Dr Mark Bannister

Senior Lecturer

Biomedical Sciences

m.l.bannister@swansea.ac.uk

Office CNH - 016
Ground Floor
Institute of Life Science 2
Singleton Campus

Available For Postgraduate Supervision

Research Links

https://orcid.org/0000-0002-0865-5912

About

After gaining his PhD at the University of Leeds School of Chemistry, Dr Bannister has held postdoctoral positions at Imperial College, Boston Biomedical Research Institute, and Cardiff University. He moved to Swansea in 2017 as a British Heart Foundation funded PI where he is a researcher in the Molecular Cardiology group and Radiation Protection Supervisor for the School of Medicine. His research is centred on understanding mechanisms of pharmacological regulation of the ryanodine receptor.

Areas Of Expertise

Calcium signalling
Ion channels
Model membrane systems

Publications

Research Highlights

Williams, A., Bannister, M., Thomas, N., Sikkel, M., Mukherjee, S., Maxwell, C., MacLeod, K., George, C., Bannister, M., George, C., Thomas, N., Mukherjee, S., & Williams, A. (2016). Questioning flecainide's mechanism of action in the treatment of catecholaminergic polymorphic ventricular tachycardia. The Journal of Physiology, 594(21), 6431-6432.
https://doi.org/10.1113/jp272497, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34319
http://europepmc.org/abstract/med/27800620
Aggeli, A., Bannister, M., Bell, M., Boden, N., Findlay, J., Hunter, M., Knowles, P., Yang, J., & Bannister, M. (1998). Conformation and Ion-Channeling Activity of a 27-Residue Peptide Modeled on the Single-Transmembrane Segment of the IsK (minK) Protein†,‡. Biochemistry, 37(22), 8121-8131.
https://doi.org/10.1021/bi972112h, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34333
http://europepmc.org/abstract/med/9609707
Bannister, M., Williams, A., Sitsapesan, R., Bannister, M., & Williams, A. (2004). Removal of clustered positive charge from dihydropyridine receptor II–III loop peptide augments activation of ryanodine receptors. Biochemical and Biophysical Research Communications, 314(3), 667-674.
https://doi.org/10.1016/j.bbrc.2003.12.128, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34332
http://europepmc.org/abstract/med/14741687
Bannister, M., Williams, A., Bannister, M., & Williams, A. (2004). Activation of the sheep cardiac Ca2+ release channel by simple heteroaromatics. Biochemical and Biophysical Research Communications, 317(2), 397-400.
https://doi.org/10.1016/j.bbrc.2004.03.073, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34331
http://europepmc.org/abstract/med/15063771
Kobayashi, S., Bannister, M., Gangopadhyay, J., Hamada, T., Parness, J., Ikemoto, N., & Bannister, M. (2005). Dantrolene Stabilizes Domain Interactions within the Ryanodine Receptor. Journal of Biological Chemistry, 280(8), 6580-6587.
https://doi.org/10.1074/jbc.m408375200, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34330
http://europepmc.org/abstract/med/15611117
Bannister, M., Ikemoto, N., & Bannister, M. (2006). Effects of peptide C corresponding to the Glu724–Pro760region of the II–III loop of the DHP (dihydropyridine) receptor α1 subunit on the domain- switch-mediated activation of RyR1 (ryanodine receptor 1) Ca2+channels. Biochemical Journal, 394(1), 145-152.
https://doi.org/10.1042/bj20051373, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34329
http://europepmc.org/abstract/med/16302848
Bannister, M., Hamada, T., Murayama, T., Harvey, P., Casarotto, M., Dulhunty, A., Ikemoto, N., & Bannister, M. (2007). Malignant hyperthermia mutation sites in the Leu2442–Pro2477(DP4) region of RyR1 (ryanodine receptor 1) are clustered in a structurally and functionally definable area. Biochemical Journal, 401(1), 333-339.
https://doi.org/10.1042/bj20060902, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34328
http://europepmc.org/abstract/med/16958617
Hamada, T., Bannister, M., Ikemoto, N., & Bannister, M. (2007). Peptide Probe Study of the Role of Interaction between the Cytoplasmic and Transmembrane Domains of the Ryanodine Receptor in the Channel Regulation Mechanism†. Biochemistry, 46(14), 4272-4279.
https://doi.org/10.1021/bi061557f, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34327
http://europepmc.org/abstract/med/17361990
Toth, A., Nickson, P., Mandl, A., Bannister, M., Toth, K., Erhardt, P., & Bannister, M. (2007). Endoplasmic Reticulum Stress as a Novel Therapeutic Target in Heart Diseases. Cardiovascular & Hematological Disorders-Drug Targets, 7(3), 205-218.
https://doi.org/10.2174/187152907781745260, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34326
http://europepmc.org/abstract/med/17896961
Shtifman, A., Ward, C., Laver, D., Bannister, M., Lopez, J., Kitazawa, M., LaFerla, F., Ikemoto, N., Querfurth, H., & Bannister, M. (2010). Amyloid-β protein impairs Ca2+ release and contractility in skeletal muscle. Neurobiology of Aging, 31(12), 2080-2090.
https://doi.org/10.1016/j.neurobiolaging.2008.11.003, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34325
http://europepmc.org/abstract/med/19108934
Lyon, A., Bannister, M., Collins, T., Pearce, E., Sepehripour, A., Dubb, S., Garcia, E., O'Gara, P., Liang, L., Kohlbrenner, E., Hajjar, R., Peters, N., Poole-Wilson, P., Macleod, K., Harding, S., & Bannister, M. (2011). SERCA2a Gene Transfer Decreases Sarcoplasmic Reticulum Calcium Leak and Reduces Ventricular Arrhythmias in a Model of Chronic Heart Failure. Circulation: Arrhythmia and Electrophysiology, 4(3), 362-372.
https://doi.org/10.1161/circep.110.961615, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34324
http://europepmc.org/abstract/med/21406682
Mason, S., Viero, C., Euden, J., Bannister, M., West, D., Chen, S., Williams, A., Bannister, M., & Williams, A. (2012). The contribution of hydrophobic residues in the pore-forming region of the ryanodine receptor channel to block by large tetraalkylammonium cations andShakerB inactivation peptides. The Journal of General Physiology, 140(3), 325-339.
https://doi.org/10.1085/jgp.201210851, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34323
http://europepmc.org/abstract/med/22930804
Bannister, M., Alvarez-Laviada, A., Thomas, N., Mason, S., Coleman, S., du, P., Moran, A., Neill-Hall, D., Osman, H., Bagley, M., MacLeod, K., George, C., Williams, A., Bannister, M., George, C., Thomas, N., & Williams, A. (2016). Effect of flecainide derivatives on sarcoplasmic reticulum calcium release suggests a lack of direct action on the cardiac ryanodine receptor. British Journal of Pharmacology, 173(15), 2446-2459.
https://doi.org/10.1111/bph.13521, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34321
http://europepmc.org/abstract/med/27237957
George, C., Mitchell, A., Preece, R., Bannister, M., Yousef, Z., Bannister, M., & George, C. (2016). Pleiotropic mechanisms of action of perhexiline in heart failure. Expert Opinion on Therapeutic Patents, 26(9), 1049-1059.
https://doi.org/10.1080/13543776.2016.1211111, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34320
Bannister, M., Thomas, N., Sikkel, M., Mukherjee, S., Maxwell, C., MacLeod, K., George, C., Williams, A., Bannister, M., George, C., Thomas, N., Mukherjee, S., & Williams, A. (2015). The Mechanism of Flecainide Action in CPVT Does Not Involve a Direct Effect on RyR2. Circulation Research, 116(8), 1324-1335.
https://doi.org/10.1161/CIRCRESAHA.116.305347, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34834
Seidel, M., Rabesahala de Meritens, C., Johnson, L., Parthimos, D., Bannister, M., Thomas, N., Ozekhome-Mike, E., Lai, F., & Zisimopoulos, S. (2021). Identification of an amino-terminus determinant critical for ryanodine receptor/Ca2+ release channel function. Cardiovascular Research, 117(3), 780-791.
https://doi.org/10.1093/cvr/cvaa043, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa53861
Bannister, M., MacLeod, K., & George, C. (2022). Moving in the right direction: elucidating the mechanisms of interaction between flecainide and the cardiac ryanodine receptor. British Journal of Pharmacology, 179(11), 2558-2563.
https://doi.org/10.1111/bph.15718, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa58568

All Research

Journal Articles

Bannister, M., MacLeod, K., & George, C. (2022). Moving in the right direction: elucidating the mechanisms of interaction between flecainide and the cardiac ryanodine receptor. British Journal of Pharmacology, 179(11), 2558-2563.
https://doi.org/10.1111/bph.15718, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa58568
Seidel, M., Rabesahala de Meritens, C., Johnson, L., Parthimos, D., Bannister, M., Thomas, N., Ozekhome-Mike, E., Lai, F., & Zisimopoulos, S. (2021). Identification of an amino-terminus determinant critical for ryanodine receptor/Ca2+ release channel function. Cardiovascular Research, 117(3), 780-791.
https://doi.org/10.1093/cvr/cvaa043, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa53861
Williams, A., Bannister, M., Thomas, N., Sikkel, M., Mukherjee, S., Maxwell, C., MacLeod, K., George, C., Bannister, M., George, C., Thomas, N., Mukherjee, S., & Williams, A. (2016). Questioning flecainide's mechanism of action in the treatment of catecholaminergic polymorphic ventricular tachycardia. The Journal of Physiology, 594(21), 6431-6432.
https://doi.org/10.1113/jp272497, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34319
http://europepmc.org/abstract/med/27800620
George, C., Mitchell, A., Preece, R., Bannister, M., Yousef, Z., Bannister, M., & George, C. (2016). Pleiotropic mechanisms of action of perhexiline in heart failure. Expert Opinion on Therapeutic Patents, 26(9), 1049-1059.
https://doi.org/10.1080/13543776.2016.1211111, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34320
Bannister, M., Alvarez-Laviada, A., Thomas, N., Mason, S., Coleman, S., du, P., Moran, A., Neill-Hall, D., Osman, H., Bagley, M., MacLeod, K., George, C., Williams, A., Bannister, M., George, C., Thomas, N., & Williams, A. (2016). Effect of flecainide derivatives on sarcoplasmic reticulum calcium release suggests a lack of direct action on the cardiac ryanodine receptor. British Journal of Pharmacology, 173(15), 2446-2459.
https://doi.org/10.1111/bph.13521, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34321
http://europepmc.org/abstract/med/27237957
Bannister, M., Thomas, N., Sikkel, M., Mukherjee, S., Maxwell, C., MacLeod, K., George, C., Williams, A., Bannister, M., George, C., Thomas, N., Mukherjee, S., & Williams, A. (2015). The Mechanism of Flecainide Action in CPVT Does Not Involve a Direct Effect on RyR2. Circulation Research, 116(8), 1324-1335.
https://doi.org/10.1161/CIRCRESAHA.116.305347, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34834
Mason, S., Viero, C., Euden, J., Bannister, M., West, D., Chen, S., Williams, A., Bannister, M., & Williams, A. (2012). The contribution of hydrophobic residues in the pore-forming region of the ryanodine receptor channel to block by large tetraalkylammonium cations andShakerB inactivation peptides. The Journal of General Physiology, 140(3), 325-339.
https://doi.org/10.1085/jgp.201210851, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34323
http://europepmc.org/abstract/med/22930804
Lyon, A., Bannister, M., Collins, T., Pearce, E., Sepehripour, A., Dubb, S., Garcia, E., O'Gara, P., Liang, L., Kohlbrenner, E., Hajjar, R., Peters, N., Poole-Wilson, P., Macleod, K., Harding, S., & Bannister, M. (2011). SERCA2a Gene Transfer Decreases Sarcoplasmic Reticulum Calcium Leak and Reduces Ventricular Arrhythmias in a Model of Chronic Heart Failure. Circulation: Arrhythmia and Electrophysiology, 4(3), 362-372.
https://doi.org/10.1161/circep.110.961615, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34324
http://europepmc.org/abstract/med/21406682
Shtifman, A., Ward, C., Laver, D., Bannister, M., Lopez, J., Kitazawa, M., LaFerla, F., Ikemoto, N., Querfurth, H., & Bannister, M. (2010). Amyloid-β protein impairs Ca2+ release and contractility in skeletal muscle. Neurobiology of Aging, 31(12), 2080-2090.
https://doi.org/10.1016/j.neurobiolaging.2008.11.003, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34325
http://europepmc.org/abstract/med/19108934
Toth, A., Nickson, P., Mandl, A., Bannister, M., Toth, K., Erhardt, P., & Bannister, M. (2007). Endoplasmic Reticulum Stress as a Novel Therapeutic Target in Heart Diseases. Cardiovascular & Hematological Disorders-Drug Targets, 7(3), 205-218.
https://doi.org/10.2174/187152907781745260, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34326
http://europepmc.org/abstract/med/17896961
Hamada, T., Bannister, M., Ikemoto, N., & Bannister, M. (2007). Peptide Probe Study of the Role of Interaction between the Cytoplasmic and Transmembrane Domains of the Ryanodine Receptor in the Channel Regulation Mechanism†. Biochemistry, 46(14), 4272-4279.
https://doi.org/10.1021/bi061557f, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34327
http://europepmc.org/abstract/med/17361990
Bannister, M., Hamada, T., Murayama, T., Harvey, P., Casarotto, M., Dulhunty, A., Ikemoto, N., & Bannister, M. (2007). Malignant hyperthermia mutation sites in the Leu2442–Pro2477(DP4) region of RyR1 (ryanodine receptor 1) are clustered in a structurally and functionally definable area. Biochemical Journal, 401(1), 333-339.
https://doi.org/10.1042/bj20060902, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34328
http://europepmc.org/abstract/med/16958617
Bannister, M., Ikemoto, N., & Bannister, M. (2006). Effects of peptide C corresponding to the Glu724–Pro760region of the II–III loop of the DHP (dihydropyridine) receptor α1 subunit on the domain- switch-mediated activation of RyR1 (ryanodine receptor 1) Ca2+channels. Biochemical Journal, 394(1), 145-152.
https://doi.org/10.1042/bj20051373, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34329
http://europepmc.org/abstract/med/16302848
Kobayashi, S., Bannister, M., Gangopadhyay, J., Hamada, T., Parness, J., Ikemoto, N., & Bannister, M. (2005). Dantrolene Stabilizes Domain Interactions within the Ryanodine Receptor. Journal of Biological Chemistry, 280(8), 6580-6587.
https://doi.org/10.1074/jbc.m408375200, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34330
http://europepmc.org/abstract/med/15611117
Bannister, M., Williams, A., Bannister, M., & Williams, A. (2004). Activation of the sheep cardiac Ca2+ release channel by simple heteroaromatics. Biochemical and Biophysical Research Communications, 317(2), 397-400.
https://doi.org/10.1016/j.bbrc.2004.03.073, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34331
http://europepmc.org/abstract/med/15063771
Bannister, M., Williams, A., Sitsapesan, R., Bannister, M., & Williams, A. (2004). Removal of clustered positive charge from dihydropyridine receptor II–III loop peptide augments activation of ryanodine receptors. Biochemical and Biophysical Research Communications, 314(3), 667-674.
https://doi.org/10.1016/j.bbrc.2003.12.128, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34332
http://europepmc.org/abstract/med/14741687
Aggeli, A., Bannister, M., Bell, M., Boden, N., Findlay, J., Hunter, M., Knowles, P., Yang, J., & Bannister, M. (1998). Conformation and Ion-Channeling Activity of a 27-Residue Peptide Modeled on the Single-Transmembrane Segment of the IsK (minK) Protein†,‡. Biochemistry, 37(22), 8121-8131.
https://doi.org/10.1021/bi972112h, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34333
http://europepmc.org/abstract/med/9609707

Taught Modules

PM-130 Fundamental Research Skills

This module is designed to develop the skills required for students of biochemistry and genetics degree programmes. Students meet with their tutors and will be given a series of assignments designed to develop skills in key areas such as essay writing, presentations and general numeracy.
PM-154 Human Physiology

Human physiology is the study of how our body works in an integrated way. A central principle of human physiology is homeostasis, the maintenance of a relatively stable internal environment. Failure to maintain homeostasis disrupts normal function that may lead to disease (or pathophysiology). Students will be taught the key concepts of homeostasis in the physiological systems of the body, enabling the student to understand the consequences of pathophysiology to human health. Emphasis will be given to how malfunction of key physiological systems gives rise to disease, using specific examples to enable students to appreciate the relationship between physiology/anatomy and medicine. Fundamental principles of physiology will be illustrated with appropriate clinical examples and during lectures and in practical assignments. Students will gain practical experience in assessing physiological function during four laboratory-based exercises. The impact of pathophysiology of such systems will be assessed through clinical case studies.
PM-154C Ffisioleg Ddynol

Ffisioleg Ddynol yw astudio sut mae ein cyrff yn gweithio mewn ffordd integredig. Egwyddor sydd wrth wraidd ffisioleg ddynol yw homeostasis, sef cynnal amgylchedd mewnol cymharol sefydlog. Os na chynhelir homeostasis, bydd yn amharu ar swyddogaeth arferol a allai arwain at glefyd (neu bathoffisioleg). Caiff myfyrwyr eu haddysgu am gysyniadau allweddol homeostasis yn systemau ffisiolegol y corff, gan alluogi'r myfyriwr i ddeall canlyniadau pathoffisioleg i iechyd pobl.Rhoddir pwyslais ar y ffordd y mae methiannau systemau ffisiolegol allweddol yn arwain at glefyd, gan ddefnyddio enghreifftiau penodol i alluogi myfyrwyr i werthfawrogi'r berthynas rhwng ffisioleg/anatomeg a meddygaeth.Caiff egwyddorion sylfaenol ffisioleg eu hesbonio ag enghreifftiau clinigol priodol ac yn ystod darlithoedd ac mewn aseiniadau ymarferol.Bydd myfyrwyr yn cael profiad ymarferol o asesu swyddogaeth ffisiolegol yn ystod pedwar ymarfer yn y labordy. Asesir effaith pathoffisioleg mewn systemau o'r fath drwy astudiaethau achos clinigol.
PM-266 The Cardiovascular System

Leading on from the first year Human Physiology Module (PM-154), the Cardiovascular Module will introduce and define the fundamental cellular mechanisms that regulate the physiology of healthy cardiovascular function. The Module will describe the processes that allow regular heartbeat and blood vessel function and how perturbations in the systems covered may lead to pathophysiological conditions. There will be an emphasis on experimental approaches used to study the cardiovascular mechanisms described.
PM-266C Y System Gardiofasgwlaidd

Gan adeiladu ar fodiwl Ffisioleg Ddynol y flwyddyn gyntaf (PM-154), bydd y Modiwl Cardiofasgwlaidd yn cyflwyno ac yn diffinio'r mecanweithiau cellol sylfaenol sy'n rheoleiddio ffisioleg gweithrediad cardiofasgiwlaidd iach. Bydd y modiwl yn disgrifio'r prosesau sy'n galluogi gweithrediad iach curiad y galon a'r pibellau gwaed a sut gall aflonyddiadau yn y systemau a drafodir arwain at gyflyrau pathoffisiolegol. Bydd pwyslais ar ddulliau arbrofol a ddefnyddir i astudio'r mecanweithiau cardiofasgwlaidd a ddisgrifir.
PM-340 Being a Medical Scientist

Much of a scientist¿s career is spent writing and speaking about science. The aim of this module is to give students a higher level experience of what being a lead researcher is like, away from the lab bench. Drawing on core knowledge from other modules, students will refine their oral and written communication and learn what leadership skills are needed to succeed in modern science. They will also be challenged to consider ethical aspects of research, including new technologies and the use of animal and human subjects. The module will be highly interactive, taught using informal lectures interspersed with students working in groups.
PM-344 Capstone Project

The aim of this module is to provide a capstone experience to students¿ learning, through participating in their own enquiry-based research project, with guidance from an academic supervisor. The project may be laboratory or non-laboratory based, but it will always involve a research question that is drawn from the literature, and focused on a topic relevant to the life sciences. It will ask a research question and involve the critical analysis of research findings. Students will refine their oral and written communication skills to a graduate level through an oral presentation and dissertation on their research findings and conclusions.
PMGM17 Post Graduate Taught Masters Dissertation

The module is for students to build on their previous knowledge, skills and experience by undertaking a laboratory based or suitable non-laboratory based project on a specific subject related to genomics.
PMRM04 Dissertation (Research)

This module builds on the knowledge and skills developed in teaching components in part one of their relevant programme. Students will work independently in order to critically explore and add to the evidence base for a topic of relevance to their area of study.

Dr Mark Bannister

Email address

Research Links

About

Areas Of Expertise

Publications

Research Highlights

All Research

Journal Articles

Taught Modules

PM-130 Fundamental Research Skills

PM-154 Human Physiology

PM-154C Ffisioleg Ddynol

PM-266 The Cardiovascular System

PM-266C Y System Gardiofasgwlaidd

PM-340 Being a Medical Scientist

PM-344 Capstone Project

PMGM17 Post Graduate Taught Masters Dissertation

PMRM04 Dissertation (Research)