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It was twenty ?ve years ago this year that for the ?rst time a
protein under- ing a form of human cerebral amyloidosis, the
Icelandic-type hereditary cerebral haemorrhage was identi?ed. This,
together with the recognition that an amino acid substitution can
transform the wild type cystatin C into a disease-associated
amyloid-forming protein in this condition, was only a prelude to a
series of imp- tant discoveries that followed. As a result,
pathologically altered proteins have been brought into the centre
stage of research into the pathomechanism of a n- ber of
neurodegenerative diseases, which include epidemiologically such
important conditions as Alzheimer's disease or Parkinson's disease
and, among others, also the transmissible spongiform
encephalopathies, Huntington's chorea, spinocereb- lar ataxias,
frontotemporal lobar degenerations and amyotrophic lateral
sclerosis. Despite the diversity in the amino acid sequence of the
different proteins involved in these neurological diseases, one of
the common themes underlying the patho- chanisms of all these
conditions is protein misfolding, aggregation - hence the term
protein folding disorders -, which can trigger cascades of events
ultimately resulting in synapse loss and neuron death with
devastating clinical consequences in many of the most precious
spheres of human existence including personality, cognition,
memory, skilled movements and affection. It is always a challenging
task to unite the different topics of the individual ch- ters into
a common theme in a multi-author volume, but the current book
edited by Judit Ovadi and Ferenc Orosz ?ts this task admirably.
The worldwide increasing age of populations brought the
neurodegenerative diseases into the focus of interest. A number of
the diverse human neurodegenerative diseases are now recognized as
conformational diseases frequently caused by aggregations of
unfolded or misfolded proteins. Knowledge on the intrinsically
unstructured proteins, a new family of gene products as well as on
the misfolded proteins produced by genetic mutation or
environmental effects has been extensively accumulated in the past
years. These proteins frequently cause proteolytic stress and/ or
enter into aberrant, non-physiological protein-protein interactions
leading to sequestration of protein aggregates which are assemblies
of many not-yet-identified components in addition to the deposition
of well-characterized misfolded peptides and proteins such as
b-amyloid, tau, a-synuclein and polyglutamine containing proteins.
These protein assemblies display diverse ultrastructures such
aggresomes, fibers, oligomers or amorphous structures, however, the
nature of these species concerning their cytoprotective or
cytotoxic effects has not been clarified yet. The main focus of
this volume is to review the molecular events initiated by unfolded
or misfolded proteins leading to conformational human diseases,
with special emphasis on the macromolecular homo- and
heteroassociations of the malfolded proteins into characteristic
ultrastructures found primarily in Parkinson's and Alzheimer's
diseases. This book reviews the structural knowledge accumulated
for well-studied and for newly discovered proteins involved in
paradigmatic conformational disorders with the aim to broaden our
understanding of the pathomechanisms of neurodegeneration, which is
crucial for finding effective therapeutic interventions that could
prevent or circumvent the development of neurodegenerative
disorders in humans.
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