Atsushi Kurahashi
Tokyo Kasei University
Network
Latest external collaboration on country level. Dive into details by clicking on the dots.
Publication
Featured researches published by Atsushi Kurahashi.
Journal of Lipid Research | 2013
Hema Balakrishna Bhat; Takuma Kishimoto; Mitsuhiro Abe; Asami Makino; Takehiko Inaba; Motohide Murate; Naoshi Dohmae; Atsushi Kurahashi; Kozo Nishibori; Fumihiro Fujimori; Peter Greimel; Reiko Ishitsuka; Toshihide Kobayashi
A mixture of sphingomyelin (SM) and cholesterol (Chol) exhibits a characteristic lipid raft domain of the cell membranes that provides a platform to which various signal molecules as well as virus and bacterial proteins are recruited. Several proteins capable of specifically binding either SM or Chol have been reported. However, proteins that selectively bind to SM/Chol mixtures are less well characterized. In our screening for proteins specifically binding to SM/Chol liposomes, we identified a novel ortholog of Pleurotus ostreatus, pleurotolysin (Ply)A, from the extract of edible mushroom Pleurotus eryngii, named PlyA2. Enhanced green fluorescent protein (EGFP)-conjugated PlyA2 bound to SM/Chol but not to phosphatidylcholine/Chol liposomes. Cell surface labeling of PlyA2-EGFP was abolished after sphingomyelinase as well as methyl-β-cyclodextrin treatment, removing SM and Chol, respectively, indicating that PlyA2-EGFP specifically binds cell surface SM/Chol rafts. Tryptophan to alanine point mutation of PlyA2 revealed the importance of C-terminal tryptophan residues for SM/Chol binding. Our results indicate that PlyA2-EGFP is a novel protein probe to label SM/Chol lipid domains both in cell and model membranes.
The FASEB Journal | 2015
Hema Balakrishna Bhat; Reiko Ishitsuka; Takehiko Inaba; Motohide Murate; Mitsuhiro Abe; Asami Makino; Ayako Kohyama-Koganeya; Kohjiro Nagao; Atsushi Kurahashi; Takuma Kishimoto; Michiru Tahara; Akinori Yamano; Kisaburo Nagamune; Yoshio Hirabayashi; Naoto Juni; Masato Umeda; Fumihiro Fujimori; Kozo Nishibori; Akiko Yamaji-Hasegawa; Peter Greimel; Toshihide Kobayashi
Ceramide phosphoethanolamine (CPE), a sphingomyelin analog, is a major sphingolipid in invertebrates and parasites, whereas only trace amounts are present in mammalian cells. In this study, mushroom‐derived proteins of the aegerolysin family—pleurotolysin A2 (PlyA2; KD = 12nM), ostreolysin (Oly; KD = 1.3 nM), and erylysin A (EryA; KD = 1.3 nM)—strongly associated with CPE/cholesterol (Chol)‐containing membranes, whereas their low affinity to sphingomyelin/Chol precluded establishment of the binding kinetics. Binding specificity was determined by multilamellar liposome binding assays, supported bilayer assays, and solid‐phase studies against a series of neutral and negatively charged lipid classes mixed 1:1 with Chol or phosphatidylcholine. No cross‐reactivity was detected with phosphatidylethanolamine. Only PlyA2 also associated with CPE, independent of Chol content (KD = 41 μM), rendering it a suitable tool for visualizing CPE in lipid‐blotting experiments and biologic samples from sterol auxotrophic organisms. Visualization of CPE enrichment in the CNS of Drosophila larvae (by PlyA2) and in the bloodstream form of the parasite Trypanosoma brucei (by EryA) by fluorescence imaging demonstrated the versatility of aegerolysin family proteins as efficient tools for detecting and visualizing CPE.—Bhat, H. B., Ishitsuka, R., Inaba, T., Murate, M., Abe, M., Makino, A., Kohyama‐Koganeya, A., Nagao, K., Kurahashi, A., Kishimoto, T., Tahara, M., Yamano, A., Nagamune, K., Hirabayashi, Y., Juni, N., Umeda, M., Fujimori, F., Nishibori, K., Yamaji‐Hasegawa, A., Greimel, P., Kobayashi, T. Evaluation of aegerolysins as novel tools to detect and visualize ceramide phosphoethanolamine, a major sphingolipid in invertebrates. FASEB J. 29, 3920‐3934 (2015). www.fasebj.org
The FASEB Journal | 2017
Asami Makino; Mitsuhiro Abe; Reiko Ishitsuka; Motohide Murate; Takuma Kishimoto; Shota Sakai; Françoise Hullin-Matsuda; Yukiko Shimada; Takehiko Inaba; Hideyuki Miyatake; Hideko Tanaka; Atsushi Kurahashi; Chan-Gi Pack; Rinshi S. Kasai; Shuku Kubo; Nicole L. Schieber; Naoshi Dohmae; Naoya Tochio; Kyoji Hagiwara; Yutaka Sasaki; Yoko Aida; Fumihiro Fujimori; Takanori Kigawa; Kozo Nishibori; Robert G. Parton; Akihiro Kusumi; Yasushi Sako; Gregor Anderluh; Makoto Yamashita; Toshihide Kobayashi
We identified a novel, nontoxic mushroom protein that specifically binds to a complex of sphingomyelin (SM), a major sphingolipid in mammalian cells, and cholesterol (Chol). The purified protein, termed nakanori, labeled cell surface domains in an SM‐ and Chol‐dependent manner and decorated specific lipid domains that colocalized with inner leaflet small GTPase H‐Ras, but not K‐Ras. The use of nakanori as a lipid‐domain–specific probe revealed altered distribution and dynamics of SM/Chol on the cell surface of Niemann‐Pick type C fibro‐blasts, possibly explaining some of the disease phenotype. In addition, that nakanori treatment of epithelial cells after influenza virus infection potently inhibited virus release demonstrates the therapeutic value of targeting specific lipid domains for anti‐viral treatment. —Makino, A., Abe, M., Ishitsuka, R., Murate, M., Kishimoto, T., Sakai, S., Hullin‐Matsuda, F., Shimada, Y., Inaba, T., Miyatake, H., Tanaka, H., Kurahashi, A., Pack, C.‐G., Kasai, R. S., Kubo, S., Schieber, N. L., Dohmae, N., Tochio, N., Hagiwara, K., Sasaki, Y., Aida, Y., Fujimori, F., Kigawa, T., Nishibori, K., Parton, R. G., Kusumi, A., Sako, Y., Anderluh, G., Yamashita, M., Kobayashi, T., Greimel, P., Kobayashi, T. A novel sphingomyelin/cholesterol domain‐specific probe reveals the dynamics of the membrane domains during virus release and in Niemann‐Pick type C. FASEB J. 31, 1301–1322 (2017) www.fasebj.org
IFAC Proceedings Volumes | 2013
Bolaji Oguntoyinbo; Toshio Ozawa; Keiju Kawabata; Junji Hirama; Hideyuki Yanagibashi; Yoshio Matsui; Atsushi Kurahashi; Takefumi Shimoda; Makoto Taniguchi; Kouzou Nishibori
Abstract This paper defines the principles of automating the mushroom cultivation process by using their bioelectric potential feedback as a control parameter. Previous studies within this research group examined different environmental stimulations with respect to mushroom bioelectric potential feedback characteristics. This SMA (Speaking Mushroom Approach) system proposes the use of these identified bioelectric feedback characteristics as a method to control the environmental variables. It is theorized that through this system, optimal growth conditions can be realized in a repeatable and reliable manner.
東京家政大学研究紀要. 2, 自然科学 | 2012
Atsushi Kurahashi; Fumihiro Fujimori; Kozo Nishibori
Mycoscience | 2015
Atsushi Kurahashi; Takafumi Shimoda; Masayuki Sato; Fumihiro Fujimori; Junji Hirama; Kozo Nishibori
東京家政大学研究紀要. 2, 自然科学 | 2013
Masayuki Sato; Atsushi Kurahashi; Masahiro Ezaki; Aya Takeda; Yasuo Uemura; Tatsunari Nishi; Kozo Nishibori; Fumihiro Fujimori
Mycoscience | 2015
Masayuki Sato; Atsushi Kurahashi; Kozo Nishibori; Fumihiro Fujimori
Mycoscience | 2014
Atsushi Kurahashi; Masayuki Sato; Toshihide Kobayashi; Kozo Nishibori; Fumihiro Fujimori
Mycoscience | 2015
Masayuki Sato; Atsushi Kurahashi; Kozo Nishibori; Fumihiro Fujimori