Dr Catherine Arden
Newcastle University Research Fellow
- Email: firstname.lastname@example.org
- Telephone: +44 (0) 191 208 3868
- Address: Institute of Cellular Medicine
4th Floor William Leech Building
The Medical School
Newcastle Upon Tyne
I obtained a BSc in biomedical science from the University of Hull in 2001 and a PhD from Newcastle University in 2004. My interest in diabetes research continued during post-doc positions in the Diabetes Research Group at Newcastle University and during a travel fellowship at the University of Michigan, USA in 2007 (funded by EMBO/EFSD). In 2008 I was awarded the RD Lawrence Fellowship from Diabetes UK followed by the Newcastle University Research Fellowship in 2014.
PhD - Newcastle University, UK
BSc(hons) - Hull University, UK
2014-Present: Newcastle University Research Fellow
2008-2013: RD Lawrence Research Fellow, University of Newcastle
2007: EMBO/EFSD Travel Fellow, University of Michigan, USA
2004-2007: Research Associate, University of Newcastle
European Association for the Study of Diabetes
Google Scholar: Click here.
My overarching research aim is to understand the mechanisms underlying the impairment in function and survival of pancreatic beta-cells in type 2 diabetes, cells with a critical role in regulating blood glucose homeostasis. I am particularly interested in how glucose sensing impacts on both beta-cell function and survival. My research falls into two main research areas: i) delineating the pathways mediating cell survival. vs death in type 2 diabetes, with a particular focus on autophagy; ii) identifying mechanisms for preserving the metabolic function of beta-cells. These areas are particularly relevant given the loss of beta-cell function and increased cell death evident in type 2 diabetes.
i) Role for autophagy in regulating beta-cell survival – aim is to delineate the complex interplay between apoptosis and autophagy in regulating beta-cell death and to understand how a current therapeutic target for type 2 diabetes (GLP-1) alters this crosstalk.
ii) Impact of glucose sensing on beta-cell autophagy - aim is to determine how glucose sensing impacts on autophagy in the pancreatic beta-cell under conditions mimicking type 2 diabetes.
iii) Understanding the role of cell connectivity in preserving the pancreatic beta-cell phenotype - aim is to identify the role of cell connectivity in preserving appropriate glucose-sensing by the pancreatic beta-cells.
I currently supervise 3 PhD students and 1 MRes student.
- Newcastle University Research Fellowship
- Diabetes UK RD Lawrence Fellowship
- EFSD Albert Renold Travel Fellowship
- EMBO Short-Term Travel Fellowship
- Innovators in Diabetes (iDia) programme recipient
- Diabetes UK
- Diabetes Research and Wellness Foundation
- North East Diabetes Trust
- Royal Society
- MRC/Faculty of Medical Sciences PhD studentship
- Wellcome Trust ISSF grant
Supervision of final year undergraduate student laboratory projects.
Supervision of MRes and MSc student laboratory projects
Lecturer/Assessor on MMB8008 Cell Signalling in Health and Disease
Lecturer/Assessor on MMB8035 Diabetes
Internal PhD examiner
- Arden C. A role for Glucagon-Like Peptide-1 in the regulation of β-cell autophagy. Peptides 2018, 100, 85-93.
- Zummo FP, Cullen KS, Honkanen-Scott M, Shaw JAM, Lovat PE, Arden C. Glucagon-like peptide-1 protects pancreatic beta-cells from death by increasing autophagic flux and restoring lysosomal function. Diabetes 2017, 66(5), 1272-1285.
- Al-Oanzi ZH, Fountana S, Moonira T, Tudhope SJ, Petrie JL, Alshawi A, Patman G, Arden C, Reeves HL, Agius L. Opposite effects of a glucokinase activator and metformin on glucose-regulated gene expression in hepatocytes. Diabetes, Obesity and Metabolism 2017, 19(8), 1078-1087.
- Cullen KS, Al-Oanzi ZH, O'Harte FPM, Agius L, Arden C. Glucagon induces translocation of glucokinase from the cytoplasm to the nucleus of hepatocytes by transfer between 6-phosphofructo 2-kinase/fructose 2,6-bisphosphatase-2 and the glucokinase regulatory protein. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 2014, 1843(6), 1123-1134.
- Petrie JL, Al-Oanzi ZH, Arden C, Tudhope SJ, Mann J, Kieswich J, Yaqoob MM, Towle HC, Agius L. Glucose induces protein targeting to glycogen in hepatocytes by fructose 2,6-bisphosphate-mediated recruitment of MondoA to the promoter. Molecular and Cellular Biology 2013, 33(4), 725-738.
- Tudhope SJ, Wang CC, Petrie JL, Potts L, Malcomson F, Kieswich J, Yaqoob MM, Arden C, Hampson LJ, Agius L. A Novel Mechanism for Regulating Hepatic Glycogen Synthesis Involving Serotonin and Cyclin-Dependent Kinase-5. Diabetes 2012, 61(1), 49-60.
- Arden C, Tudhope SJ, Petrie JL, Al-Oanzi ZH, Cullen KS, Lange AJ, Towle HC, Agius L. Fructose 2,6-bisphosphate is essential for glucose-regulated genetranscription of glucose-6-phosphatase and other ChREBP target genes inhepatocytes. Biochemical Journal 2012, 443(1), 111-123.
- Arden C, Petrie JL, Tudhope SJ, Al-Oanzi Z, Claydon AJ, Beynon RJ, Towle HC, Agius L. Elevated glucose represses liver glucokinase and induces its regulatory protein to safeguard hepatic phosphate homeostasis. Diabetes 2011, 60(12), 3110-3120.
- Cullen KS, Matschinsky FM, Agius L, Arden C. Susceptibility of Glucokinase-MODY Mutants to Inactivation by Oxidative Stress in Pancreatic β-Cells. Diabetes 2011, 60(12), 3175-3185.
- Persaud S, Arden C, Bergsten P, Bone A, Brown J, Dunmore S, Harrison M, Hauge-Evans A, Kelly C, King A, Maffucci T, Marriott C, McClenaghan N, Morgan N, Reers C, Russell M, Turner M, Willoughby E, Younis M, Zhi Z, Jones P. Pseudoislets as primary islet replacements for research: Report on a symposium at King's College London, London UK. Islets 2010, 2(4), 236-239.
- Arden C, Hampson L, Huang G, Shaw J, Aldibbiat A, Holliman G, Manas D, Khan S, Lange A, Agius L. A role for PFK-2/FBPase-2, as distinct from fructose 2,6-bisphosphate, in regulation of insulin secretion in pancreatic β-cells. Biochemical Journal 2008, 411(1), 41-51.
- Mukhtar MH, Payne VA, Arden C, Harbottle A, Khan S, Lange AJ, Agius L. Inhibition of glucokinase translocation by AMP-activated protein kinase is associated with phosphorylation of both GKRP and 6-phosphofructo-2-kinase/ fructose-2,6-bisphosphatase. American Journal of Physiology: Regulatory, Integrative and Comparative Physiology 2008, 294(3), R766-R774.
- Arden C, Trainer A, De La Iglesia N, Scougall KT, Gloyn AL, Lange AJ, Shaw J, Matschinsky FM, Agius L. Cell biology assessment of glucokinase mutations V62M and G72R in pancreatic β-cells: Evidence for cellular instability of catalytic activity. Diabetes 2007, 56(7), 1773-1782.
- Payne VA, Arden C, Lange AJ, Agius L. Contributions of glucokinase and phosphofructokinase-2/fructose bisphosphatase-2 to the elevated glycolysis in hepatocytes from Zucker fa/fa rats. American Journal of Physiology - Regulatory Integrative and Comparative Physiology 2007, 293(2), R618-R625.
- Hampson LJ, Arden C, Agius L, Ganotidis M, Kosmopoulou MN, Tiraidis C, Elemes Y, Sakarellos C, Leonidas DD, Oikonomakos NG. Bioactivity of glycogen phosphorylase inhibitors that bind to the purine nucleoside site. Bioorganic and Medicinal Chemistry 2006, 14(23), 7835-7845.
- Arden C, Baltrusch S, Agius L. Glucokinase regulatory protein is associated with mitochondria in hepatocytes. FEBS Letters 2006, 580(8), 2065-2070.
- Arden C, Green AR, Hampson LJ, Aiston S, Harndahl L, Greenberg CC, Brady MJ, Freeman S, Poucher SM, Agius L. Increased sensitivity of glycogen synthesis to phosphorylase-a and impaired expression of the glycogen-targeting protein R6 in hepatocytes from insulin-resistant Zucker fa/fa rats. FEBS Journal 2006, 273(9), 1989-1999.
- Aiston S, Hampson LJ, Arden C, Iynedjian PB, Agius L. The role of protein kinase B/Akt in insulin-induced inactivation of phosphorylase in rat hepatocytes. Diabetologia 2006, 49(1), 174-182.
- Payne VA, Arden C, Wu C, Lange AJ, Agius L. Dual role of phosphofructokinase-2/fructose bisphosphatase-2 in regulating the compartmentation and expression of glucokinase in hepatocytes. Diabetes 2005, 54(7), 1949-1957.
- Arden C, Harboottle A, Baltrusch S, Tiedge M, Agius L. Glucokinase is an integral component of the insulin granules in glucose-responsive insulin secretory cells and does not translocate during glucose stimulation. Diabetes 2004, 53(9), 2346-2352.