Fumio Amano
Osaka University of Pharmaceutical Sciences
73 Papers
660 Citations
Fumio Amano is an academic researcher from Osaka University of Pharmaceutical Sciences. The author has contributed to research in topics: Cell culture & Tumor necrosis factor alpha. The author has an hindex of 21, co-authored 72 publications. Previous affiliations of Fumio Amano include National Institutes of Health & Osaka University.
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Papers
Inhibitory Effects of Hydrolyzable Tannins form Melastoma dodecandrum LOUR. on Nitric Oxide Production by a Murine Macrophage-Like Cell Line, RAW264.7, Activated with Lipopolysaccharide and Interferon-γ
TL;DR: The results suggest that MDL has the pharmacological ability to suppress NO production by activated macrophages and that the hydrolyzable tannins have major inhibitory activities.
67
Salivary gland extract of Rhipicephalus appendiculatus ticks inhibits in vitro transcription and secretion of cytokines and production of nitric oxide by LPS-stimulated JA-4 cells.
TL;DR: The results of the present study suggest that tick salivary gland compounds may exert their effect in vivo by blocking the functions of macrophages in the transcription of cytokines and production of nitric oxide.
65
Isolation of a lipopolysaccharide (LPS)-resistant mutant, with defective LPS binding, of cultured macrophage-like cells.
TL;DR: Results show that one or both of the two LPS-binding proteins might relate to the specific membrane receptor for LPS.
58
Differences in nitric oxide synthase activity in a macrophage-like cell line, RAW264.7 cells, treated with lipopolysaccharide (LPS) in the presence or absence of interferon-gamma (IFN-gamma): possible heterogeneity of iNOS activity.
Tetsuji Noda,Fumio Amano +1 more
TL;DR: There is some heterogeneity of iNOSs induced in macrophage-like cell line treated with bacterial lipopolysaccharide alone and with LPS + IFN-gamma, and the heterogeneity seems to be due at least in part to the requirement for beta-NADPH.
55
Regulation of SulA cleavage by Lon protease by the C-terminal amino acid of SulA, histidine.
Yoshiyuki Ishii,Fumio Amano +1 more
TL;DR: The results suggest that the histidine residue at the extreme C-terminus of SulA is recognized specifically by Lon, leading to a high-affinity interaction between SulA and Lon.