Ken Ando
University of Tokyo
28 Papers
392 Citations
Ken Ando is an academic researcher from University of Tokyo. The author has contributed to research in topics: Vitamin E & Lipid peroxidation. The author has an hindex of 15, co-authored 28 publications.
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Papers
Membrane proteins of human erythrocytes are modified by advanced glycation end products during aging in the circulation.
TL;DR: Results indicate that membrane proteins of circulating erythrocytes undergo CML-modification, and the modified proteins accumulated in an age-dependent manner during the life span of ery Throcytes.
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Effect of n-3 polyunsaturated fatty acid supplementation on lipid peroxidation of rat organs.
TL;DR: The results indicate that high fish oil intake does not induce increased levels of phospholipid hydroperoxides and TBARS in rat organs.
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Novel insights into FGD3, a putative GEF for Cdc42, that undergoes SCF(FWD1/beta-TrCP)-mediated proteasomal degradation analogous to that of its homologue FGD1 but regulates cell morphology and motility differently from FGD1.
Makio Hayakawa,Masahide Matsushima,Hiroshi Hagiwara,Toshiyuki Oshima,Tomofumi Fujino,Ken Ando,Kiyomi Kikugawa,Hirofumi Tanaka,Keiji Miyazawa,Masatoshi Kitagawa +9 more
TL;DR: It is demonstrated that the highly homologous GEFs, FGD1 and FGD3 play different roles to regulate cellular functions but that their intracellular levels are tightly controlled by the same destruction pathway through SCFFWD1/β‐TrCP.
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Effect of n-3 fatty acid supplementation on lipid peroxidation and protein aggregation in rat erythrocyte membranes
Ken Ando,Kunihide Nagata,Masatoshi Beppu,Kiyomi Kikugawa,Terue Kawabata,Kyoko Hasegawa,Masao Suzuki +6 more
TL;DR: If a sufficient amount of vitamin E is supplied, n−3 fatty acid supplementation may give no undesirable oxidative effects on rat erythrocytes in the circulation and the supplementation increased the susceptibility of isolated ery throatcytes to lipid peroxidation, but not to protein aggregation, under the aerobic conditions.
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Induction of band 3 aggregation in erythrocytes results in anti-band 3 autoantibody binding to the carbohydrate epitopes of band 3.
TL;DR: The results indicate that anti-band 3 binds to the carbohydrate epitopes of band 3 on erythrocytes when band 3 is aggregated by oxidative and nonoxidative mechanisms.
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