H
Hiroshi Nakagawa
Researcher at Chubu University
Publications - 86
Citations - 2530
Hiroshi Nakagawa is an academic researcher from Chubu University. The author has contributed to research in topics: ATP-binding cassette transporter & Single-nucleotide polymorphism. The author has an hindex of 28, co-authored 80 publications receiving 2354 citations. Previous affiliations of Hiroshi Nakagawa include Heidelberg University & Tokyo Institute of Technology.
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Journal ArticleDOI
Generation of hydrogen peroxide primarily contributes to the induction of Fe(II)-dependent apoptosis in Jurkat cells by (−)-epigallocatechin gallate
TL;DR: The mechanism that make catechins cytotoxic in certain tumor cells is due to their ability to produce H(2)O( 2) and that the resulting increase in H-O-2 levels triggers Fe(II)-dependent formation of highly toxic hydroxyl radical, which in turn induces apoptotic cell death.
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Fenton Reaction Is Primarily Involved in a Mechanism of (−)-Epigallocatechin-3-gallate to Induce Osteoclastic Cell Death ☆
Hiroshi Nakagawa,Masaaki Wachi,Je-Tae Woo,Masanori Kato,Shinya Kasai,Fuminori Takahashi,In-Seon Lee,Kazuo Nagai +7 more
TL;DR: Results indicate that the Fenton reaction is primarily involved in EGCG-induced osteoclastic cell death, which is associated with osteoporosis.
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Major SNP (Q141K) variant of human ABC transporter ABCG2 undergoes lysosomal and proteasomal degradations.
Tomoka Furukawa,Kanako Wakabayashi,Ai Tamura,Hiroshi Nakagawa,Yoshihiro Morishima,Yoichi Osawa,Toshihisa Ishikawa +6 more
TL;DR: The results strongly suggest that the major non-synonymous SNP Q141K affects the stability of the ABCG2 protein in the endoplasmic reticulum and enhances its susceptibility to ubiquitin-mediated proteasomal degradation.
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Functional validation of the genetic polymorphisms of human ATP-binding cassette (ABC) transporter ABCG2: identification of alleles that are defective in porphyrin transport
Ai Tamura,Masato Watanabe,Hikaru Saito,Hiroshi Nakagawa,Toshiaki Kamachi,Ichiro Okura,Toshihisa Ishikawa +6 more
TL;DR: Evidence is provided that the variants Q126stop, F208S, S248P, E334stop, and S441N are defective in porphyrin transport, whereas F489L exhibited impaired transport, approximately 10% of the activity observed for the wild type.
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Quercetin suppresses bone resorption by inhibiting the differentiation and activation of osteoclasts.
Je-Tae Woo,Hiroshi Nakagawa,Michitaka Notoya,Takayuki Yonezawa,Nobuyuki Udagawa,In-Seon Lee,Motoko Ohnishi,Hiromi Hagiwara,Kazuo Nagai +8 more
TL;DR: The results suggest that osteoclast progenitors as well as mature osteoclasts, are quercetin's target cells in relation to bone resorption, and that quercETin's suppressive effect on bone Resorption results from both its inhibitory effect on the differentiation of osteoc last progenitor cells into pOCs and from its disruptive effect on actin rings in mature osteclasts.