Taking the heat out of chaperokine function
23rd May 2012
The meeting will explore the diverse functions of heat shock proteins over and above their action as chaperones and stress indicators.
The role of HSPs in health and disease and their potential as immunemodulators will be examined and discussed.
This event has CPD accreditation and will have a discussion panel session.
On registration you will be able to submit your questions to the panel that will be asked by the chair on the day of the event
Meeting Chair: Dr Lesley Bergmeier, CBiol, MIBiol, PhD, FHEA
Institute of Dentistry, Barts and The London School of Medicine and Dentistry, UK
9:00 – 9:45 Registration
9:45 – 10:00 Introduction by the Chair: Dr Lesley Bergmeier, CBiol, MIBiol, PhD, FHEA.
Institute of Dentistry, Barts and The London School of Medicine and Dentistry, UK
10:00 – 10:30 Heat Shock Protein 70 induces cytotoxicity of T-helper cells and augmented the immunosuppressive capacity of FoxP3+ T regulatory cells
Professor Britta Eiz-Vesper, Institut für Transfusionsmedizin, Medizinische Hochschule Hannover, Germany
Heat shock proteins (HSPs) play a regulatory role for maturation of antigen-presenting cells (APCs) and gained plenty of attention because of its potent adjuvant capability to induce antigen-specific CD8+ cytotoxic T-lymphocyte and CD4+ T-helper cell responses, but the mechanism how HSP70 affects the immunosuppressive function of Tregs is still unknown. Our data pro-vide novel insights into the role of extracellular HSP70 and Calreticulin on antigen presentation, maturation of APCs as well as T-cell immune response.
10:30 – 11:00 Function of hspB1 in inflammation
Dr Jonathan Dean, University of Oxford, UK
Heat shock protein B1 (human hsp27, or the murine orthologue hsp25) has long been known to be phosphorylated in cells in response to pro-inflammatory stimuli. Purification of activities responsible for its phosphorylation led to the identification of the p38 mitogen-activated protein kinase pathway, one of the major signalling pathways in inflammation. Despite being a downstream component of the p38 pathway the role of hspB1 in inflammation has remained obscure until recently. I will outline progress in our understanding of the function of hspB1 in inflammation.
11:00 – 11:30 Speakers’ photo then mid-morning break and trade show
11:30 – 12:00 Binding immunoglobulin protein (BiP): a powerful anti-inflammatory mediator
Dr Valerie Corrigall, Kings College London, UK
Binding immunoglobulin protein (BiP) is a ubiquitously expressed protein resident of the endoplasmic reticulum. During cellular stress, particularly lack of glucose and oxygen, BiP is upregulated, secreted and, as an extracellular protein, has an immunoregulatory role outwith its vital intracellular role. BiP acts predominantly through a monocyte expressed receptor, as yet unknown, initiating alternative activation of these cells. Although profuse IL-10 production is characteristic of BiP activated monocytes the downstream effects differ from those attributable solely to IL-10. Downregulation of costimulatory molecules, HLA-DR and inhibition of TNFα production are among the most consistent biomarkers of BiP activation. Additionally, monocyte differentiation into either dendritic cells or osteoclasts is inhibited by the presence of BiP. Cell–to-cell contact between BiP-treated dendritic cells and T cells, in the absence of BiP, leads to increased CD152 +regulatory T cell function. In vitro development of human BiP specific T cell clones show a predominantly CD8+ phenotype and a clear TH2 bias. This skewed TH2 response is consistent with the T cell recall antigen responses seen in the murine collagen induced arthritis model where BiP has been successfully used both prophylactically and therapeutically. The overall impression from these studies is that BiP acts to switch the immune response from a pro-inflammatory to an anti-inflammatory profile and therefore aid resolution of inflammation.
12:00 – 12:30 Talk to be confirmed
Professor Graham Pockley, University of Sheffield, UK
12:30 – 13:30 Lunch and trade show
13:30 – 14:30 Question and Answer Session
Delegates will be asked to submit questions to a panel of experts. Questions can be submitted before the event or on the day
14:30– 15:00 Afternoon Tea/Coffee and trade show
15:00 – 15:30 Specialised functions of the Hsc70 chaperone system
Dr Paul Chapple, William Harvey Research Institute, London, UK
In humans there are 13 different Hsp70 proteins and approximately 50 J proteins. This diversity of cochaperone J proteins allows the recruitment of Hsp70 family members to multiple cellular locales and clients, mediating functions beyond de novo protein folding and quality control. Specialized function of the Hsc70 chaperone system will be illustrated using examples from our recent work that link to human disease. This will include evidence for Hsc70 functioning to promote traffic to the cell surface of melanocortin-4 receptor. Data linking Hsc70 to the regulation of mitochondrial dynamics through the J protein sacsin will also be outlined.
15:30 – 16:00 Bacterial molecular chaperones: moonlighting proteins involved in bacterial virulence
Professor Brian Henderson, Eastman Dental Institute, London, UK
Protein moonlighting describes the phenomenon of proteins having more than one unique biological function. It turns out that a number of bacterial pathogens use well known proteins in their virulence behaviour. A major group of such proteins are the molecular chaperones with major pathogens such as Mycobacterium tuberculosis, Helicobacter pylori and Chlamydia pneumoniae using such proteins to aid in the infectious process. A detailed description of the use of molecular chaperones in bacterial virulence will be provided.
16:00 Chairman’s summing up
Expected Number of Attendees
MA
View Conference Website: Taking the heat out of chaperokine function
Contact
Name: Astrid Englezou
Email: astrid.englezou@euroscicon.com
URL: Website
Price of Attendance
N/A
Brochure
Location
The Penridge Suite
470 Bowes Road
London
United Kingdom
N11 1NL
