Abstract:
:Prion diseases are subacute neurodegenerative diseases that affect humans and a range of domestic and free-ranging animal species. These diseases are characterized by the accumulation of PrP (Sc), an abnormally folded isoform of the cellular prion protein (PrP (C)), in affected tissues. The pathology during prion disease appears to occur almost exclusively within the central nervous system. The extensive neurodegeneration which occurs ultimately leads to the death of the host. An intriguing feature of the prion diseases, when compared with other protein-misfolding diseases, is their transmissibility. Following peripheral exposure, some prion diseases accumulate to high levels within lymphoid tissues. The replication of prions within lymphoid tissue has been shown to be important for the efficient spread of disease to the brain. This article describes recent progress in our understanding of the cellular mechanisms that influence the propagation of prions from peripheral sites of exposure (such as the lumen of the intestine) to the brain. A thorough understanding of these events will lead to the identification of important targets for therapeutic intervention, or alternatively, reveal additional processes that influence disease susceptibility to peripherally-acquired prion diseases.
journal_name
Prionjournal_title
Prionauthors
Mabbott NAdoi
10.4161/pri.20676subject
Has Abstractpub_date
2012-09-01 00:00:00pages
322-33issue
4eissn
1933-6896issn
1933-690Xpii
20676journal_volume
6pub_type
杂志文章相关文献
Prion文献大全abstract::We propose models for in vitro grown mammalian prion protein fibrils based upon left handed beta helices formed both from the N-terminal and C-terminal regions of the proteinase resistant infectious prion core. The C-terminal threading onto a beta-helical structure is almost uniquely determined by fixing the cysteine ...
journal_title:Prion
pub_type: 杂志文章
doi:10.4161/pri.2.2.7059
更新日期:2008-04-01 00:00:00
abstract::Many laboratory studies and epidemiological observations confirm that nematodes prevent some immune-mediated diseases. The development of immunologically well-defined laboratory models of intestinal nematode infection has allowed significant advances to be made in understanding the immunological basis of effector mech...
journal_title:Prion
pub_type: 杂志文章
doi:10.4161/pri.25008
更新日期:2013-07-01 00:00:00
abstract::The prion paradigm is increasingly invoked to explain the molecular pathogenesis of neurodegenerative diseases involving the misfolding and aggregation of proteins other than the prion protein (PrP). Extensive evidence from in vitro and in vivo studies indicates that misfolded and aggregated Aβ peptide, which is the p...
journal_title:Prion
pub_type: 杂志文章
doi:10.1080/19336896.2017.1334029
更新日期:2017-07-04 00:00:00
abstract::The degeneration of pre-synaptic boutons in the stratum radiatum of the dorsal hippocampus is one of earliest components of neurodegeneration in several models of murine prion disease. We recently showed that blockade of synaptic transmission by infusion of botulinum neurotoxin A (BoNT/A) into the hippocampus several ...
journal_title:Prion
pub_type: 杂志文章
doi:10.4161/pri.23327
更新日期:2013-03-01 00:00:00
abstract::Amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD) are clinically overlapping neurodegenerative disorders whose pathophysiology remains incompletely understood. ALS initiates in a discrete location, and typically progresses in a pattern consistent with spread of the degenerative process t...
journal_title:Prion
pub_type: 杂志文章,评审
doi:10.4161/pri.5.1.14265
更新日期:2011-01-01 00:00:00
abstract::Proteins with expanded polyglutamine (polyQ) regions are prone to form amyloids, which can cause diseases in humans and toxicity in yeast. Recently, we showed that in yeast non-toxic amyloids of Q-rich proteins can induce aggregation and toxicity of wild type huntingtin (Htt) with a short non-pathogenic polyglutamine ...
journal_title:Prion
pub_type: 杂志文章
doi:10.1080/19336896.2016.1176659
更新日期:2016-05-03 00:00:00
abstract::Bovine spongiform encephalopathy (BSE) created a global European crisis in the 1980s and 90s, with very serious health and economic implications. Classical BSE now appears to be under control, to a great extent as a result of a global research effort that identified the sources of prions in meat and bone meal (MBM) an...
journal_title:Prion
pub_type: 杂志文章
doi:10.1080/19336896.2016.1175801
更新日期:2016-05-03 00:00:00
abstract::Scrapie and CWD are horizontally transmissible, and the environment likely serves as a stable reservoir of infectious prions, facilitating a sustained incidence of CWD in free-ranging cervid populations and complicating efforts to eliminate disease in captive herds. Prions will enter the environment through mortalitie...
journal_title:Prion
pub_type: 杂志文章,评审
doi:10.4161/pri.2.4.7951
更新日期:2008-10-01 00:00:00
abstract::The molecular chaperone network plays a critical role in the formation and propagation of self-replicating yeast prions. Not only do individual prions differ in their requirements for certain chaperones, but structural variants of the same prion can also display distinct dependences on the chaperone machinery, specifi...
journal_title:Prion
pub_type: 杂志文章
doi:10.4161/pri.26547
更新日期:2013-09-01 00:00:00
abstract::Among different types of protein aggregation, amyloids are a biochemically well characterized state of protein aggregation that are associated with a large number of neurodegenerative diseases including Parkinson's disease, Alzheimer and Creutzfeldt-Jakob disease. Yeast, Saccharomyces cerevisiae is an insightful model...
journal_title:Prion
pub_type: 杂志文章
doi:10.1080/19336896.2016.1141858
更新日期:2016-03-03 00:00:00
abstract::Modified nucleosides in tRNA anticodon loops such as 5-methoxy-carbonyl-methyl-2-thiouridine (mcm5s2U) and pseuduridine (Ψ) are thought to be required for an efficient decoding process. In Saccharomyces cerevisiae, the simultaneous presence of mcm5s2U and Ψ38 in tRNAGlnUUG was shown to mediate efficient synthesis of t...
journal_title:Prion
pub_type: 杂志文章
doi:10.1080/19336896.2017.1284734
更新日期:2017-01-02 00:00:00
abstract::A case of L-type-like atypical bovine spongiform encephalopathy was detected in 14-year-old Japanese black beef cattle (BSE/JP24). To clarify the biological and biochemical properties of the prion in BSE/JP24, we performed a transmission study with wild-type mice and bovinized transgenic mice (TgBoPrP). The BSE/JP24 p...
journal_title:Prion
pub_type: 杂志文章
doi:10.4161/pri.2.3.7437
更新日期:2008-07-01 00:00:00
abstract::Yeast have been extensively used to model aspects of protein folding diseases, yielding novel mechanistic insights and identifying promising candidate therapeutic targets. In particular, the neurodegenerative disorder Huntington disease (HD), which is caused by the abnormal expansion of a polyglutamine tract in the hu...
journal_title:Prion
pub_type: 杂志文章,评审
doi:10.4161/pri.18005
更新日期:2011-10-01 00:00:00
abstract::The description of prions as causal agents of Transmissible Spongiform Encephalopathies (TSE), is nowadays accepted as an important breakthrough in biology as revealed the existence of a completely new group of pathogens and a new way of transmission for biological information. A common feature of many neurodegenerati...
journal_title:Prion
pub_type:
doi:10.1080/19336896.2019.1569451
更新日期:2019-01-01 00:00:00
abstract::Heat shock proteins HSP27, HSP70 and HSP90 are molecular chaperones whose expression is increased after many different types of stress. They have a protective function helping the cell to cope with lethal conditions. The cytoprotective function of HSPs is largely explained by their anti-apoptotic function. HSPs have b...
journal_title:Prion
pub_type: 杂志文章,评审
doi:10.4161/pri.1.1.4059
更新日期:2007-01-01 00:00:00
abstract::Early detection and diagnosis of neurodegenerative diseases has been hampered by the lack of sensitive testing. Real-time quaking induced conversion (RT-QuIC) has been used for the early and sensitive detection of prion-induced neurologic disease, and has more recently been adapted to detect misfolded alpha-synuclein ...
journal_title:Prion
pub_type: 杂志文章
doi:10.1080/19336896.2020.1832946
更新日期:2020-12-01 00:00:00
abstract::Prion protein, PrP(C), is a glycoprotein that is expressed on the cell surface beginning with the early stages of embryonic stem cell differentiation. Previously, we showed that ectopic expression of PrP(C) in human embryonic stem cells (hESCs) triggered differentiation toward endodermal, mesodermal, and ectodermal li...
journal_title:Prion
pub_type: 杂志文章
doi:10.4161/pri.32079
更新日期:2014-01-01 00:00:00
abstract::Here, we report a Chinese case of Creutzfeldt-Jakob disease (CJD) with a rare mutation in the prion protein gene (PRNP) leading to an exchange of amino acid from valine (Val) to isoleucine (I) at codon 203 (V203I). The 80-y-old male presented with sudden memory loss, rapid loss of vocabulary, inattention and slow resp...
journal_title:Prion
pub_type: 杂志文章
doi:10.4161/pri.24674
更新日期:2013-05-01 00:00:00
abstract::Synaptic dysfunction is a key process in the evolution of many neurodegenerative diseases, with synaptic loss preceding that of neuronal cell bodies. In Alzheimer, Huntington, and prion diseases early synaptic changes correlate with cognitive and motor decline, and altered synaptic function may also underlie deficits ...
journal_title:Prion
pub_type: 杂志文章,评审
doi:10.4161/pri.3.4.9981
更新日期:2009-10-01 00:00:00
abstract::We report here on the proceedings of the Global Alzheimer Summit that took place September 22-23, 2011 in Madrid, Spain. As Alzheimer disease (AD) is the leading cause of neurodegeneration in elderly individuals and as yet has no effective therapeutic option, it continues to stimulate global research interests. At the...
journal_title:Prion
pub_type:
doi:10.4161/pri.6.1.18854
更新日期:2012-01-01 00:00:00
abstract::Genetic prion diseases are degenerative brain disorders caused by mutations in the gene encoding the prion protein (PrP). Different PrP mutations cause different diseases, including Creutzfeldt-Jakob disease (CJD), Gerstmann-Sträussler-Scheinker (GSS) syndrome and fatal familial insomnia (FFI). The reason for this var...
journal_title:Prion
pub_type: 杂志文章
doi:10.1080/19336896.2016.1139276
更新日期:2016-03-03 00:00:00
abstract::Studies of the ovine prion-related protein (testis-specific) gene (PRNT), including studies of genetic diversity, have highlighted its potential relationship to scrapie infection and economically important ovine traits. PRNT was previously reported to be highly polymorphic in Portuguese sheep. To characterize genetic ...
journal_title:Prion
pub_type: 杂志文章
doi:10.1080/19336896.2018.1467193
更新日期:2018-01-01 00:00:00
abstract::Prion and Alzheimer diseases are fatal neurodegenerative diseases caused by misfolding and aggregation of the cellular prion protein (PrP(C)) and the β-amyloid peptide, respectively. Soluble oligomeric species rather than large aggregates are now believed to be neurotoxic. PrP(C) undergoes three proteolytic cleavages ...
journal_title:Prion
pub_type: 杂志文章,评审
doi:10.4161/pri.27438
更新日期:2014-01-01 00:00:00
abstract::The evolutionary origins of vertebrate prion genes had remained elusive until recently when multiple lines of evidence converged to the proposition that members of the prion gene family represent an ancient branch of a larger family of ZIP metal ion transporters. (1) A follow-up investigation which explored the mechan...
journal_title:Prion
pub_type: 杂志文章
doi:10.4161/pri.20196
更新日期:2012-09-01 00:00:00
abstract::It has been described that the breakdown of β-sheets in PrP (Sc) by denaturation results in loss of infectivity and PK-sensitivity, suggesting a relationship between the structure and PK-resistance. It is also known that an important fraction of total PrP (Sc) is PK-sensitive and can be isolated by the method we alr...
journal_title:Prion
pub_type: 杂志文章
doi:10.4161/pri.22309
更新日期:2012-11-01 00:00:00
abstract::Prion diseases are consistently associated with prion protein (PrP(C)) misfolding rendering a cascade of auto-catalytic self-perpetuation of misfolded PrP in an afflicted individual. The molecular process is intriguingly similar to all known amyloid diseases both local and systemic. The prion disease is also infectiou...
journal_title:Prion
pub_type: 杂志文章
doi:10.4161/pri.27601
更新日期:2014-01-01 00:00:00
abstract::Many neurodegenerative disorders share common features including the accumulation of aggregated misfolded proteins, neuroinflammation and the induction of apoptosis. While the contributions of each of these individual elements to neuronal death remain unclear, a commonly used antibiotic, minocycline, has been shown to...
journal_title:Prion
pub_type: 杂志文章,评审
doi:10.4161/pri.3.2.8820
更新日期:2009-04-01 00:00:00
abstract::Abstract Here, we reported a Chinese case of Creutzfeldt-Jakob disease (CJD) with a rare mutation in the prion protein gene (PRNP) leading to an exchange of amino acid from valine (V) to isoleucine (I) at codon 180 (V180I). The 72 year-old Chinese women started with gradual memory loss. On admission, she did not prese...
journal_title:Prion
pub_type: 杂志文章
doi:10.4161/19336896.2014.967040
更新日期:2014-01-01 00:00:00
abstract::Prions are self-propagating infectious protein aggregates of mammals and fungi. The exact mechanism of prion formation is poorly understood. In a recent study, a comparative analysis of the aggregation propensities of chimeric proteins derived from the yeast Sup35p and mouse PrP prion proteins was performed in neurobl...
journal_title:Prion
pub_type: 杂志文章
doi:10.4161/pri.2.3.7147
更新日期:2008-07-01 00:00:00
abstract::The conformational diseases, linked to protein aggregation into amyloid conformations, range from non-infectious neurodegenerative disorders, such as Alzheimer disease (AD), to highly infectious ones, such as human transmissible spongiform encephalopathies (TSEs). They are commonly known as prion diseases. However, si...
journal_title:Prion
pub_type: 杂志文章
doi:10.4161/19336896.2014.968464
更新日期:2014-01-01 00:00:00