同: PrP

WordNet

have or establish a relationship to; "She relates well to her peers"
be in a relationship with; "How are these two observations related?" (同)interrelate
give an account of; "The witness related the events"
connected by kinship, common origin, or marriage
being connected either logically or causally or by shared characteristics ; "painting and the related arts"; "school-related activities"; "related to micelle formation is the...ability of detergent actives to congregate at oil-water interfaces" (同)related to
any of a large group of nitrogenous organic compounds that are essential constituents of living cells; consist of polymers of amino acids; essential in the diet of animals for growth and for repair of tissues; can be obtained from meat and eggs and milk and legumes; "a diet high in protein"
(microbiology) an infectious protein particle similar to a virus but lacking nucleic acid; thought to be the agent responsible for scrapie and other degenerative diseases of the nervous system

PrepTutorEJDIC

(…に)〈事件・事情など〉‘を'『物語る』《+『名』+『to』+『名』》 / (…と)…‘を'『関係させる』,結びつける《+『名』+『to(with)』+『名』》 / 〈物・事が〉(…に)関係がある,かかわる《+『to(with)』+『名(wh・節・句)』》 / (…に)〈人が〉なじむ,順応する《+『to』+『名』》
関係のある
蛋白(たんばく)質

UpToDate Contents

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1. プリオンの生物学および遺伝学 biology and genetics of prions
2. クロイツフェルト・ヤコブ病 creutzfeldt jakob disease
3. 変異型クロイツフェルト・ヤコブ病 variant creutzfeldt jakob disease
4. アミロイド疾患の遺伝的要因 genetic factors in the amyloid diseases
5. プリオンによる中枢神経系疾患 diseases of the central nervous system caused by prions

English Journal

Classifying prion and prion-like phenomena.

Harbi D, Harrison PM.Author information Department of Biology; McGill University; Montreal, QC Canada.AbstractThe universe of prion and prion-like phenomena has expanded significantly in the past several years. Here, we overview the challenges in classifying this data informatically, given that terms such as "prion-like", "prion-related" or "prion-forming" do not have a stable meaning in the scientific literature. We examine the spectrum of proteins that have been described in the literature as forming prions, and discuss how 'prion' can have a range of meaning, with a strict definition being for demonstration of infection with in vitro -derived recombinant prions. We suggest that although prion/prion-like phenomena can largely be apportioned into a small number of broad groups dependent on the type of transmissibility evidence for them, as new phenomena are discovered in the coming years, a detailed ontological approach might be necessary that allows for subtle definition of different "flavors" of prion / prion-like phenomena.
Prion.Prion.2014 Feb 18;8(2). [Epub ahead of print]
The universe of prion and prion-like phenomena has expanded significantly in the past several years. Here, we overview the challenges in classifying this data informatically, given that terms such as "prion-like", "prion-related" or "prion-forming" do not have a stable meaning in the scientific lite
PMID 24549098

Pan-amyloid oligomer specific scFv antibody attenuates memory deficits and brain amyloid burden in mice with Alzheimer's disease.

Zhao M, Wang SW, Wang YJ, Zhang R, Li YN, Su YJ, Zhou WW, Yu XL, Liu RT1.Author information 1National Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, Beijing 100190, China. rtliu@home.ipe.ac.AbstractAmyloid oligomers have a critical function in the pathologic processes of various amyloidoses, such as Alzheimer's disease (AD), Parkinson disease (PD), Huntington's disease, prion-related diseases, type 2 diabetes, and hereditary renal amyloidosis. Our previous reports demonstrated that a conformation-dependent oligomer-specific single-chain variable fragment (scFv) antibody, W20, isolated from a naïve human scFv library, can recognize oligomers assembled from α-synuclein, amylin, insulin, Aβ40/42, prion peptide 106-126, and lysozyme, inhibit the aggregation of various amyloid, and attenuate amyloid oligomer-induced cytotoxicity In vitro. Furthermore, W20 recognized the amyloid oligomers in all types of plaques, Lewy bodies, and amylin deposits in the brain tissues of AD and PD patients and in the pancreas of type 2 diabetes patients. In the current study, we showed that W20 blocked the binding of Aβ oligomers to SH-SY5Y cells, did not bind to heat shock protein, rescued cognitive impairments in APP/PS1 transgenic mice, and interfered with Aβ levels and deposits in mouse brain. These results suggest that W20 may be a promising therapeutic for the treatment of AD.
Current Alzheimer research.Curr Alzheimer Res.2014 Jan;11(1):69-78.
Amyloid oligomers have a critical function in the pathologic processes of various amyloidoses, such as Alzheimer's disease (AD), Parkinson disease (PD), Huntington's disease, prion-related diseases, type 2 diabetes, and hereditary renal amyloidosis. Our previous reports demonstrated that a conformat
PMID 24156260

Role of proteolytic activation of protein kinase Cδ in the pathogenesis of prion disease.

Harischandra DS, Kondru N, Martin D, Kanthasamy A, Jin H, Anantharam V, Kanthasamy A.Author information Department of Biomedical Sciences; Iowa Center for Advanced Neurotoxicology; Iowa State University; Ames, IA USA.AbstractPrion diseases are infectious and inevitably fatal neurodegenerative diseases characterized by prion replication, widespread protein aggregation and spongiform degeneration of major brain regions controlling motor function. Oxidative stress has been implicated in prion-related neuronal degeneration but the molecular mechanisms underlying prion-induced oxidative damage are not well understood. In this study, we evaluated the role of oxidative stress-sensitive, pro-apoptotic protein kinase Cδ (PKCδ) in prion-induced neuronal cell death using cerebellar organotypic slice cultures (COSC) and mouse models of prion diseases. We found a significant upregulation of PKCδ in RML scrapie infected COSC as evidenced by increased levels of both PKCδ protein and its mRNA. We also found an enhanced regulatory phosphorylation of PKCδ at its two regulatory sites, Thr505 in the activation loop and Tyr311 at the caspase-3 cleavage site. The prion infection also induced proteolytic activation of PKCδ in our COSC model. Immunohistochemical analysis of scrapie-infected COSC revealed loss of PKCδ positive Purkinje cells and enhanced astrocyte proliferation. Further examination of PKCδ signaling in the RML scrapie adopted in vivo mouse model showed increased proteolytic cleavage and Tyr 311 phosphorylation of the kinase. Notably, we observed a delayed onset of scrapie-induced motor symptoms in PKCδ knockout (PKCδ-/-) mice as compared with wild type (PKCδ+/+) mice, further substantiating the role of PKCδ in prion disease. Collectively, these data suggest that PKCδ signaling likely plays a role in the neurodegenerative processes associated with prion diseases.
Prion.Prion.2014 Jan 1;8(1). [Epub ahead of print]
Prion diseases are infectious and inevitably fatal neurodegenerative diseases characterized by prion replication, widespread protein aggregation and spongiform degeneration of major brain regions controlling motor function. Oxidative stress has been implicated in prion-related neuronal degeneration
PMID 24576946

Japanese Journal

Construction and Characterization of a Peptide Library Related to the Human Prion Protein

HIRATA Akiyoshi,KAWAHIRA Noboru,SUZUKI Kanae,KAWAKAMI Hirochika,OHYAMA Takafumi,SOGON Tetsuya,NOKIHARA Kiyoshi
Peptide science : proceedings of the ... Japanese Peptide Symposium 2007, 167-170, 2008-03-01
NAID 10021906797

Stressing out the ER : a role of the unfolded protein response in prion-related disorders

HETZ C. A.
Curr Mol Med 6, 37-43, 2006
NAID 30016411057

MOLECULAR GENETICS OF TRANSMISSIBLE SPONGIFORM ENCEPHALOPATHIES : AN INTRODUCTION

Weissmann Charles
Journal of toxicological sciences 27(2), 69-77, 2002-05-17
… Prnp knockout mice disrupted PrP^C-related genes have played an essential role to elucidate the relationship between PrP^C, a normal host gene product, and PrP^<SC>, a protease-resistant, infectious PrP;Prnp knockout mice developed by Bijeler et al. … How these murine models for human prion-related disease would contribute to the presently ongoing TSE research? …
NAID 110001807070