TY - CHAP
T1 - Advances in Heat Shock Proteomics: Towards a Better Understanding of the Physiology and Pathophysiology of Molecular Chaperones.
AU - Scatena, Roberto
AU - Bottoni, Patrizia
AU - Giardina, Bruno
AU - FACOLTA', DI MEDICINA E CHIRURGIA "A.GEMELLI"
AU - FACOLTA', DI MEDICINA E CHIRURGIA "A.GEMELLI"
AU - FACOLTA', DI MEDICINA E CHIRURGIA "A.GEMELLI"
AU - FACOLTA', DI MEDICINA E CHIRURGIA "A.GEMELLI"
PY - 2009
Y1 - 2009
N2 - Chaperones are a large group of unrelated protein families that stabilize unfolded
proteins, unfold them for translocation across membranes or degradation, and assist in
their correct folding and assembly. They represent one of the most ancient and
evolutionarily conserved protective protein families found in nature. A fundamental
group of molecular chaperones is the so-called heat shock proteins (HSPs), also known
as stress proteins. Originally discovered as inducible molecules capable of maintaining
cellular homeostasis against abrupt temperature changes, HSPs were later considered an
adaptive physiological response that protects against a variety of different cellular
proteotoxic stresses. Early in the study of these proteins, it was evident that these
molecules also have physiological roles that facilitate the synthesis, folding, assembly,
trafficking, and secretion of specific proteins in various cellular compartments in the
absence of significant pathological processes. In summary, these proteins guard the
cellular proteome against misfolding and inappropriate aggregation.
From a clinical point of view, modification of the chaperone proteome, mainly the
induction of HSPs, has been observed in a wide spectrum of inflammatory and
degenerative diseases, including cancer, infectious disease, autoimmune processes,
neurodegenerative conditions, and prion disease. The involvement of HSPs in these diverse diseases highlights the importance of the chaperone machinery not only in cell
biology, but also in pathophysiology. At the same time, the induction of HSPs in diseases
suggests potential clinical applications for molecular chaperones, particularly HSPS, in
the diagnosis, prognosis and, above all, therapy of different degenerative and
inflammatory human diseases. On this basis, proteomic approaches represent a valuable
method to study the roles, structural interrelationships, and intimate molecular
mechanisms of the major chaperone families that have been insufficiently characterized,
limiting their diagnostic and therapeutic potential.
AB - Chaperones are a large group of unrelated protein families that stabilize unfolded
proteins, unfold them for translocation across membranes or degradation, and assist in
their correct folding and assembly. They represent one of the most ancient and
evolutionarily conserved protective protein families found in nature. A fundamental
group of molecular chaperones is the so-called heat shock proteins (HSPs), also known
as stress proteins. Originally discovered as inducible molecules capable of maintaining
cellular homeostasis against abrupt temperature changes, HSPs were later considered an
adaptive physiological response that protects against a variety of different cellular
proteotoxic stresses. Early in the study of these proteins, it was evident that these
molecules also have physiological roles that facilitate the synthesis, folding, assembly,
trafficking, and secretion of specific proteins in various cellular compartments in the
absence of significant pathological processes. In summary, these proteins guard the
cellular proteome against misfolding and inappropriate aggregation.
From a clinical point of view, modification of the chaperone proteome, mainly the
induction of HSPs, has been observed in a wide spectrum of inflammatory and
degenerative diseases, including cancer, infectious disease, autoimmune processes,
neurodegenerative conditions, and prion disease. The involvement of HSPs in these diverse diseases highlights the importance of the chaperone machinery not only in cell
biology, but also in pathophysiology. At the same time, the induction of HSPs in diseases
suggests potential clinical applications for molecular chaperones, particularly HSPS, in
the diagnosis, prognosis and, above all, therapy of different degenerative and
inflammatory human diseases. On this basis, proteomic approaches represent a valuable
method to study the roles, structural interrelationships, and intimate molecular
mechanisms of the major chaperone families that have been insufficiently characterized,
limiting their diagnostic and therapeutic potential.
KW - heat shock proteins
KW - heat shock proteins
UR - http://hdl.handle.net/10807/9404
M3 - Chapter
SN - 978-1608763665
SP - 149
EP - 178
BT - Handbook of Molecular Chaperones: Roles, Structures and Mechanisms
ER -