Taking the heat out of chaperokine function – 23 May 2012

  Taking the heat out of chaperokine function

Wednesday, 23 May 2012

The Penridge Suite, 470 Bowes Road, London N11 1NL

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 ChairDr 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       Talk to be confirmed

Dr Valerie Corrigall, Kings College London, UK

 

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

 


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This meeting was organised by Euroscicon (www.euroscicon.com), a team  of dedicated professionals working for the continuous improvement of technical knowledge transfer to all scientists. Euroscicon believe that they can make a positive difference to the quality of science by providing cutting edge information on new technological advancements to the scientific community.  This is provided via our exceptional services to individual scientists, research institutions and industry.

 

About the Chair
Lesley Bergmeier  is Senior Lecturer in Applied Mucosal Immunology in the Institute of Dentistry at Queen Mary, University of London. Her career has focused on mucosal immunity research with early work on the development of a vaccine against dental caries.  She then went on to investigate mucosal vaccine candidates for HIV/SIV and the use of heat shock proteins as adjuvants. She has contributed to studies on the immune modulation of HSPs in both Behçet’s disease and Crohn’s disease and continues to work in the Behçet’s field where her interest now focuses on the induction of the pro-inflammatory cytokine nature of this autoimmune/auto inflammatory disease.

About the Speakers
Jonathan Dean studied for his PhD at the University of Sheffield before taking up a post-doctoral fellowship at the Kennedy Institute of Rheumatology Division, Imperial College London.  In 2003 he became Lecturer in Cell Signalling at the Kennedy which recently joined the University of Oxford.  His research focuses pro-inflammatory signalling downstream of p38, including post-transcriptional regulation by the RNA-binding protein, TTP and the small heat shock protein.

 

Brian Henderson is Professor of Biochemistry at UCL’s Eastman Dental Institute and is one of the early discoverers that bacteria secrete molecular chaperones which signal to host cells.  This has led on to the thesis that bacteria use their molecular chaperones as secreted moonlighting proteins which aid in the process of bacterial virulence.

 

Paul Chapple was awarded a PhD by UCL in 1997. His PhD studied the role of molecular chaperones in environmental adaptation. The majority of my postdoctoral research was undertaken in the laboratory of Mike Cheetham at the Institute of Ophthalmology UCL, where he researched the cell biology of chaperones with links to neurodegenerative disease. He also spent a year working with Jean-Marc Gallo at the MRC Centre for Neurodegeneration Research KCL. He moved to Barts and the London Medical School QMUL as a lecturer in 2005 and was promoted to reader in 2010. His current research investigates specialized chaperone systems..

Keywords:  HSP, imunnemodulation, adjuvant, regulatory, signalling,hspB1, hsp27, inflammation, inflammatory gene expression, HSP70, Calreticulin, dendritic cells, regulatory T cell, Bacterial diseases, protein moonlighting, virulence factors, molecular chaperones, Hsc70, J protein, neurodegeneration, sacsin, trafficking

 

Registration Web Site: www.regonline.co.uk/chap2012

 

 

Post expires at 9:44am on Thursday May 24th, 2012


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