Heat Shock Proteins and Modulation of Cellular Function

Roben's suite, Guy's Tower, Guy's Hospital Campus, London, UK

16 April 2004

Biochemical Society Focused Meeting

Heat shock proteins (HSPs) play essential roles in protein folding and membrane translocation. In the last few years it has become clear that in addition to the well-characterised chaperone activity, HSPs are potent stimulators of adaptive immune responses. HSPs can efficiently introduce antigen into both MHC class I and MHC class II processing pathways following receptor-mediated uptake of HSP-antigen complexes. Moreover HSPs also stimulate maturation of dendritic cells and production of chemokines and cytokines. They therefore form a link between innate and adaptive immunity. These novel properties of HSPs are being exploited in the development of new approaches to vaccination and cancer therapy.

Significant developments have come from determination of the 3-D structures of a number of HSPs, and the determination of the basis of interaction with substrate and definition of cellular receptors that mediate endocytosis and chemokine or cytokine production. This one day meeting is therefore timely and will bring together leading workers in these areas.


Proceedings will be published in Biochemical Society Transactions

Note: Early Registration Deadline 16 March 2004
Register early to avoid disappointment.


Poster Abstracts will be available to view on-line 2 weeks before the meeting.


Image of 'Surface representation of an unliganded section of GroEL', kindly supplied by Helen Saibil (Birkbeck College, London, UK). "Reprinted from CELL, Vol 107, 869-878, figure 3a. N.A. Ranson et al (2001) ATP-bound states of GroEL captured by cryo-electron microscopy, with permission from Elsevier."

POSTER ABSTRACTS

Abstracts first published on the Internet 30 March 2004

Poster Session

P001 Functional domain mapping of the HSP70 cochaperone HSJ1

J.P. Chapple, J. van der Spuy, S. Poopalasundaram and M.E. Cheetham

P002 The adjuvanticity of HSP70: dissection of in vivo and in vitro activity

S. Brode, B. Javid, P.A. MacAry, A. Cooke and P.J. Lehner

P003 In vitro inhibition of SIV infection following in vivo immunisation with HSP derived from human cell lines.

L.A. Bergmeier, K. Babaahamady, C.G. Kelly, T. Whittall and T. Lehner

P004 a-Crystallin protection of the enzymes against inactivation is influenced by macromolecular crowding

E. Ganea and J.J. Harding

P005 HSP70 and IEG expression following exposure of human and rat proximal tubular cell cultures to platinum analogues: correlation with toxicity

R.D. Wainford, R. Weaver, H. Merdjan and G.M. Hawksworth

P006 Vaccination with mycobacterial heat shock protein complexes induces interferon gamma and provides protection in the murine aerosol challenge model of TB

K.B. Walker, J. Keeble, C. Bailey and C. Colaco

P007 Coxsackievirus A9 utilises glucose-regulated protein (GRP)-78 and MHC class I as cell surface receptors

M. Triantafilou and K. Triantafilou

P008 The LCA associated protein AIPL1 modulates NUB1

J. van der Spuy and M.E. Cheetham

P009 Expression of Heat shock protein 70 and Heat shock protein 90 in membrane microdomains

C.L. Paul, M. Triantafilou and K. Triantafilou

P010 Stimulation of inflammatory cytokines, CC-chemokines, DC maturation and adjuvant function by the 18 kDa HSP70 peptide binding domain

Y. Wang, C.G. Kelly, T. Whittall, E. McGowan, M. Singh, L.A. Bergmeier and T. Lehner

P011 Circulating Chaperonin 60 in the plasma of British civil servants

A. Shamaei-Tousi, A. Steptoe, A. Coates and B. Henderson

P012 Curcumin induces an atypical stress response in hepatoma cells

S.J. McNally, J.A. Ross, O.J. Garden and S.J. Wigmore

P013 Differentiation and stress mediated induction of heat shock protein expression in retinal pigment epithelial cells

N. Kanuga, T.A. Bailey, P.J. Luthert and M.E. Cheetham

P014 Peptides complexed to HSP70 generate efficient human CTL responses

P.A. MacAry, B. Javid, R. Andres Floto, K.G.C. Smith, W. Oehlmann, M. Singh and P.J. Lehner

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