Papers - ATARASHI Ryuichiro
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Pentosan polysulfate induces low-level persistent prion infection keeping measurable seeding activity without PrP-res detection in Fukuoka-1 infected cell cultures. Reviewed
Takatsuki H, Imamura M, Mori T, Atarashi R
Sci Rep 12 ( 1 ) 7923 2022.5
Authorship：Last author, Corresponding author Language：English Publishing type：Research paper (scientific journal)
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Spontaneous generation of distinct prion variants with recombinant prion protein from a baculovirus-insect cell expression system. Reviewed
Imamura M, Tabeta N, Iwamaru Y, Takatsuki H, Mori T, Atarashi R*
Biochem Biophys Res Commun 613 67 - 72 2022.5
Authorship：Last author, Corresponding author Language：English Publishing type：Research paper (scientific journal)
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Discrimination between L-type and C-type bovine spongiform encephalopathy by the strain-specific reactions of real-time quaking-induced conversion. Reviewed
Ubagai K, Fukuda S, Mori T, Takatsuki H, Taguchi Y, Kageyama S, Nishida N, Atarashi R
Biochem Biophys Res Commun 526 ( 4 ) 1049 - 1053 2020.6
Authorship：Last author, Corresponding author Language：English Publishing type：Research paper (scientific journal)
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Identification of alprenolol hydrochloride as an anti-prion compound using surface plasmon resonance imaging. Reviewed
Miyazaki Y, Ishikawa T, Kamatari YO, Nakagaki T, Takatsuki H, Ishibashi D, Kuwata K, Nishida N, Atarashi R
Mol Neurobiol 56 ( 1 ) 367 - 377 2019.1
Authorship：Last author, Corresponding author Language：English Publishing type：Research paper (scientific journal)
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Cerebrospinal fluid real-time quaking-induced conversion is a robust and reliable test for sporadic CJD: An international study. Reviewed International coauthorship
McGuire, L.I., Poleggi, A., Poggiolini, I., Suardi, S., Grznarova, K., Shi, S., de Vil, B., Sarros, S., Satoh, K., Cheng, K., Cramm, M., Fairfou,l G., Schmitz, M., Zerr, I., Cras, P., Equestre, M., Tagliavini, F., Atarashi, R., Knox, D., Collins, S., Haïk, S., Parchi, P., Pocchiari, M., Green, A.
Annals of neurology 80 ( 1 ) 160 - 165 2016.4
Language：English Publishing type：Research paper (scientific journal)
DOI： 10.1002/ana.24679.
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Conformational properties of prion strains can be transmitted to recombinant prionprotein fibrils in real-time quaking-induced conversion. Reviewed
Sano K, Atarashi R, Ishibashi D, Nakagaki T, Satoh K, Nishida N
Journal of Virology 88 ( 20 ) 11791 - 11801 2014.10
Authorship：Corresponding author Language：English Publishing type：Research paper (scientific journal)
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FK506 reduces abnormal prion protein through the activation of autolysosomal degradation and prolongs survival in prion-infected mice. Reviewed
Nakagaki T, Satoh K, Ishibashi D, Fuse T, Sano K, Kamatari YO, Kuwata K, Shigematsu K, Iwamaru Y, Takenouchi T, Kitani H, Nishida N, Atarashi R
Autophagy 9 ( 9 ) 1386 - 1394 2013.6
Authorship：Last author, Corresponding author Language：English Publishing type：Research paper (scientific journal)
DOI： 10.4161/auto.25381
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Ultrasensitive human prion detection in cerebrospinal fluid by real-time quaking-induced conversion. Reviewed
Atarashi R, Satoh K, Sano K, Fuse T, Yamaguchi N, Ishibashi D, Matsubara T, Nakagaki T, Yamanaka H, Shirabe S, Yamada M, Mizusawa H, Kitamoto T, Klug G, McGlade A, Collins SJ, Nishida N
Nature Medicine 17 ( 2 ) 175 - 178 2011.1
Authorship：Lead author, Corresponding author Language：English Publishing type：Research paper (scientific journal)
DOI： 10.1038/nm.2294
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Rapid end-point quantitation of prion seeding activity with sensitivity comparable to bioassays. Reviewed International coauthorship
Wilham JM, Orrú CD, Bessen RA, Atarashi R, Sano K, Race B, Meade-White KD, Taubner LM, Timmes A, Caughey B
PLoS Pathogens 6 ( 12 ) e1001217 2010.12
Language：English Publishing type：Research paper (scientific journal)
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Hyperefficient PrP Sc amplification of mouse-adapted BSE and scrapie strain by protein misfolding cyclic amplification technique. Reviewed
Fujihara A, Atarashi R, Fuse T, Ubagai K, Nakagaki T, Yamaguchi N, Ishibashi D, Katamine S, Nishida N
The FEBS Journal 276 ( 10 ) 2841 - 2848 2009.4
Authorship：Corresponding author Language：English Publishing type：Research paper (scientific journal)
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Ultrasensitive detection of scrapie prion protein using seeded conversion of recombinant prion protein. Reviewed International coauthorship
Atarashi R, Moore RA, Sim VL, Hughson AG, Dorward DW, Onwubiko HA, Priola SA, Caughey B
Nature methods 4 ( 8 ) 645 - 650 2007.7
Authorship：Lead author Language：English Publishing type：Research paper (scientific journal)
DOI： 10.1038/nmeth1066
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Prion strain-dependent differences in conversion of mutant prion proteins in cell culture. Reviewed International coauthorship
Atarashi R, Sim VL, Nishida N, Caughey B, Katamine S
Journal of Virology 80 ( 16 ) 7854 - 7862 2006.8
Authorship：Lead author, Corresponding author Language：English Publishing type：Research paper (scientific journal)
DOI： 10.1128/JVI.00424-06
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Deletion of N-terminal residues 23-88 from prion protein (PrP) abrogates the potential to rescue PrP-deficient mice from PrP-like protein/doppel-induced Neurodegeneration. Reviewed
Atarashi R, Nishida N, Shigematsu K, Goto S, Kondo T, Sakaguchi S, Katamine S
The Journal of biological chemistry 278 ( 31 ) 28944 - 28949 2003.8
Authorship：Lead author Language：English Publishing type：Research paper (scientific journal)
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Lysine residues are not required for proteasome-mediated proteolysis of cellular prion protein Reviewed
Nishinakagawa T., Homma T., Ikeda A., Hazekawa M., Morita Y., Nakagaki T., Atarashi R., Nishida N., Ishibashi D.
Biochemical and Biophysical Research Communications 735 150807 2024.11
Language：English Publishing type：Research paper (scientific journal) Publisher：Biochemical and Biophysical Research Communications
Cellular prion protein (PrPC) is a glycosylphosphatidylinositol (GPI)-anchored cell-surface protein. The mature cell-surface PrPC is internalized and subsequently degraded by lysosomes. Although, proteasomes are proposed to be involved, the precise mechanism of PrPC degradation remains uncertain. Given that proteins are ubiquitinated primarily on lysine residues, we sought to determine whether lysine residues within PrPC are involved in the ubiquitination and subsequent degradation of PrPC. We generated a plasmid vector expressing a mutant PrPC (called lysine-null PrPC) in which all lysine residues were replaced with arginine residues. Subsequently, we established stably transformed cell lines (designated HpL2-1 PrP-WT and HpL2-1 PrP-K/R, respectively) using the mouse PrPC-deficient neuronal cell line (HpL2-1) and plasmids expressing wild-type (WT) or lysine-null PrPC (PrP-K/R). We found that HpL2-1 PrP-WT and HpL2-1 PrP-K/R cells correctly expressed their respective PrPC which translocated efficiently to the plasma membrane. Subsequently, using immunoblotting and confocal microscopy, we found that treatment with cycloheximide (CHX; a protein synthesis inhibitor) significantly reduced PrPC expression in both these transformed cell lines, indicating that WT and lysine-null PrPC are degraded similarly. Taken together, these results indicate that the lysine residues of PrPC do not regulate its degradation.
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RT-QuIC as ultrasensitive method for prion detection
Atarashi R.
Cell and Tissue Research 392 ( 1 ) 295 - 300 2023.4
Language：English Publishing type：Research paper (scientific journal) Publisher：Cell and Tissue Research
Real-time quaking-induced conversion (RT-QuIC) is a cell-free abnormal form of prion protein (PrPSc) amplification method using recombinant prion protein from Escherichia coli that can measure prion seeding activity in samples with high sensitivity. The advantages of this method are that it is much more sensitive than Western blotting, which is usually used to detect PrPSc, and that prion seeding activity can be easily quantified by combining it with endpoint dilution of the sample, and that it can be amplified in most species and prion strains. A decade has passed since the development of RT-QuIC, and many studies have been reported that take advantage of its characteristics. In particular, its usefulness in the diagnosis of sporadic CJD has been clarified, and it is recommended to be one of the diagnostic criteria. Future challenges include the establishment of a method to differentiate prion strains and application of RT-QuIC to early diagnosis of prion diseases and determination of treatment efficacy.
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Central residues in prion protein PrPC are crucial for its conversion into the pathogenic isoform. Reviewed
Pasiana AD, Miyata H, Chida J, Hara H, Imamura M, Atarashi R, Sakaguchi S
The Journal of biological chemistry 298 ( 9 ) 102381 2022.9
Language：English Publishing type：Research paper (scientific journal)
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Ethanolamine is a new anti-prion compound. Reviewed
Uchiyama K, Hara H, Chida J, Pasiana AD, Imamura M, Mori T, Takatsuki H, Atarashi R, Sakaguchi S
Int J Mol Sci 22 ( 21 ) 11742 2021.10
Language：English Publishing type：Research paper (scientific journal)
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Dextran sulphate inhibits an association of prions with plasmamembrane at the early phase of infection. Reviewed
Fuse T, Nakagaki T, Homma T, Tange H, Yamaguchi N, Atarashi R, Ishibashi D*, Nishida N
Neuroscience Research 171 34 - 40 2021.1
Language：English Publishing type：Research paper (scientific journal)
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Strain-dependent prion infection in mice expressing prion protein with deletion of central residues 91-106. Reviewed
Uchiyama K, Miyata H, Yamaguchi Y, Imamura M, Okazaki M, Pasiana AD, Chida J, Hara H, Atarashi R, Watanabe H, Kondoh G, Sakaguchi S
Int J Mol Sci 21 ( 19 ) 7260 2020.10
Language：English Publishing type：Research paper (scientific journal)
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Impairment of cerebellar long-term depression and GABAergic transmission in prion protein deficient mice ectopically expressing PrPLP/Dpl. Reviewed
Kishimoto Y, Hirono M, Atarashi R, Sakaguchi S, Yoshioka T, Katamine S, Kirino Y
Sci Rep 10 ( 1 ) 15900 2020.9
Language：English Publishing type：Research paper (scientific journal)