Secreting Cells, Insulin Secretion, medicine, Animals, Insulin, Secretion, Pancreatic hormone, Neurotensin, Protein Stability, medicine.disease, Homeostasis, Signal Transduction
Abstract: Recently, glucagon-like peptide 1 (GLP1) and glucose-dependent insulinotropic polypeptide (GIP) have received much attention regarding possible roles in aetiology and treatment of type 2 diabetes. However, peptides co-secreted from the same enteroendocrine cells are less well studied. The present investigation was designed to characterise the in vitro and in vivo effects of xenin, a peptide co-secreted with GIP from intestinal K-cells. We examined the enzymatic stability, insulin-releasing activity and associated cAMP production capability of xenin in vitro. In addition, the effects of xenin on satiety, glucose homoeostasis and insulin secretion were examined in vivo. Xenin was time dependently degraded (t1/2=162±6 min) in plasma in vitro. In clonal BRIN-BD11 cells, xenin stimulated insulin secretion at 5.6 mM (PPP2+. In normal mice, xenin exhibited a short-acting (Pin vivo. Overall, these data demonstrate that xenin may have significant metabolic effects on glucose control, which merit further study.
Published: 2010

29. Decreased dipeptidyl peptidase-IV activity and glucagon-like peptide-1(7-36)amide degradation in type 2 diabetic subjects

Author: Nicola A. Duffy, Peter R. Flatt, Patrick M. Bell, John R. Lindsay, Finbarr O'Harte, and Aine McKillop
Subjects: Blood Glucose, Male, medicine.medical_specialty, Endocrinology, Diabetes and Metabolism, Metabolite, Dipeptidyl Peptidase 4, Population, Type 2 diabetes, Dipeptidyl peptidase, Body Mass Index, chemistry.chemical_compound, Endocrinology, Glucagon-Like Peptide 1, Internal medicine, Diabetes mellitus, Diet, Diabetic, Internal Medicine, Medicine, Humans, Hypoglycemic Agents, education, Aged, Glycated Hemoglobin, education.field_of_study, biology, business.industry, General Medicine, Middle Aged, medicine.disease, Glucagon-like peptide-1, Enzyme assay, Peptide Fragments, Kinetics, chemistry, Diabetes Mellitus, Type 2, Metabolic control analysis, Creatinine, biology.protein, Female, business
Abstract: Dipeptidyl peptidase (DPP-IV) rapidly metabolizes hormones such as glucagon-like peptide-1(7-36)amide. This study evaluated circulating DPP-IV activity in type 2 diabetic patients in relation to GLP-1 degradation and metabolic control. Blood samples were collected from type 2 diabetic patients in three main categories: good glycaemic control (HbA(1c)7%, upper limit of non-diabetic range), moderate glycaemic control (HbA(1c) 7-9%) and poor glycaemic control (HbA(1c)9%). Age- and sex-matched non-diabetic subjects were used as controls. Circulating DPP-IV activity of healthy control subjects was 22.5+/-0.7 nmol/ml/min (n=70). In the combined groups of type 2 diabetic subjects, circulating DPP-IV activity was significantly decreased at 18.1+/-0.7 nmol/ml/min (p0.001, n=54). DPP-IV activity was negatively correlated with both glucose (p0.01) and HbA(1c) (p0.01) in this population. Furthermore, DPP-IV activity was reduced 1.2-fold (p0.01, n=25), 1.3-fold (p0.001, n=19) and 1.3-fold (p0.05, n=10) in good, moderate and poorly controlled diabetic groups, 18.7+/-1.0, 17.4+/-1.4 and 18.0+/-1.5 nmol/ml/min, respectively. Degradation of GLP-1 by in vitro incubation with pooled plasma samples from healthy and type 2 diabetic subjects revealed decreased degradation to the inactive metabolite, GLP-1(9-36), in the diabetic group. These data indicate decreased DPP-IV activity and GLP-1 degradation in type 2 diabetes. DPP-IV enzyme activity appears to be depressed in response to poor glycaemic control.
Published: 2007

30. Effects of antidiabetic drugs on dipeptidyl peptidase IV activity: nateglinide is an inhibitor of DPP IV and augments the antidiabetic activity of glucagon-like peptide-1

Author: Nigel Irwin, Nicola A. Duffy, Finbarr O'Harte, Peter R. Flatt, Brian D. Green, Aine McKillop, and Victor A. Gault
Subjects: Blood Glucose, endocrine system, medicine.medical_specialty, medicine.medical_treatment, Dipeptidyl Peptidase 4, Phenylalanine, Incretin, Mice, Obese, Nateglinide, Gastric Inhibitory Polypeptide, Dipeptidyl peptidase, Cell Line, Mice, Cyclohexanes, Glucagon-Like Peptide 1, Internal medicine, medicine, Diabetes Mellitus, Animals, Humans, Hypoglycemic Agents, Insulin, Pancreatic hormone, Pharmacology, Dipeptidyl-Peptidase IV Inhibitors, Chemistry, digestive, oral, and skin physiology, Glucagon-like peptide-1, Peptide Fragments, Meglitinide, Metformin, Endocrinology, hormones, hormone substitutes, and hormone antagonists, medicine.drug
Abstract: Dipeptidyl peptidase IV (DPP IV) is the primary inactivator of glucoregulatory incretin hormones. This has lead to development of DPP IV inhibitors as a new class of agents for the treatment of type 2 diabetes. Recent reports indicate that other antidiabetic drugs, such as metformin, may also have inhibitory effects on DPP IV activity. In this investigation we show that high concentrations of several antidiabetic drug classes, namely thiazolidinediones, sulphonylureas, meglitinides and morphilinoguanides can inhibit DPP IV. The strongest inhibitor nateglinide, the insulin-releasing meglitinide was effective at low therapeutically relevant concentrations as low as 25 micromol/l. Nateglinide also prevented the degradation of glucagon-like peptide-1 (GLP-1) by DPP IV in a time and concentration-dependent manner. In vitro nateglinide and GLP-1 effects on insulin release were additive. In vivo nateglinide improved the glucose-lowering and insulin-releasing activity of GLP-1 in obese-diabetic ob/ob mice. This was accompanied by significantly enhanced circulating concentrations of active GLP-1(7-36)amide and lower levels of DPP IV activity. Nateglinide similarly benefited the glucose and insulin responses to feeding in ob/ob mice and such actions were abolished by co-administration of exendin(9-39) and (Pro(3))GIP to block incretin hormone action. These data indicate that the use of nateglinide as a prandial insulin-releasing agent may partly rely on inhibition of GLP-1 degradation as well as beta-cell K(ATP) channel inhibition.
Published: 2007

31. Inhibition of dipeptidyl peptidase IV activity by oral metformin in Type 2 diabetes

Author: Peter R. Flatt, Patrick M. Bell, John R. Lindsay, Finbarr O'Harte, Nicola A. Duffy, Joy Ardill, and Aine McKillop
Subjects: Blood Glucose, Male, medicine.medical_specialty, Endocrinology, Diabetes and Metabolism, medicine.medical_treatment, Dipeptidyl Peptidase 4, Incretin, Administration, Oral, Type 2 diabetes, Gastric Inhibitory Polypeptide, Dipeptidyl peptidase, Endocrinology, Gastric inhibitory polypeptide, Glucagon-Like Peptide 1, Diabetes mellitus, Internal medicine, Internal Medicine, medicine, Humans, Hypoglycemic Agents, Protein Precursors, Cross-Over Studies, business.industry, Insulin, digestive, oral, and skin physiology, Middle Aged, medicine.disease, Glucagon, Glucagon-like peptide-1, Metformin, Peptide Fragments, Diabetes Mellitus, Type 2, Female, business, medicine.drug
Abstract: Aims Glucagon-like peptide-1 (GLP-1) and gastric inhibitory polypeptide (GIP) are important insulinotropic hormones that enhance the insulin secretory response to feeding. Their potential for treating Type 2 diabetes is limited by short biological half-life owing to degradation by dipeptidyl peptidase IV (DPP IV). We investigated the acute effects of metformin on DPP IV activity in Type 2 diabetes to elucidate inhibition of DPP IV as a possible mechanism of action. Methods Eight fasting subjects with Type 2 diabetes (5M/3F, age 53.1 +/- 4.2 years, BMI 36.8 +/- 1.8 kg/m(2), glucose 8.9 +/- 1.2 mmol/l, HbA(1c) 7.8 +/- 0.6%) received placebo or metformin 1 g orally 1 week apart in a random, crossover design. Results Following metformin, DPP IV activity was suppressed compared with placebo (AUC(0-6 h) 3230 +/- 373 vs. 5764 +/- 504 nmol ml/l, respectively, P = 0.001). Circulating glucose, insulin and total GLP-1 were unchanged. Metformin also concentration-dependently inhibited endogenous DPP IV activity in vitro in plasma from Type 2 diabetic subjects. Conclusion Oral metformin effectively inhibits DPP IV activity in Type 2 diabetic patients, suggesting that the drug may have potential for future combination therapy with incretin hormones.
Published: 2005

32. 40(th) EASD Annual Meeting of the European Association for the Study of Diabetes : Munich, Germany, 5-9 September 2004

Author: S. Artigas, A V Dreval, Mark I. McCarthy, C Watson, Peter H. Bennett, M Quint, Y Ikeda, E Alpert, F Schiele, H Sekihara, Erik Gylfe, P Lowe, J Kuhlmann, Alain Golay, V Longo, Shahidul Alam Khan Akm., L G Mantovani, M Zawodniak-Szalapska, G Winkler, T Harrity, L Virág, U Johne, Kuo S-W., Linda C Tapsell, J Rodriguez, Michel Komajda, K Kankova, Carole A. Cull, M Sporna, E Estilles, U Ribel, M C Spruce, E Buzzigoli, T Prazak, J K McLaughlin, M K Lingohr, M Lim, F Calara, A Siebenhofer, G Meregalli, Roberto Anichini, A D Baron, R Kurashvili, P C Butler, G I Fantus, T. E. De Gooyer, Park Y-M., R. Walther, S Heinrich, Agnieszka Zawiejska, S Mukherjee, Nikolaos Papanas, G Wong, Ian D. Caterson, David M. Maahs, Shuichi Kaneko, Alexandra E. Butler, Francisco Javier Ampudia-Blasco, O N Kong, Attali J-R., C A Hedman, K Oshinyemi, Nicolle Müller, I C Cranston, N Okumus, M V Vlaiculescu, Balasubramanian Ravikumar, W W Cheatham, K Mukasa, K B Biswas, Annunziata Lapolla, Phil McEwan, G Mader, Gilles Chassot, Dragi Anevski, Werner A. Scherbaum, M Donath, C Hesselmann, R A Gandhi, David E. Moller, Ezio Bonifacio, C Garcia, V Ifandi, P Hornnes, Nieuwenhoven Fav., C Puech, S Pérez-Del-Pulgar, Kim S-R., G Hines, C Rubio Terrés, Michael Gaster, N. Hosszufalusi, A Scholze, Andrew A. Young, Stavros Liatis, F Hariri, S Tan, Paul Valensi, Allan E. Karlsen, J Kim, E. Moberg, J Kaiser, L Berman, G Nelson, A Altkrüger, P Kothare, D B Cook, S Doran, G. van Dijk, Shahnaz Shahinfar, Kim C-S., P Stahl, M Manousaki, S Sigrist, S K Lim, M. P. Stern, A Guberti, C Rezzani, J McKenney, Karl Thomaseth, Sofia Carlsson, M Julia, R Brillante, I Rubesova, T Darkow, E Matsumoto, Wendy M. Macfarlane, M Di Martino, G Bardini, Rossella Menghini, D Duhot, E Farcasiu, Annalisa Natalicchio, I Lindner, J Buvat, Christian L. Brand, Harry Dorchy, Iwona Pietrzak, Z T Luo, P Home, M Ekelund, Jesper Gromada, Kristine Færch, F Piarulli, H Kim, R Mentel, Zsuzsanna K. Zsengellér, Dullaart Rpf., Anton Luger, Thomas A. Pearson, V Manicardi, P Rösen, Feng Y-M., R Morganti, Lars Hansen, Demuth H-U., Haruo Kasai, A Shostak, Rudi Steffensen, G Taylor, Markolf Hanefeld, C Santini, E Hamaguchi, Roberto Miccoli, F Storms, M Cooper, Y Lee, Allison E. Aiello, P Smith, T Suehiro, K Treece, M Waluś, Timothy A Welborn, Simone Baltrusch, E Kontela, S Chai, J Crean, H Yokoyama, Johan G. Eriksson, Rafael Hernández Hernández, J Rodríguez-Saldaña, M P Tornero, G Formoso, D. Lovell, E Bingham, A Mylonakis, M Manteghetti, D Fedele, Antonio Martín-Duce, Ralph A. DeFronzo, D Salcedo, Kurt Højlund, Antonio Petrone, Sheu Whh., C Gutierrez, Flavia Pricci, S Kurita, Z G Abbas, M M Benedetti, Philippe A. 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Trautmann, S Smirnov, J Mannion, M Eto, C Rousseau, M Conti, C S Ernest, Antonio Ceriello, D H Schweitzer, Jung E-D., Andreas Festa, Avijit Lahiri, A Shepelkevich, A Murro, A Kollmann, Jonathan R.S. Arch, R Landgraf, Son H-Y., I Engelsberger, E Agardh, S Rodríguez-Mulero, P J Kraml, K Lee, D. F. Du Toit, E Kim, G Fadini, Williams Ajk., Philip Home, M B Antcieferov, C Perlemoine, D Perrea, Song X-L., D Ruggieri, Krister Bokvist, Heidi Sørensen, Bilbao, G Yoshino, J P Taylor, Shen H-M., S M Furier, R Urquhart, J Wohlgelernter, Jianping Weng, T. Baba, Q Hong, C Silva, Castaigne J-P., M Felaco, X X Zhang, M Jaroň, Milla Rosengård-Bärlund, J G Papp, Toshio Miyata, Lervang H-H., Park M-K., I Kinalska, A Long, Oomen Phn., N Kogawa, Ippolita Patrizia Patera, S. Karadeniz, Dinesh Selvarajah, D S Chung, A Wensaas, Richard Imrich, M Recasens, J Ruxer, O Buchea, E Wilpart, S P Stepanenko, Le Ttd., H Ohgawara, Mariaconsuelo Valentini, A Mondok, M Peltonen, Marianne O. 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Parkinson, Claudia Sommer, C Park, F E Griffiths, M L Martí, R Demirtunc, S Taniguchi, J Lundkvist, T Siegmund, Juan Sztajzel, C Dienesch, F Baumgartner, L Scalone, T M Mckolanis, K Otake, Ullrik Pedersen-Bjergaard, T M Vriesendorp, Michael B. Wheeler, Henry Schmitt, Peter Hovind, S Lange, Stephane Roze, L. Van Gaal, B Klaproth, Anthony E. Civitarese, D Eckland, A Dagar, D F Hopkins, Kari Stefansson, C Gonzalez-Yanes, B Meyboom-de Jong, D. J. Betteridge, K Buhling, M Crepaldi, Ana M. Wägner, L Renna, L Volpe, R McBride, V Corbo, E O Brennesvik, R P Hayes, R Abdollahnia, G Viviani, C F Liew, Francisco Pérez-Bravo, Jeffrey Baron, Brian M. Frier, H H Samira, D Szentendrei, K. J. Schjoedt, W K Waldhäusl, D Gniuli, D Zou, G Tschank, V Urbančič, A L Nolan, Albertini J-P., J Malcomson, M Larbig, C Cheyssac, K Aurich, C M Kesson, S Heller, Maija E. Miettinen, R F Luco, Adrian J. Cameron, Luigi Mattiello, Z. Metelko, X E Zhang, M Parramón, I. G. Obrosova, J Fruchart, M Ilic, Björn Eliasson, Gilles Chatellier, M A Martín, D M Kendall, Holger Luthman, V F Varillas, D Maccubbin, Jang S-A., Amalia Gastaldelli, E Salzsieder, P. de Mol, A Yoshida, H D Lindner, D Gostiljac, M Just, Pan C-Y., J M Fujitaki, G Eiermann, K Bergenheim, A D Frick, A Agacdiken, K Varytimiadis, K Cseh, D A Jackson, S Calderari, Dena G. Hernandez, H M Liebich, K Min, F. de Zegher, Bernd Kulzer, K Han, Ulrich A. Müller, D Marrero, H Hatakeyama, René Koopman, Doo H-K., Petr Wohl, P. Sharp, P Forder, Thor Aspelund, N Meneveau, R M Schmülling, R Aubert, Thom Sam., H Youshikawa, M Ankelo, D Bowden, I Kelly, Frédéric Fumeron, M Sartini, Robert S. Sherwin, L Varadhan, A Criscimanna, John Betteridge, V Jelic, M Bartnik, N Lemke, B Ursø, A Bertoldo, A M Owona, H Okochi, L Pérez-Tamajó, S L Monfre, Daniel Brandhorst, K T Legg, Andries J. Smit, Veronica Sancho, Masashi Hirai, C Klein, Paul J. 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Jensen, A D'Avanzo, J Monaghan, K P Yeo, Guivarch P-H., B Bauduceau, D Weghuber, P Tatti, J Ybarra, S Gwozdziewiczová, E Gasparini, B Saltin, Charlotte Granhall, Howard Leventhal, R Marin, M Tumiati, Cicero Afg., L Csémy, B Berger, S Mikros, D Dall'Asta, M Shahmanesh, Y G Vasiljev, F Potthoff, H S Randeva, G De Berardis, J O Logan, K Warncke, P Uitterlinden, E Rehring, K Gilmore, K Shankhdhar, V V Bojko, M Vahatalo, E A Korolyova, D Wiemann, P G Lankisch, D Hendrie, F Galtier, M Rybarczyk, Gisela Dahlquist, N N Rudovich, G Stein, A Liebl, F Tan, A Westerlund, S Gronemann, I Franklin, Jonathan A. Prince, Peter Arner, E Skliros, T. Sparre, M Vigas, Maddalena Trombetta, L. Bjerre Knudsen, A C Sima, I Dubroca, Alastair Gray, I Weets, R Ferraresi, Schauer Ujw., E. Leinonen, S Corazza, Jonathan Levy, P K Prakash, R Guzder, S. Barnhill, John Blangero, J Herreros, G. de Vries, Cheng Ptw., A Macías-Batista, K. 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Liu, H, Jeong, I, Chae, M, Choi, M, Yoo, H, Kim, C, Yun, M, Na, M, Kang, Y, Kong, O, Son, S, Kim, I, Tanaka, N, Hosoi, M, Matsuyama, Y, Fukumoto, M, Yamakita, T, Yoshioka, K, Ishii, T, Sato, T, Fujii, S, Aoki, T, Shibata, T, Mizutani, N, Suzuki, J, Fowelin, J, Samuelsson, P, Brandrup wogsen, G, Okumura, K, Tokmakova, A, Staroverova, D, Antcieferov, M, Shutichina, I, Kuntchevich, G, Vriesendorp, T, Morélis, Q, Legemate, D, Schaper, F, Mainas, E, Gkioulmpasanis, I, Panagiotou, I, Vassilikos, G, Skorda, L, Sidira, M, Christoforidou, M, Alaveras, A, Artikis, V, Evdemon, E, Lechleitner, M, Koch, T, Ebenbichler, C, Sturm, W, Moretti, L, Moruzzo, D, Boldrini, E, Pandolfo, C, Kameyama, M, Iwasa, R, Cho, M, Nam, J, Huh, K, Kaplar, M, Paragh, G, Erdei, A, Csongradi, E, Garai, I, Varga, J, Galuska, L, Udvardy, M, Higa, M, Kaneko, Y, Hiroi, N, Koziarska, D, Nowacki, P, Majkowska, L, Luzniak, P, Wojciechowska luźniak, A, Tushuizen, M, Nieuwland, R, Snoeck, D, Sturk, A, Diamant, M, Aguiar, L, Bahia, L, Villela, N, Laflor, C, Conde, C, Bottino, D, Dorigo, D, Bouskela, E, Pu, S, Luo, Z, Lam, K, Dan, Q, Xu, A, Shen, J, Cheng, K, Xu, J, Thamer, C, Stefan, N, Haap, M, Heller, E, Tschritter, O, De Prado, A, Ortiz, A, Ybarra, J, Gich, I, Pou, J, Ehren, M, Roggenland, D, Reinsen, B, Klein, H, Rittig, K, Stock, J, Kocher, B, Balletshofer, B, Shon, H, Chung, D, Nakatani, Y, Matsuhisa, M, Kaneto, H, Hatazaki, M, Yoshiuchi, K, Katakami, N, Kawamori, D, Ohtoshi, K, Sakamoto, K, Matsuoka, T, Ozawa, K, Ogawa, S, Hori, M, Yamasaki, Y, Zitouni, K, Harry, D, Nourooz zadeh, J, Earle, K, Olesen, P, Franco, L, Corvaja, C, Semplicini, A, Ceylan işık, A, Arı, N, Rösen, P, Lee, I, Park, K, Jung, E, Shin, D, Jo, S, Obuobie, K, Prakash, P, Hanna, F, Lazarus, J, Varadhan, L, Gurushankar, J, James, D, Sheikh, S, Gaede, P, Zou, D, Vilarrasa, N, Perez maraver, M, Mena, E, Perez, D, Setti, G, Buckingham, R, Urbančič, V, Stefanovska, A, Bernjak, A, Ažman juvan, K, Kocijančič, A, Glowania, A, Filters, T, Fosmark, D, Torjesen, P, Kilhovd, B, Berg, T, Sandvik, L, Hanssen, K, Mentink, C, Donchenko, G, Stepanenko, S, Maingrette, F, Deng, H, Lindenmair, A, Freudenthaler, A, Baumgartner parzer, S, Nizheradze, K, Khoruzhenko, A, Tronko, N, Sheu, W, Ou, H, Shen, H, Lin, T, Wu, H, Yang, C, Mogylnytska, L, Schmoelzer, I, Davies, J, Band, M, Struthers, A, Prázný, M, Škrha, J, Kasalová, Z, Neelotpol, S, Jahan, P, Kauschke, S, Harrop, C, Schäfer, A, Widder, J, Eigenthaler, M, Walter, U, Uchimura, I, Ikebukuro, M, Kaibara, M, Hirata, M, Helal, R, Pervin, F, Yang, X, Jansson, P, Nagaev, I, Jack, M, Carvalho, E, Sunnerhagen, K, Cam, M, Cushman, S, Smith, U, Creely, S, Farmer, J, Gustafson, B, Kusminski, C, Krusinova, E, Wohl, P, Klementova, M, Lanska, V, Mcdougall, C, Kelly, I, Abbas, Z, Lutale, J, Archibald, L, Karunajeewa, H, Stingemore, N, Stuccio, G, Mcgechie, D, Muller, L, Hak, E, Goudzwaard, W, Montorsi, F, Homering, M, Sprenger, K, Goldstein, I, Asnaghi, V, Ferrari, G, Rastaldi, M, Gabellini, D, Dell'Antonio, G, Maestroni, A, Ruggieri, D, Luzi, L, Piemonti, L, Zerbini, G, Anafaroglu, I, Tutuncu, N, Sultana, M, Siddiqua, N, Iwasaki, T, Nakajima, A, Yoneda, M, Mukasa, K, Tanaka, S, and Sekihara, H
Subjects: 0303 health sciences, medicine.medical_specialty, business.industry, EASD, Endocrinology, Diabetes and Metabolism, Human physiology, medicine.disease, 03 medical and health sciences, 0302 clinical medicine, Diabetes mellitus, Family medicine, Internal Medicine, Medicine, business, 030217 neurology & neurosurgery, 030304 developmental biology
Published: 2004

33. Effects of nateglinide on the secretion of glycated insulin and glucose tolerance in type 2 diabetes

Author: Peter R. Flatt, Mark Mooney, Patrick M. Bell, John R. Lindsay, Finbarr O'Harte, and Aine McKillop
Subjects: Blood Glucose, Male, medicine.medical_specialty, Glycosylation, Endocrinology, Diabetes and Metabolism, medicine.medical_treatment, Phenylalanine, Nateglinide, Type 2 diabetes, Islets of Langerhans, Endocrinology, Insulin resistance, Glycation, Cyclohexanes, Internal medicine, Diabetes mellitus, Insulin Secretion, Internal Medicine, medicine, Humans, Hypoglycemic Agents, Insulin, Single-Blind Method, Pancreatic hormone, Glucose tolerance test, Cross-Over Studies, medicine.diagnostic_test, C-Peptide, business.industry, General Medicine, Glucose Tolerance Test, Middle Aged, medicine.disease, Diabetes Mellitus, Type 2, Female, business, medicine.drug
Abstract: Aims: Glycation of insulin has been demonstrated within pancreatic β-cells and the resulting impaired bioactivity may contribute to insulin resistance in diabetes. We used a novel radioimmunoassay to evaluate the effect of nateglinide on plasma concentrations of glycated insulin and glucose tolerance in type 2 diabetes. Methods: Ten patients (5 M/5 F, age 57.8±1.9 years, HbA 1c 7.6±0.5%, fasting plasma glucose 9.4±1.2 mmol/l, creatinine 81.6±4.5 μmol/l) received oral nateglinide 120 mg or placebo, 10 min prior to 75 g oral glucose in a random, single blind, crossover design, 1 week apart. Blood samples were taken for glycated insulin, glucose, insulin and C-peptide over 225 min. Results: Plasma glucose and glycated insulin responses were reduced by 9% ( P =0.005) and 38% ( P =0.047), respectively, following nateglinide compared with placebo. Corresponding AUC measures for insulin and C-peptide were enhanced by 36% ( P =0.005) and 25% ( P =0.007) by nateglinide. Conclusions: Glycated insulin in type 2 diabetes is reduced in response to the insulin secretagogue nateglinide, resulting in preferential release of native insulin. Since glycated insulin exhibits impaired biological activity, reduced glycated insulin release may contribute to the antihyperglycaemic action of nateglinide.
Published: 2003

34. Evaluation of glycated glucagon-like peptide-1(7-36)amide in intestinal tissue of normal and diabetic animal models

Author: Yasser Abdel-Wahab, Peter R. Flatt, Mark Mooney, Finbarr O'Harte, and Aine McKillop
Subjects: Blood Glucose, medicine.medical_specialty, Glycosylation, Hydrocortisone, Biophysics, Glucagon-Like Peptides, Mice, Obese, Peptide, Biochemistry, Diabetes Mellitus, Experimental, Mice, Glycation, Glucagon-Like Peptide 1, Diabetes mellitus, Internal medicine, Intestine, Small, medicine, Endocrine system, Animals, Molecular Biology, chemistry.chemical_classification, Chemistry, Body Weight, Radioimmunoassay, Organ Size, medicine.disease, Glucagon, Glucagon-like peptide-1, Small intestine, Peptide Fragments, Rats, Disease Models, Animal, medicine.anatomical_structure, Endocrinology, Hormone
Abstract: Glucagon-like peptide-1(7-36)amide (tGLP-1) is an important insulin-releasing hormone of the enteroinsular axis which is secreted by endocrine L-cells of the small intestine following nutrient ingestion. The present study has evaluated tGLP-1 in the intestines of normal and diabetic animal models and estimated the proportion present in glycated form. Total immunoreactive tGLP-1 levels in the intestines of hyperglycaemic hydrocortisone-treated rats, streptozotocin-treated mice and ob/ob mice were similar to age-matched controls. Affinity chromatographic separation of glycated and non-glycated proteins in intestinal extracts followed by radioimmunoassay using a fully crossreacting anti-serum demonstrated the presence of glycated tGLP-1 within the intestinal extracts of all control animals (approximately 19%., of total tGLP-1 content). Chemically induced and spontaneous animal models of diabetes were found to possess significantly greater levels of glycated tGLP-1 than controls, corresponding to between 24-71% of the total content. These observations suggest that glycated tGLP-1 may be of physiological significance given that such N-terminal modification confers resistance to DPP IV inactivation and degradation, extending the very short half-life (< 3 min) and bioactivity of the native peptide. (C) 2002 Elsevier Science B.V. All rights reserved.
Published: 2002

35. Degradation and glycemic effects of His(7)-glucitol glucagon-like peptide-1(7-36)amide in obese diabetic ob/ob mice

Author: Cmn Kelly, Finbarr O'Harte, Peter R. Flatt, Aine McKillop, and Mark Mooney
Subjects: Blood Glucose, medicine.medical_specialty, Spectrometry, Mass, Electrospray Ionization, Time Factors, Physiology, medicine.medical_treatment, Dipeptidyl Peptidase 4, Clinical Biochemistry, Glucagon-Like Peptides, Mice, Obese, Type 2 diabetes, Biochemistry, Dipeptidyl peptidase, Cellular and Molecular Neuroscience, Eating, Mice, Endocrinology, Glucagon-Like Peptide 1, Internal medicine, Diabetes mellitus, medicine, Animals, Humans, Hypoglycemic Agents, Insulin, Protease Inhibitors, Protein Precursors, Chromatography, High Pressure Liquid, biology, Chemistry, Biological activity, Metabolism, Exopeptidase, medicine.disease, Glucagon, Glucagon-like peptide-1, Peptide Fragments, Diabetes Mellitus, Type 2, Hyperglycemia, biology.protein, Oligopeptides
Abstract: Glucagon-like peptide-1(7-36)amide (tGLP-1) has attracted considerable potential as a possible therapeutic agent for type 2 diabetes. However, tGLP-1 is rapidly inactivated in vivo by the exopeptidase dipeptidyl peptidase IV (DPP IV), thereby terminating its insulin releasing activity. The present study has examined the ability of a novel analogue, His(7)-glucitol tGLP-1 to resist plasma degradation and enhance the insulin-releasing and antihyperglycemic activity of the peptide in 20-25-week-old obese diabetic ob/ob mice. Degradation of native tGLP-1 by incubation at 37 degrees C with obese mouse plasma was clearly evident after 3 h (35% intact). After 6 h, more than 87% of tGLP-1 was converted to GLP-1(9-36)amide and two further N-terminal fragments, GLP-1(7-28) and GLP-1(9-28). In contrast, His(7)-glucitol tGLP-1 was completely resistant to N-terminal degradation. The formation of GLP-1(9-36)amide from native tGLP-1 was almost totally abolished by addition of diprotin A, a specific inhibitor of DPP IV. Effects of tGLP-1 and His(7)-glucitol tGLP-1 were examined in overnight fasted obese mice following i.p. injection of either peptide (30 nmol/kg) together with glucose (18 mmol/kg) or in association with feeding. Plasma glucose was significantly lower and insulin response greater following administration of His(7)-glucitol tGLP-1 as compared to glucose alone. Native tGLP-1 lacked antidiabetic effects under the conditions employed, and neither peptide influenced the glucose-lowering action of exogenous insulin (50 units/kg). Twice daily s.c. injection of ob/ob mice with His(7)-glucitol tGLP-1 (10 nmol/kg) for 7 days reduced fasting hyperglycemia and greatly augmented the plasma insulin response to the peptides given in association with feeding. These data demonstrate that His(7)-glucitol tGLP-1 displays resistance to plasma DPP IV degradation and exhibits antihyperglycemic activity and substantially enhanced insulin-releasing action in a commonly used animal model of type 2 diabetes.
Published: 2000

36. Impaired ability of glycated insulin to regulate plasma glucose and stimulate glucose transport and metabolism in mouse abdominal muscle

Author: Yasser Abdel-Wahab, AC Boyd, Aine McKillop, Christopher R. Barnett, Helene McNulty, Finbarr O'Harte, and Peter R. Flatt
Subjects: Blood Glucose, Male, medicine.medical_specialty, Glycosylation, medicine.medical_treatment, Glucose uptake, Biophysics, Spectrometry, Mass, Secondary Ion, Carbohydrate metabolism, Biochemistry, chemistry.chemical_compound, Mice, Internal medicine, Diabetes mellitus, medicine, Animals, Insulin, Muscle, Skeletal, Molecular Biology, Abdominal Muscles, Glycogen, Glucose transporter, Biological Transport, Metabolism, medicine.disease, Kinetics, Endocrinology, Glucose, chemistry, Blood sugar regulation
Abstract: Previous studies have shown that glycated insulin is secreted from pancreatic beta-cells under conditions of hyperglycaemia. This study has investigated the effects of monoglycated insulin on plasma glucose homeostasis and in vitro cellular glucose transport and metabolism by isolated abdominal muscle of mice. Monoglycated insulin was prepared under hypeglycaemic reducing conditions, purified by RP-HPLC and identified by electrospray ionisation mass spectrometry (5971.1 Dal. When administered to mice at an intraperitoneal dose of 7 nmoles/kg body weight, insulin (non-glycated) decreased plasma glucose concentrations and substantially reduced the glycaemic excursion induced by conjoint intraperitoneal injection of 2 g glucose/kg body weight. In comparison, the same dose of monoglycated insulin decreased plasma glucose concentrations to a lesser extent (P < 0.05), corresponding to an approx. 20% reduction of glucose lowering potency. Using isolated abdominal muscle, insulin (10(-9)-10(-7) M) stimulated dose-dependent increases in cellular 2-deoxy-D-[1(-3)H]glucose uptake, D-[U-14C]glucose oxidation and glycogen production. Monoglycated insulin was approx. 20% less effective than native insulin in stimulating glucose uptake and both indices of metabolism, generally requiring 10-fold greater concentrations to achieve significant stimulatory effects. These data indicate that the impaired biological activity of glycated insulin may contribute to glucose intolerance of diabetes. (C) 2000 Elsevier Science B.V. All rights reserved.
Published: 2000

37. Xenin: An anorectic peptide involved in insulin secretion and glucose homeostasis

Author: AI Taylor, Aine McKillop, Peter R. Flatt, I. Irwin, and Victor A. Gault
Subjects: chemistry.chemical_classification, medicine.medical_specialty, Physiology, Chemistry, Clinical Biochemistry, Peptide, Xenin, Biochemistry, Cellular and Molecular Neuroscience, Endocrinology, Internal medicine, Anorectic, medicine, Glucose homeostasis, Insulin secretion
Published: 2010
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38. Involvement of proinsulin C-peptide in the regulation of pancreatic beta cell function and glucose homeostasis

Author: Peter R. Flatt, Aine McKillop, Yasser Abdel-Wahab, and Ming T. Ng
Subjects: medicine.medical_specialty, Physiology, Chemistry, Clinical Biochemistry, Beta-cell Function, Biochemistry, Proinsulin C-Peptide, Cellular and Molecular Neuroscience, Endocrinology, Internal medicine, medicine, Glucose homeostasis, Proinsulin
Published: 2010
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39. Metformin inhibits dipeptidyl peptidase IV activity in type 2 diabetes

Author: Joy Ardill, John R. Lindsay, Aine McKillop, Peter R. Flatt, Patrick M. Bell, Nicola A. Duffy, and Finbarr O'Harte
Subjects: medicine.medical_specialty, endocrine system diseases, business.industry, General Medicine, Type 2 diabetes, medicine.disease, Metformin, Endocrinology, Internal medicine, Metabolic effects, medicine, Dipeptidyl peptidase IV activity, business, Fasting state, medicine.drug, Hormone
Abstract: Administration of metformin has effective inhibitory action on circulating DPP IV. Although this was not associated with significant metabolic effects in the fasting state, metformin-induced inhibition of DPP IV may contribute to glycaemic control by promoting insulin-releasing activity of the enteroinsular hormones actively secreted following feeding.
Published: 2002
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40. Detection, isolation and fluctuation of glycated insulin in type 2 diabetic subjects

Author: John R. Lindsay, Peter R. Flatt, P. M. Bell, Aine McKillop, Mark Mooney, and Finbarr O'Harte
Subjects: medicine.medical_specialty, Endocrinology, Isolation (health care), business.industry, Internal medicine, medicine, General Medicine, Glycated insulin, business
Published: 2002
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