The Biology of Extracellular Molecular Chaperones (PDF)
(Sprache: Englisch)
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...
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...
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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.
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.
Autoren-Porträt
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.
Bibliographische Angaben
- 2008, 248 Seiten, Englisch
- Herausgegeben: Derek J. Chadwick, Jamie A. Goode
- Verlag: John Wiley & Sons
- ISBN-10: 0470754028
- ISBN-13: 9780470754023
- Erscheinungsdatum: 02.08.2008
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