@article{miyazawa_bogdan_hashimoto_tsuji_2019, title={Iron-induced transferrin receptor-1 mRNA destabilization: A response to "Neither miR-7-5p nor miR-141-3p is a major mediator of iron-responsive transferrin receptor-1 mRNA degradation"}, volume={25}, ISSN={["1469-9001"]}, DOI={10.1261/rna.073270.119}, abstractNote={We read with great interest the Divergent Views article by Connell and colleagues disputing our recent publication describing a role for two microRNAs in the iron-mediated regulation of transferrin receptor 1 (TfR1) mRNA stability. Our publication sought to shed light on a long-standing question in the field of cellular iron metabolism, and we welcome commentary and critique. However, there are several critical issues contained in the article by Connell and colleagues that require further consideration. We appreciate the opportunity to reply here.}, number={11}, journal={RNA}, author={Miyazawa, Masaki and Bogdan, Alexander R. and Hashimoto, Kazunori and Tsuji, Yoshiaki}, year={2019}, month={Nov}, pages={1416–1420} }
 @article{miyazawa_bogdan_tsuji_2019, title={Perturbation of Iron Metabolism by Cisplatin through Inhibition of Iron Regulatory Protein 2}, volume={26}, ISSN={["2451-9448"]}, DOI={10.1016/j.chembiol.2018.10.009}, abstractNote={Cisplatin is classically known to exhibit anticancer activity through DNA damage in the nucleus. Here we found a mechanism by which cisplatin affects iron metabolism, leading to toxicity and cell death. Cisplatin causes intracellular iron deficiency through direct inhibition of the master regulator of iron metabolism, iron regulatory protein 2 (IRP2) with marginal effects on IRP1. Cisplatin, but not carboplatin or transplatin, binds human IRP2 at Cys512 and Cys516 and impairs IRP2 binding to iron-responsive elements of ferritin and transferrin receptor-1 (TfR1) mRNAs. IRP2 inhibition by cisplatin caused ferritin upregulation and TfR1 downregulation leading to sustained intracellular iron deficiency. Cys512/516Ala mutant IRP2 made cells more resistant to cisplatin. Furthermore, combination of cisplatin and the iron chelator desferrioxamine enhanced cytotoxicity through augmented iron depletion in culture and xenograft mouse model. Collectively, cisplatin is an inhibitor of IRP2 that induces intracellular iron deficiency.}, number={1}, journal={CELL CHEMICAL BIOLOGY}, author={Miyazawa, Masaki and Bogdan, Alexander R. and Tsuji, Yoshiaki}, year={2019}, month={Jan}, pages={85-+} }
 @article{martin_gray_kilb_minchew_2016, title={Analyzing consortial "big deals" via a cost-per-cited-reference (CPCR) metric}, volume={42}, number={4}, journal={Serials Review}, author={Martin, V. and Gray, T. and Kilb, M. and Minchew, T.}, year={2016}, pages={293–305} }
 @article{ishii_yasuda_miyazawa_mitsushita_johnson_hartman_ishii_2016, title={Infertility and recurrent miscarriage with complex II deficiency-dependent mitochondrial oxidative stress in animal models}, volume={155}, journal={Mechanisms of Ageing and Development}, author={Ishii, T. and Yasuda, K. and Miyazawa, M. and Mitsushita, J. and Johnson, T. E. and Hartman, P. S. and Ishii, N.}, year={2016}, pages={22–35} }
 @misc{wilson_bogdan_miyazawa_hashimoto_tsuji_2016, title={Siderophores in Iron Metabolism: From Mechanism to Therapy Potential}, volume={22}, ISSN={["1471-499X"]}, DOI={10.1016/j.molmed.2016.10.005}, abstractNote={Iron is an essential nutrient for life. During infection, a fierce battle of iron acquisition occurs between the host and bacterial pathogens. Bacteria acquire iron by secreting siderophores, small ferric iron-binding molecules. In response, host immune cells secrete lipocalin 2 (also known as siderocalin), a siderophore-binding protein, to prevent bacterial reuptake of iron-loaded siderophores. To counter this threat, some bacteria can produce lipocalin 2-resistant siderophores. This review discusses the recently described molecular mechanisms of siderophore iron trafficking between host and bacteria, highlighting the therapeutic potential of exploiting pathogen siderophore machinery for the treatment of antibiotic-resistant bacterial infections. Because the latter reflect a persistent problem in hospital settings, siderophore-targeting or siderophore-based compounds represent a promising avenue to combat such infections.}, number={12}, journal={TRENDS IN MOLECULAR MEDICINE}, author={Wilson, Briana R. and Bogdan, Alexander R. and Miyazawa, Masaki and Hashimoto, Kazunori and Tsuji, Yoshiaki}, year={2016}, month={Dec}, pages={1077–1090} }
 @misc{bogdan_miyazawa_hashimoto_tsuji_2016, title={Regulators of Iron Homeostasis: New Players in Metabolism, Cell Death, and Disease}, volume={41}, ISSN={["1362-4326"]}, DOI={10.1016/j.tibs.2015.11.012}, abstractNote={Iron is necessary for life, but can also cause cell death. Accordingly, cells evolved a robust, tightly regulated suite of genes for maintaining iron homeostasis. Previous mechanistic studies on iron homeostasis have granted insight into the role of iron in human health and disease. We highlight new regulators of iron metabolism, including iron-trafficking proteins [solute carrier family 39, SLC39, also known as ZRT/IRT-like protein, ZIP; and poly-(rC)-binding protein, PCBP] and a cargo receptor (NCOA4) that is crucial for release of ferritin-bound iron. We also discuss emerging roles of iron in apoptosis and a novel iron-dependent cell death pathway termed 'ferroptosis', the dysregulation of iron metabolism in human pathologies, and the use of iron chelators in cancer therapy.}, number={3}, journal={TRENDS IN BIOCHEMICAL SCIENCES}, author={Bogdan, Alexander R. and Miyazawa, Masaki and Hashimoto, Kazunori and Tsuji, Yoshiaki}, year={2016}, month={Mar}, pages={274–286} }
 @article{huang_miyazawa_tsuji_2014, title={Distinct regulatory mechanisms of the human ferritin gene by hypoxia and hypoxia mimetic cobalt chloride at the transcriptional and post-transcriptional levels}, volume={26}, ISSN={["1873-3913"]}, DOI={10.1016/j.cellsig.2014.08.018}, abstractNote={Cobalt chloride has been used as a hypoxia mimetic because it stabilizes hypoxia inducible factor-1α (HIF1-α) and activates gene transcription through a hypoxia responsive element (HRE). However, differences between hypoxia and hypoxia mimetic cobalt chloride in gene regulation remain elusive. Expression of ferritin, the major iron storage protein, is regulated at the transcriptional and posttranscriptional levels through DNA and RNA regulatory elements. Here we demonstrate that hypoxia and cobalt chloride regulate ferritin heavy chain (ferritin H) expression by two distinct mechanisms. Both hypoxia and cobalt chloride increased HIF1-α but a putative HRE in the human ferritin H gene was not activated. Instead, cobalt chloride but not hypoxia activated ferritin H transcription through an antioxidant responsive element (ARE), to which Nrf2 was recruited. Intriguingly, cobalt chloride downregulated ferritin H protein expression while it upregulated other ARE-regulated antioxidant genes in K562 cells. Further characterization demonstrated that cobalt chloride increased interaction between iron regulatory proteins (IRP1 and IRP2) and iron responsive element (IRE) in the 5′UTR of ferritin H mRNA, resulting in translational block of the accumulated ferritin H mRNA. In contrast, hypoxia had marginal effect on ferritin H transcription but increased its translation through decreased IRP1–IRE interaction. These results suggest that hypoxia and hypoxia mimetic cobalt chloride employ distinct regulatory mechanisms through the interplay between DNA and mRNA elements at the transcriptional and post-transcriptional levels.}, number={12}, journal={CELLULAR SIGNALLING}, author={Huang, Bo-Wen and Miyazawa, Masaki and Tsuji, Yoshiaki}, year={2014}, month={Dec}, pages={2702–2709} }
 @article{miyazawa_tsuji_2014, title={Evidence for a novel antioxidant function and isoform-specific regulation of the human p66Shc gene}, volume={25}, ISSN={["1939-4586"]}, DOI={10.1091/mbc.e13-11-0666}, abstractNote={The mammalian Shc family, composed of p46, p52, and p66 isoforms, serves as an adaptor protein in cell growth and stress response. p66Shc was shown to be a negative lifespan regulator by acting as a prooxidant protein in mitochondria; however, the regulatory mechanisms of p66Shc expression and function are incompletely understood. This study provides evidence for new features of p66Shc serving as an antioxidant and critical protein in cell differentiation. Unique among the Shc family, transcription of p66Shc is activated through the antioxidant response element (ARE)–nuclear factor erythroid 2–related factor 2 (Nrf2) pathway in K562 human erythroleukemia and other cell types after treatment with hemin, an iron-containing porphyrin. Phosphorylated p66Shc at Ser-36, previously reported to be prone to mitochondrial localization, is increased by hemin treatment, but p66Shc remains exclusively in the cytoplasm. p66Shc knockdown inhibits hemin-induced erythroid differentiation, in which reactive oxygen species production and apoptosis are significantly enhanced in conjunction with suppression of other ARE-dependent antioxidant genes. Conversely, p66Shc overexpression is sufficient for inducing erythroid differentiation. Collectively these results demonstrate the isoform-specific regulation of the Shc gene by the Nrf2-ARE pathway and a new antioxidant role of p66Shc in the cytoplasm. Thus p66Shc is a bifunctional protein involved in cellular oxidative stress response and differentiation.}, number={13}, journal={MOLECULAR BIOLOGY OF THE CELL}, author={Miyazawa, Masaki and Tsuji, Yoshiaki}, year={2014}, month={Jul}, pages={2116–2127} }