Tuyển tập các báo cáo nghiên cứu về y học được đăng trên tạp chí y học General Psychiatry cung cấp cho các bạn kiến thức về ngành y đề tài: Decreased levels of soluble amyloid β-protein precursor and β-amyloid protein in cerebrospinal fluid of patients with systemic lupus erythematosus...
The amyloid precursor family of proteins are of considerable interest, both
because of their role in Alzheimer’s disease pathogenesis and because of
their normal physiological functions. In mammals, the amyloid precursor
protein (APP) has two homologs, amyloid precursor-like protein (APLP) 1
Tuyển tập báo cáo các nghiên cứu khoa học quốc tế ngành hóa học dành cho các bạn yêu hóa học tham khảo đề tài: Dexamethasone diminishes the pro-inflammatory and cytotoxic effects of amyloid β-protein in cerebrovascular smooth muscle cells
It is assumed that protein fibrils manifested in amyloidosis result from an
aggregation reaction involving small misfolded protein sequences being
in an ‘oligomeric’ or ‘prefibrillar’ state. This review covers recent optical
spectroscopic studies of amyloid protein misfolding, oligomerization and
amyloid fibril growth.
Amyloid protein (Ab1–40) aggregation and conformation
was examined using native and sodium dodecyl sulfate/
polyacrylamide gel electrophoresis,and the results com-pared with those obtained by atomic force microscopy,
and with Congo red binding,sedimentation and turbidity
assays. The amount of Ab aggregation measured was
different,depending upon the method used. Incubation
for 15 min at pH 5.0 or in the presence of Fe
did not alter the level of Aboligomers observed on
SDS and native gels....
Viêm đóng một vai trò quan trọng trong bệnh động mạch vành tim vì những biến đổi do viêm
phát triển trong vách động mạch. Nhận xét trên đã làm tăng sự chú ý để khám phá sự liên hệ giữa
bệnh động mạch vành tim và những dấu hiệu cuả viêm, gồm có C-Reactive protein, fibrinogen,
chất amyloid A trong huyết thanh và nhiều dấu hiệu mới.
Alzheimer’s disease (AD) is an age-related, progressive degenerative dis-order that is characterized by synapse and neuron loss in the brain and the
accumulation of protein-containing deposits (referred to as ‘senile plaques’)
and neurofibrillary tangles. Insoluble amyloid b-peptide (Ab) fibrillar
aggregates found in extracellular plaques have long been thought to cause
the neurodegenerative cascades of AD.
Proteins might aggregate into ordered or amorphous structures, utilizing
relatively short sequence stretches, usually organized in b-sheet-like assem-blies. Here, we attempt to list all available software, developed during the
last decade or so, for the prediction of such aggregation-prone stretches
from protein primary structure, without distinguishing whether these algo
The cleavage of amyloid precursor protein (APP) byb- and c-secretases
results in the production of amyloid-b(Ab) in Alzheimer’s disease. We
raised two monoclonal antibodies, 2B3 and 2B12, that recognize the
b-secretase cleavage site on APP but not Ab.
The accumulation of misfolded proteins in the cytosol and nucleus of
neuronal cells leads to neurodegenerative disorders. Polyglutamine diseases
are caused by polyglutamine-expanded proteins, whereas mutations in
superoxide dismutase 1 lead to amyotrophic lateral sclerosis.
The amyloid protein precursor (APP) was incorporated into liposomes or phospholipid monolayers. APP insertion into liposomes required neutral lipids, such as L-a-phosphatidylcholine, in the target membrane. It was prevented in vesicles containing L-a-phosphatidylserine. The insertion was enhanced in acidic solutions, suggesting that it is modulated by speciﬁc charge/charge interactions. Surfaceactive properties and behaviour of APP were characterized during insertion of the protein in monomolecular ﬁlms of L-a-phosphatidylcholine, L-a-phosphatidylethanolamine or L-a-phosphatidylserine. ...
The main component of cerebral amyloid angiopathy (CAA) in Alzheimer’s disease is the amyloid-b protein (Ab), a 4-kDa polypeptide derived from the b-amyloid protein precursor (APP). The accumulation of Ab in the basement membrane has been implicated in the degeneration of adjacent vascular smooth muscle cells (VSMC). However, the mechanism of Ab toxicity is still unclear. In this study, we examined the eﬀect of substrate-bound Ab on VSMC in culture. The use of substrate-bound proteins in cell culture mimics presentation of the proteins to cells as if bound to the basement membrane.
The molecular biology underlying protein aggregation and neuronal death
in Alzheimer’s disease is not yet completely understood, but small soluble
nonamyloid aggregates of the amyloidb-protein (Ab) have been shown to
play a fundamental neurotoxic role.
Viêm đóng một vai trò quan trọng trong bệnh động mạch vành tim vì những biến đổi do viêm phát triển trong vách động mạch. Nhận xét trên đã làm tăng sự chú ý để khám phá sự liên hệ giữa bệnh động mạch vành tim và những dấu hiệu cuả viêm, gồm có C-Reactive protein, fibrinogen, chất amyloid A trong huyết thanh và nhiều dấu hiệu mới.
The conformational conversion of prion protein (PrP) from a native con-formation to the amyloid form is a hallmark of transmissible spongiform
encephalopathies. Conversion is usually monitored by fluorescent dyes,
which bind generic amyloids and are less suited for living cell imaging.
Cleavage of the amyloid precursor protein (APP) within the amyloid-beta
(Ab) sequence by the a-secretase prevents the formation of toxic Abpep-tides. It has been shown that the disintegrin-metalloproteinases ADAM10
and TACE (ADAM17) act asa-secretases and stimulate the generation of
a soluble neuroprotective fragment of APP, APPsa.
We report the secreted expression byPichia pastorisof two human lyso-zyme variants F57I and W64R, associated with systemic amyloid disease,
and describe their characterization by biophysical methods. Both variants
have a substantially decreased thermostability compared with wild-type
human lysozyme, a finding that suggests an explanation for their increased
propensity to form fibrillar aggregates and generate disease.
The phenomenon of the transformation of proteins into amyloid-ﬁbrils is of interest, ﬁrstly, because it is closely connected to the so-called conformational diseases, many of which are hitherto incurable, and secondly, because it remains to be explained in physical terms (energetically and structurally). The process leads to ﬁbrous aggregates in the form of extracellular amyloid plaques, neuro-ﬁbrillary tangles and other intracytoplasmic or intranuclear inclusions.
Tuyển tập báo cáo các nghiên cứu khoa học quốc tế ngành hóa học dành cho các bạn yêu hóa học tham khảo đề tài: Repeated administration of the noradrenergic neurotoxin N-(2-chloroethyl)-N-ethyl-2-bromobenzylamine (DSP-4) modulates neuroinflammation and amyloid plaque load in mice bearing amyloid precursor protein and presenilin-1 mutant transgenes
Several protein misfolding diseases are associated with the conversion of
native proteins into ordered protein aggregates known as amyloid. Studies
of amyloid assemblies have indicated that non-native proteins are responsi-ble for initiating aggregationin vitro andin vivo.