Author: "Aine McKillop" / Search Limiters: Available in Library Collection - Searchworks@Jio Institute Digital Library Search Results

13 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. 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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7. 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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8. 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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9. 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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10. 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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11. 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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12. 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

13. 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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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

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13 results on '"Aine McKillop"'

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

2. Development and characterisation of novel, enzymatically stable oxytocin analogues with beneficial antidiabetic effects in high fat fed mice

3. Development of novel ligands for peptide GPCRs

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

5. Pharmacological potential of novel agonists for FFAR4 on islet and enteroendocrine cell function and glucose homeostasis

6. Evaluation of the insulin releasing and antihyperglycaemic activities of GPR55 lipid agonists using clonal beta-cells, isolated pancreatic islets and mice

7. Emerging Applications of Metabolomic and Genomic Profiling in Diabetic Clinical Medicine

8. Insulinotropic actions of nateglinide in type 2 diabetic patients and effects on dipeptidyl peptidase-IV activity and glucose-dependent insulinotropic polypeptide degradation

9. Demonstration of increased concentrations of circulating glycated insulin in human Type 2 diabetes using a novel and specific radioimmunoassay

10. Demonstration of Glycated Insulin in Human Diabetic Plasma and Decreased Biological Activity Assessed by Euglycemic-Hyperinsulinemic Clamp Technique in Humans

11. Production and characterization of specific antibodies for evaluation of glycated insulin in plasma and biological tissues

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

13. 40(th) EASD Annual Meeting of the European Association for the Study of Diabetes : Munich, Germany, 5-9 September 2004

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13 results on '"Aine McKillop"'

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