The heat shock, or cell stress, response was first identified in
the polytene chromosomes of Drosophila. This was later
related to the appearance of novel proteins within stressed cells,
and the key signal stimulating this appearance was identified as
the presence of unfolded proteins within the cell. It is now known
that this is a key mechanism enabling cells to survive a multitude
of physical, chemical and biological stresses.
Since the promulgation of the ‘molecular chaperone’
concept as a general cellular function to control the process of
correct protein folding, a large number of molecular chaperones and
protein folding catalysts have been identified, and it has been
recognized that not all molecular chaperones are stress proteins
and vice versa. The discovery of molecular chaperones as folding
proteins went hand-in-hand with their recognition as potent
immunogens in microbial infection. It was subsequently shown that
administration of molecular chaperones such as Hsp60, Hsp70 or
Hsp90 could inhibit experimental autoimmune diseases and
cancer.
More recently evidence has accumulated to show that certain
molecular chaperones are also present on the surface of cells or in
extracellular fluids. A new paradigm is emerging: at least some
molecular chaperones are secreted proteins with pro- or
anti-inflammatory actions, regulating the immune response in human
diseases such as coronary heart disease, diabetes and rheumatoid
arthritis. In addition to having direct effects on cells, molecular
chaperones can bind peptides and present them to T cells to
modulate immune responses. This may be significant in the treatment
of cancer.
This is the first book bringing leading researchers in this
field together to review and discuss:
* our current knowledge of cell stress response and molecular
chaperones
* the changing paradigms of protein trafficking and function
* cell stress proteins as immunomodulators and pro- and
anti-inflammatory signalling molecules
* the role of these proteins in various chronic diseases and
their potential as preventative or therapeutic agents.
The Biology of Extracellular Molecular Chaperones is of
particular interest to immunologists, cell and molecular
biologists, microbiologists and virologists, as well as clinical
researchers working in cardiology, diabetes, rheumatoid arthritis
and other inflammatory diseases.
Содержание
Symposium on The biology of extracellular molecular chaperones,
held at the Novartis Foundation, London, 5-7 June 2007.
Editors: Derek J. Chadwick (Organizer) and Jamie
Goode.
This symposium is based on a proposal made by Brian
Henderson, R. John Ellis and A. Graham Pockley
Péter Csermely Chair’s introduction.
Jodie Haak and Kevin C. Kregel 1962-2007: a
cell stress odyssey.
Discussion.
Peter A. Lund and R. John Ellis The chaperone
function: meanings and myths.
Discussion.
Péter Csermely, Tamás Korcsmáros, István
A. Kovács, Máté S. Szalay and Csaba Soti
Systems biology of molecular chaperone networks.
Discussion.
Radhey S. Gupta , Nallur B. Ramachandra, Timothy Bowes
and Bhag Singh Unusual cellular disposition of the
mitochondrial molecular chaperones Hsp60, Hsp70 and Hsp10.
Discussion.
Martha Triantafilou, Daniel Sawyer, Abdiaziz Nor,
Emmanouil Vakakis and Kathy Triantafilou Cell surface
molecular chaperones as endogenous modulators of the innate immune
response.
Discussion.
A. Graham Pockley and Gabriele Multhoff Cell
stress proteins in extracellular fluids: friend or foe?
Discussion.
Francisco J. Quintana and Irun R. Cohen HSP60
speaks to the immune system in many voices.
Discussion.
Stuart K. Calderwood, Jianlin Gong, Jimmy R. Theriault,
Salamatu S. Mambula and Philip J. Gray Jnr Cell
stress proteins: novel immunotherapeutics.
Discussion.
General discussion.
Brian Henderson Cell stress proteins as modulators of
bacteria-host interactions.
Discussion.
Anthony R. M. Coates, Ana Cehovin and Yanmin Hu
Chaperonin 60 and macrophage activation.
Discussion.
Alexzander Asea Hsp70: a chaperokine.
Discussion.
Hajime Nakamura Extracellular functions of
thioredoxin.
Discussion.
Carol L. Miller-Graziano, Asit De, Krzysztof Laudanski,
Tara Herrmann and Sanjukta Bandyopadhyay HSP27: an
anti-inflammatory and immunomodulatory stress protein acting to
dampen immune function.
Discussion.
Gabriel S. Panayi and Valerie M. Corrigall Bi P, an
anti-inflammatory ER protein, is a potential new therapy for the
treatment of rheumatoid arthritis.
Discussion.
Final discussion.
Index of contributors.
Subject index.
Об авторе
The Novartis Foundation is an international scientific and educational charity which promotes the study and general knowledge of science and in particular encourages international co-operation in scientific research.
Chair: Péter Csermely.
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