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Affiliation |
Faculty of Agriculture Region of Marine Life Science |
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Title |
Associate Professor |
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Related SDGs |
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HAYASHI Yasuhiro
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Papers 【 display / non-display 】
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Phospholipid Scramblase 1 Localizes Proximal to Sphingomyelin Synthase Isoforms but Is Not Involved in Sphingomyelin Synthesis Reviewed
Yasuhiro Hayashi, Takehiro Suzuki, Naoto Horioka, Naoshi Dohmae, Takashi Tanikawa
Biological and Pharmaceutical Bulletin 2024
Authorship：Lead author, Corresponding author Publishing type：Research paper (scientific journal)
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Two isoledene-type sesquiterpenoids from a soft coral Heteroxenia sp Reviewed
Viqqi Kurnianda, Hao-Chun Hu, Ping-Jyun Sung, Yasuhiro Hayashi, Kanami Mori-Yasumoto, Ayumi Suetake, Hikari Nakayama, Mina Yasumoto-Hirose, Yuna Tsutsumi, Genta Koja, Yu-Chi Tsai, Takahiro Jomori, Junichi Tanaka
Tetrahedron Letters 2024
Publishing type：Research paper (scientific journal)
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Baicalin target protein, Annexin A2, is a target of new antitumor drugs Reviewed
Yoshio Kusakabe, Kazuya Matsumoto, Takahiro Tsuyuki, Yasuhiro Hayashi, Hideaki Watanabe
Scientific Reports 2024
Publishing type：Research paper (scientific journal)
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Hama K., Fujiwara Y., Imai K., Kusakabe Y., Hayashi Y., Takashima S., Azuma S., Kondo M., Yamashita A., Takita R., Shimozawa N., Yokoyama K.
Journal of Lipid Research 67 ( 2 ) 2026.2
Publishing type：Research paper (scientific journal) Publisher：Journal of Lipid Research
X-linked adrenoleukodystrophy (X-ALD) is a congenital metabolic disorder characterized mainly by inflammatory demyelination and adrenal insufficiency. Newborn screening using hexacosanoyl lysophosphatidylcholine (C26:0-LPC) in dried blood spots as a diagnostic marker can successfully identify potential patients with X-ALD and prevent disease onset. C26:0-LPC accumulates in patients with X-ALD, although the machinery synthesizing it has remained unclear. In this study, we focused on phosphatidylcholine (PC) with C26:0 moiety as a precursor of C26:0-LPC. We identified that lysophospholipid (LPL) acyltransferase 10 (LPLAT10)/LPCAT4/LPEAT2/ AGPAT7 (1-acylglycerol-3-phosphate O-acyltransferase 7) is the responsible LPL acyltransferase that produces PC with C26:0 moiety by transferring C26:0-CoA into 2-acyl-LPC. We also found that LPLAT10 deficiency decreased the amount of C26:0-LPC in fibroblasts from X-ALD patients. Mechanistically, LPLAT10 introduced saturated fatty acid-CoA of various chain lengths as substrates into the sn-1 position of LPC but did not transfer C26:0-CoA to other LPL classes, such as lysophosphatidylethanolamine. Structural analysis revealed that a trimethylamine group of PC was placed between two tryptophan residues (W242 and W244), forming a W-X-W motif, possibly through cation-π interaction. Finally, it was shown that exogenously administered C26:0 FFA-d<inf>4</inf> was preferentially incorporated into sphingolipids in the absence of LPLAT10. These results suggest that C26:0-LPC is produced through acyl-chain remodeling of PC catalyzed by LPLAT10 and accumulates in the plasma from X-ALD patients.
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Onnamides A and B Suppress Hepatitis B Virus Transcription by Inhibiting Viral Promoter Activity Reviewed
Hayashi Y., Arizono S., Higa N., Tyas T.A., Akahori Y., Maeda K., Toyama M., Mori-Yasumoto K., Yasumoto-Hirose M., Miyakawa K., Tanaka J., Jomori T.
Marine Drugs 24 ( 1 ) 2026.1
Language：English Publishing type：Research paper (scientific journal) Publisher：Marine Drugs
We recently reported that onnamide A, a marine-derived natural compound isolated from the sponge Theonella sp., inhibits the entry process of SARS-CoV-2 infection. However, its antiviral activity against other viruses remains largely unexplored. Here, we investigated the effects of onnamide A and its structurally related analog, onnamide B, on hepatitis B virus (HBV) infection. Using iNTCP cells, a hepatoblastoma-derived cell line permissive to HBV infection, we found that onnamides A and B exhibited cytotoxicity, with CC<inf>50</inf> values of 0.53 ± 0.10 μM and 2.37 ± 0.25 μM, respectively. Following HBV infection, the levels of total HBV RNA were significantly reduced by onnamide A (IC<inf>50</inf> = 0.06 ± 0.01 μM) and onnamide B (IC<inf>50</inf> = 0.23 ± 0.06 μM). Notably, both compounds markedly decreased the levels of HBV pregenomic RNA. Furthermore, significant inhibition was particularly evident when onnamide treatment was initiated after HBV infection. Consistent with these observations, onnamides did not affect HBV binding, entry, or covalently closed circular DNA formation, but they significantly suppressed HBV RNA transcription. In particular, the transcriptional activities driven by the core and X promoters were markedly inhibited by onnamide treatment. Taken together, our findings demonstrate that onnamides possess potent anti-HBV activity and highlight their potential as candidate compounds targeting HBV RNA transcription.
DOI： 10.3390/md24010021
