TOHOKU UNIVERSITY Researchers - Mitsuyo Matsumoto

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Mitsuyo Matsumoto

Section

New Industry Creation Hatchery Center

Job title

Specially Appointed Assistant Professor(Research)

Degree

researchmap

https://researchmap.jp/mitsuyo.matsumoto

J-GLOBAL ID

200901012337989310

e-Rad No.

80400448

Research History 6

2026/04 - Present

東北大学未来科学技術共同研究センター特任助教
2024/01 - Present

東北大学多元物質科学研究所助教
2014 -

Tohoku University　Graduate School of Medicine
2012 -

Tohoku University　Tohoku Medical Megabank Organization
2010 -

東北大学大学院医学系研究科助教
2008 -

がん集学的治療財団若手研究員

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Research Interests 4

微小環境
転写因子
がん
Environmental and Biological Chemistry

Research Areas 2

Life sciences / Molecular biology /
Life sciences / Tumor biology /

Papers 62

The transcription factor BACH1 at the crossroads of cancer biology: From epithelial–mesenchymal transition to ferroptosis Peer-reviewed

Kazuhiko Igarashi, Hironari Nishizawa, Yuriko Saiki, Mitsuyo Matsumoto

Journal of Biological Chemistry　297　(3)　101032-101032　2021/09
Publisher: Elsevier {BV}
DOI： 10.1016/j.jbc.2021.101032 　

ISSN： 0021-9258
BACH1 Promotes Pancreatic Cancer Metastasis by Repressing Epithelial Genes and Enhancing Epithelial-Mesenchymal Transition. International-journal Peer-reviewed

Masaki Sato, Mitsuyo Matsumoto, Yuriko Saiki, Mahabub Alam, Hironari Nishizawa, Masahiro Rokugo, Andrey Brydun, Shinji Yamada, Mika K Kaneko, Ryo Funayama, Mamoru Ito, Yukinari Kato, Keiko Nakayama, Michiaki Unno, Kazuhiko Igarashi

Cancer research　80　(6)　1279-1292　2020/03/15

DOI： 10.1158/0008-5472.CAN-18-4099 　

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Pancreatic ductal adenocarcinoma (PDAC) is among the cancers with the poorest prognoses due to its highly malignant features. BTB and CNC homology 1 (BACH1) has been implicated in RAS-driven tumor formation. We focused on the role of BACH1 in PDAC, more than 90% of which have KRAS mutation. Knockdown of BACH1 in PDAC cell lines reduced cell migration and invasion, in part, by increasing E-cadherin expression, whereas its overexpression showed opposite effects. BACH1 directly repressed the expression of FOXA1 that is known to activate the expression of CDH1 encoding E-cadherin and to inhibit epithelial-to-mesenchymal transition. BACH1 also directly repressed the expression of genes important for epithelial cell adhesion including CLDN3 and CLDN4. In a mouse orthotopic implantation model, BACH1 was required for the high metastatic ability of AsPC-1 cells. IHC analysis of clinical specimens with a newly developed anti-BACH1 mAb revealed that high expression of BACH1 is a poor prognostic factor. These results suggest that the gene regulatory network of BACH1 and downstream genes including CDH1 contribute to the malignant features of PDAC by regulating epithelial-to-mesenchymal transition. SIGNIFICANCE: Greater understanding of the gene regulatory network involved in epithelial-to-mesenchymal transition of pancreatic cancer cells will provide novel therapeutic targets and diagnostic markers.
Ferroptosis is controlled by the coordinated transcriptional regulation of glutathione and labile iron metabolism by the transcription factor BACH1. International-journal Peer-reviewed

Hironari Nishizawa, Mitsuyo Matsumoto, Tomohiko Shindo, Daisuke Saigusa, Hiroki Kato, Katsushi Suzuki, Masaki Sato, Yusho Ishii, Hiroaki Shimokawa, Kazuhiko Igarashi

The Journal of biological chemistry　295　(1)　69-82　2020/01/03

DOI： 10.1074/jbc.RA119.009548 　

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Ferroptosis is an iron-dependent programmed cell death event, whose regulation and physiological significance remain to be elucidated. Analyzing transcriptional responses of mouse embryonic fibroblasts exposed to the ferroptosis inducer erastin, here we found that a set of genes related to oxidative stress protection is induced upon ferroptosis. We considered that up-regulation of these genes attenuates ferroptosis induction and found that the transcription factor BTB domain and CNC homolog 1 (BACH1), a regulator in heme and iron metabolism, promotes ferroptosis by repressing the transcription of a subset of the erastin-induced protective genes. We noted that these genes are involved in the synthesis of GSH or metabolism of intracellular labile iron and include glutamate-cysteine ligase modifier subunit (Gclm), solute carrier family 7 member 11 (Slc7a11), ferritin heavy chain 1 (Fth1), ferritin light chain 1 (Ftl1), and solute carrier family 40 member 1 (Slc40a1). Ferroptosis has also been previously shown to induce cardiomyopathy, and here we observed that Bach1-/- mice are more resistant to myocardial infarction than WT mice and that the severity of ischemic injury is decreased by the iron-chelator deferasirox, which suppressed ferroptosis. Our findings suggest that BACH1 represses genes that combat labile iron-induced oxidative stress, and ferroptosis is stimulated at the transcriptional level by BACH1 upon disruption of the balance between the transcriptional induction of protective genes and accumulation of iron-mediated damage. We propose that BACH1 controls the threshold of ferroptosis induction and may represent a therapeutic target for alleviating ferroptosis-related diseases, including myocardial infarction.
Bach1 promotes muscle regeneration through repressing Smad-mediated inhibition of myoblast differentiation. International-journal Peer-reviewed

Katsushi Suzuki, Mitsuyo Matsumoto, Yasutake Katoh, Liang Liu, Kyoko Ochiai, Yuta Aizawa, Ryoichi Nagatomi, Hiroshi Okuno, Eiji Itoi, Kazuhiko Igarashi

PloS one　15　(8)　e0236781　2020

DOI： 10.1371/journal.pone.0236781 　

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It has been reported that Bach1-deficient mice show reduced tissue injuries in diverse disease models due to increased expression of heme oxygenase-1 (HO-1)that possesses an antioxidant function. In contrast, we found that Bach1 deficiency in mice exacerbated skeletal muscle injury induced by cardiotoxin. Inhibition of Bach1 expression in C2C12 myoblast cells using RNA interference resulted in reduced proliferation, myotube formation, and myogenin expression compared with control cells. While the expression of HO-1 was increased by Bach1 silencing in C2C12 cells, the reduced myotube formation was not rescued by HO-1 inhibition. Up-regulations of Smad2, Smad3 and FoxO1, known inhibitors of muscle cell differentiation, were observed in Bach1-deficient mice and Bach1-silenced C2C12 cells. Therefore, Bach1 may promote regeneration of muscle by increasing proliferation and differentiation of myoblasts.
Regulatory signatures of liver regeneration distilled by integrative analysis of mRNA, histone methylation, and proteomics Peer-reviewed

Yoshihiro Sato, Yasutake Katoh, Mitsuyo Matsumoto, Masaki Sato, Masayuki Ebina, Ari Itoh-Nakadai, Ryo Funayama, Keiko Nakayama, Michiaki Unno, Kazuhiko Igarashi

JOURNAL OF BIOLOGICAL CHEMISTRY　292　(19)　8019-+　2017/05

DOI： 10.1074/jbc.M116.774547 　

ISSN： 0021-9258

eISSN： 1083-351X
Genomewide approaches for BACH1 target genes in mouse embryonic fibroblasts showed BACH1-Pparg pathway in adipogenesis. International-journal Peer-reviewed

Mitsuyo Matsumoto, Keiichi Kondo, Takuma Shiraki, Andrey Brydun, Ryo Funayama, Keiko Nakayama, Nobuo Yaegashi, Hideki Katagiri, Kazuhiko Igarashi

Genes to cells : devoted to molecular & cellular mechanisms　21　(6)　553-67　2016/06

DOI： 10.1111/gtc.12365 　

ISSN： 1356-9597

eISSN： 1365-2443
Validation of multiple single nucleotide variation calls by additional exome analysis with a semiconductor sequencer to supplement data of whole-genome sequencing of a human population Peer-reviewed

Ikuko N. Motoike, Mitsuyo Matsumoto, Inaho Danjoh, Fumiki Katsuoka, Kaname Kojima, Naoki Nariai, Yukuto Sato, Yumi Yamaguchi-Kabata, Shin Ito, Hisaaki Kudo, Ichiko Nishijima, Satoshi Nishikawa, Xiaoqing Pan, Rumiko Saito, Sakae Saito, Tomo Saito, Matsuyuki Shirota, Kaoru Tsuda, Junji Yokozawa, Kazuhiko Igarashi, Naoko Minegishi, Osamu Tanabe, Nobuo Fuse, Masao Nagasaki, Kengo Kinoshita, Jun Yasuda, Masayuki Yamamoto

BMC GENOMICS　15　673　2014/08

DOI： 10.1186/1471-2164-15-673 　

ISSN： 1471-2164
Bach1 is critical for the transformation of mouse embryonic fibroblasts by Ras(V12) and maintains ERK signaling Peer-reviewed

A. Nakanome, A. Brydun, M. Matsumoto, K. Ota, R. Funayama, K. Nakayama, M. Ono, K. Shiga, T. Kobayashi, K. Igarashi

ONCOGENE　32　(27)　3231-3245　2013/07

DOI： 10.1038/onc.2012.336 　

ISSN： 0950-9232
Estrogen signaling ability in human endometrial cancer through the cancer-stromal interaction Peer-reviewed

Mitsuyo Matsumoto, Yuri Yamaguchi, Yuko Seino, Atsushi Hatakeyama, Hiroyuki Takei, Hitoshi Niikura, Kiyoshi Ito, Takashi Suzuki, Hironobu Sasano, Nobuo Yaegashi, Shin-ichi Hayashi

ENDOCRINE-RELATED CANCER　15　(2)　451-463　2008/06

DOI： 10.1677/ERC-07-0227 　

ISSN： 1351-0088

eISSN： 1479-6821
Optimum Serum Concentration Enhances Migration of MDA-MB-231 Triple-Negative Breast Cancer Cells and Promotes Intracellular Delivery of Proapoptotic Domain via Cell-Penetrating Peptides. International-journal Peer-reviewed

Yurina Araki, Tomoka Takatani-Nakase, Sohei Ninomiya, Mitsuyo Matsumoto, Hisaaki Hirose, Yoshimasa Kawaguchi, Daisuke Fujiwara, Masataka Michigami, Hironori Katoh, Takehiko Wada, Shiroh Futaki, Ikuo Fujii, Masaya Hagiwara, Ikuhiko Nakase

Molecular pharmaceutics　23　(2)　730-742　2026/02/02
Publisher: American Chemical Society (ACS)
DOI： 10.1021/acs.molpharmaceut.5c00916 　

ISSN： 1543-8384

eISSN： 1543-8392

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Breast cancer remains one of the most prevalent cancers among women, with triple-negative breast cancer (TNBC), lacking estrogen receptor, progesterone receptor, and human epidermal growth factor receptor 2, accounting for approximately 15-20% of all patients with breast cancer. TNBC is notably aggressive, with a high invasive, metastatic, and recurrence potential. In this study, we found that the migration and invasion capabilities of MDA-MB-231 cells, derived from human TNBC, were strongly influenced by the serum concentration. Transwell assays revealed that TNBC cell migration varied depending on the fetal bovine serum (FBS) level, with an optimal concentration that substantially enhanced migration and invasion. In contrast, non-TNBC MCF-7 cells exhibited no such serum-dependent migration pattern. In addition to data-independent acquisition (DIA) phosphoproteomic analysis for understanding the mechanisms, the cellular uptake of the flock house virus coat (35-49) peptide, a type of arginine-rich cell-penetrating peptide with serum-dependent cellular uptake efficacy, was significantly increased under the optimal serum conditions, which induces cell migration, leading to efficient delivery of apoptosis-inducible peptide and TNBC-killing activity. Our findings highlight the critical role of serum concentration in regulating TNBC behavior and offer insights into leveraging serum-responsive delivery systems for targeted breast cancer therapy.
Transcription factor BACH1 promotes epithelial-mesenchymal transition by repressing iron metabolism-related genes. International-journal Peer-reviewed

Shuichiro Hayashi, Mitsuyo Matsumoto, Liang Liu, Miho Tanaka, Michiaki Unno, Kazuhiko Igarashi

Biochemical and biophysical research communications　767　151898-151898　2025/06/30

DOI： 10.1016/j.bbrc.2025.151898 　

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Pancreatic adenocarcinoma (PDAC) is one of the cancers with a very poor prognosis for its highly invasive and metastatic ability. Epithelial-mesenchymal transition (EMT) is critical for metastasis and invasion of PDAC cells, in which the expression of epithelial genes, such as E-cadherin (CDH1), decreases and that of mesenchymal genes increases. Transcription factor BTB and CNC homology 1 (BACH1) promotes EMT of PDAC cells in part by indirectly suppressing the expression of CDH1. However, the mechanism behind this is not yet clear. Considering recent reports on a link between intracellular iron and CDH1 expression in cancer cells, we examined whether BACH1 represses CDH1 expression by regulating ferritin gene. When AsPC-1 PDAC cells were treated with the iron chelator deferasirox (DFX), CDH1 expression was increased. While BACH1 knockdown resulted in increased CDH1 expression, combined knockdown of BACH1 and ferritin heavy chain gene (FTH1) reversed CDH1 expression. Tank-binding kinase 1 (TBK1), an upstream regulator of BACH1, was necessary to maintain EMT gene expression patterns in AsPC-1 cells. TBK1 was redundant with BACH1 to maintain VIM expression in SW1990 PDAC cells, suggesting its BACH1-independent role in EMT. Therefore, the regulation of CDH1 and EMT by BACH1 involves FTH1 and intracellular iron as mediators and TBK1 as an upstream and parallel regulator.
Positive coactivator PC4 shows dynamic nucleolar distribution required for rDNA transcription and protein synthesis. International-journal Peer-reviewed

Stephanie Kaypee, Kyoko Ochiai, Hiroki Shima, Mitsuyo Matsumoto, Mahabub Alam, Tsuyoshi Ikura, Tapas K Kundu, Kazuhiko Igarashi

Cell communication and signaling : CCS　23　(1)　283-283　2025/06/14
Publisher: Springer Science and Business Media LLC
DOI： 10.1186/s12964-025-02238-4 　

eISSN： 1478-811X

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The nucleolus is the site of rDNA transcription and ribosome biogenesis. Alterations in nucleolar function and architecture correlate with drastic heterochromatin rearrangement and global changes in gene expression. However, the precise mechanism that connects nucleolar function to heterochromatin organization and transcription is yet unknown. Here, we report that the RNA polymerase II (RNA pol II) transactivator and chromatin condenser, Positive Coactivator 4 (PC4), is a bona fide nucleolar protein. PC4 showed dynamic nucleolar accumulation, which is critical for rDNA transcription. The lysine acetyltransferase, KAT5 (Tip60) acetylates PC4 at K35, which facilitates nucleolar release of PC4 and concomitated inhibition of rDNA transcription. By employing PC4 mutant, which is defective in nucleolar accumulation, we found that nucleolar PC4 is crucial for RNA pol I-mediated rDNA transcription. To validate this significant novel role of PC4, in the context of nucleolus organization and function, at the organismal level, we looked into B cell-specific conditional knockout of Sub1 encoding PC4 in mice, which revealed that indeed the rDNA transcription and protein synthesis in B cells are severely repressed in the absence of PC4. Furthermore, PC4 CKO B cells were associated with the loss of H3K9me3-marked heterochromatin foci but not global H3K9me3 levels. LC-MS/MS analysis of the H3K9me3 chromatin complexes revealed that most non-histone heterochromatin proteins were reduced or absent in the constitutive heterochromatin of PC4 CKO B cells. These findings establish PC4 as a critical functional component of nucleolus for rDNA transcription.
Metabolic cell death of labile iron deficiency as a vulnerability of head and neck squamous cell carcinoma evaded by BACH1

Masahiro Rokugo, Kazuki Nakamura, Mitsuyo Matsumoto, Akari Endo, Long Chi Nguyen, Hironari Nishizawa, Ryohei Shima, Hitomi Kashiwagi, Akira Okoshi, Ayako Nakanome, Ryo Funayama, Keiko Nakayama, Takenori Ogawa, Takaaki Abe, Yukio Katori, Kazuhiko Igarashi

2025/04/11

DOI： 10.1101/2025.04.07.647470 　
Heme regulates protein interactions and phosphorylation of BACH2 intrinsically disordered region in humoral response Peer-reviewed

Miki Watanabe-Matsui, Shun Kadoya, Kei Segawa, Hiroki Shima, Tadashi Nakagawa, Yuko Nagasawa, Shuichiro Hayashi, Mitsuyo Matsumoto, Mariko Ikeda, Akihiko Muto, Kyoko Ochiai, Long C. Nguyen, Katsumi Doh-Ura, Mikako Shirouzu, Keiko Nakayama, Kazutaka Murayama, Kazuhiko Igarashi

iScience　28　(1)　111529-111529　2025/01
Publisher: Elsevier BV
DOI： 10.1016/j.isci.2024.111529 　

ISSN： 2589-0042
Intracellular biliverdin dynamics during ferroptosis. International-journal Peer-reviewed

Kazuma Nakajima, Hironari Nishizawa, Guan Chen, Shunichi Tsuge, Mie Yamanaka, Machi Kiyohara, Riko Irikura, Mitsuyo Matsumoto, Kozo Tanaka, Rei Narikawa, Kazuhiko Igarashi

Journal of biochemistry　2024/09/28

DOI： 10.1093/jb/mvae067 　

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Ferroptosis is a cell death mechanism mediated by iron-dependent lipid peroxidation. Although ferroptosis has garnered attention as a cancer-suppressing mechanism, there are still limited markers available for identifying ferroptotic cells or assessing their sensitivity to ferroptosis. The study focused on biliverdin, an endogenous reducing substance in cells, and examined the dynamics of intracellular biliverdin during ferroptosis using a biliverdin-binding cyanobacteriochrome. It was found that intracellular biliverdin decreases during ferroptosis and that this decrease is specific to ferroptosis among different forms of cell death. Furthermore, the feasibility of predicting sensitivity to ferroptosis by measuring intracellular biliverdin was demonstrated using a ferroptosis model induced by the re-expression of the transcription factor BACH1. These findings provide further insight into ferroptosis research and are expected to contribute to the development of cancer therapies that exploit ferroptosis.
Absolute quantification of BACH1 and BACH2 transcription factors in B and plasma cells reveals their dynamic changes and unique roles Peer-reviewed

Takeshi Kurasawa, Akihiko Muto, Mitsuyo Matsumoto, Kyoko Ochiai, Kazutaka Murayama, Kazuhiko Igarashi

The Journal of Biochemistry　176　(6)　449-459　2024/09/25
Publisher: Oxford University Press (OUP)
DOI： 10.1093/jb/mvae065 　

ISSN： 0021-924X

eISSN： 1756-2651

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Abstract Changes in the absolute protein amounts of transcription factors are important for regulating gene expression during cell differentiation and in responses to changes in the cellular and extracellular environment. However, few studies have focused on the absolute quantification of mammalian transcription factors. In this study, we established an absolute quantification method for the transcription factors BACH1 and BACH2, which are expressed in B cells and regulated by direct heme binding. The method used purified recombinant proteins as controls in western blotting and was applied to mouse naïve B cells in the spleen, as well as activated B cells and plasma cells. BACH1 was present in naïve B cells at approximately half the levels of BACH2. In activated B cells, BACH1 decreased compared to naïve B cells, whilst BACH2 increased. In plasma cells, BACH1 increased back to the same extent as in naïve B cells, whilst BACH2 was not detected. Their target genes, Prdm1 and Hmox1, were highly induced in plasma cells. BACH1 was found to undergo degradation with lower concentrations of heme than BACH2. Therefore, BACH1 and BACH2 are similarly abundant in B cells but differ in heme sensitivity, potentially regulating gene expression differently depending on their heme responsiveness.
BACH1 inhibits senescence, obesity, and short lifespan by ferroptotic FGF21 secretion. International-journal Peer-reviewed

Hironari Nishizawa, Mitsuyo Matsumoto, Mie Yamanaka, Riko Irikura, Kazuma Nakajima, Keisuke Tada, Yoshiaki Nakayama, Morichika Konishi, Nobuyuki Itoh, Ryo Funayama, Keiko Nakayama, Kazuhiko Igarashi

Cell reports　43　(7)　114403-114403　2024/06/27

DOI： 10.1016/j.celrep.2024.114403 　

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Ferroptosis is a type of regulated cell death characterized by iron-dependent lipid peroxidation. A model cell system is constructed to induce ferroptosis by re-expressing the transcription factor BACH1, a potent ferroptosis inducer, in immortalized mouse embryonic fibroblasts (iMEFs). The transfer of the culture supernatant from ferroptotic iMEFs activates the proliferation of hepatoma cells and other fibroblasts and suppresses cellular senescence-like features. The BACH1-dependent secretion of the longevity factor FGF21 is increased in ferroptotic iMEFs. The anti-senescent effects of the culture supernatant from these iMEFs are abrogated by Fgf21 knockout. BACH1 activates the transcription of Fgf21 by promoting ferroptotic stress and increases FGF21 protein expression by suppressing its autophagic degradation through transcriptional Sqstm1 and Lamp2 repression. The BACH1-induced ferroptotic FGF21 secretion suppresses obesity in high-fat diet-fed mice and the short lifespan of progeria mice. The inhibition of these aging-related phenotypes can be physiologically significant regarding ferroptosis.
TANK Binding Kinase 1 Promotes BACH1 Degradation through Both Phosphorylation-Dependent and -Independent Mechanisms without Relying on Heme and FBXO22. International-journal Peer-reviewed

Liang Liu, Mitsuyo Matsumoto, Miki Watanabe-Matsui, Tadashi Nakagawa, Yuko Nagasawa, Jingyao Pang, Bert K K Callens, Akihiko Muto, Kyoko Ochiai, Hirotaka Takekawa, Mahabub Alam, Hironari Nishizawa, Mikako Shirouzu, Hiroki Shima, Keiko Nakayama, Kazuhiko Igarashi

International journal of molecular sciences　25　(8)　2024/04/09

DOI： 10.3390/ijms25084141 　

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BTB and CNC homology 1 (BACH1) represses the expression of genes involved in the metabolism of iron, heme and reactive oxygen species. While BACH1 is rapidly degraded when it is bound to heme, it remains unclear how BACH1 degradation is regulated under other conditions. We found that FBXO22, a ubiquitin ligase previously reported to promote BACH1 degradation, polyubiquitinated BACH1 only in the presence of heme in a highly purified reconstitution assay. In parallel to this regulatory mechanism, TANK binding kinase 1 (TBK1), a protein kinase that activates innate immune response and regulates iron metabolism via ferritinophagy, was found to promote BACH1 degradation when overexpressed in 293T cells. While TBK1 phosphorylated BACH1 at multiple serine and threonine residues, BACH1 degradation was observed with not only the wild-type TBK1 but also catalytically impaired TBK1. The BACH1 degradation in response to catalytically impaired TBK1 was not dependent on FBXO22 but involved both autophagy-lysosome and ubiquitin-proteasome pathways judging from its suppression by using inhibitors of lysosome and proteasome. Chemical inhibition of TBK1 in hepatoma Hepa1 cells showed that TBK1 was not required for the heme-induced BACH1 degradation. Its inhibition in Namalwa B lymphoma cells increased endogenous BACH1 protein. These results suggest that TBK1 promotes BACH1 degradation in parallel to the FBXO22- and heme-dependent pathway, placing BACH1 as a downstream effector of TBK1 in iron metabolism or innate immune response.
Ferroptosis model system by the re-expression of BACH1. International-journal Peer-reviewed

Riko Irikura, Hironari Nishizawa, Kazuma Nakajima, Mie Yamanaka, Guan Chen, Kozo Tanaka, Masafumi Onodera, Mitsuyo Matsumoto, Kazuhiko Igarashi

Journal of biochemistry　2023/04/24

DOI： 10.1093/jb/mvad036 　

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Ferroptosis is a regulated cell death induced by iron-dependent lipid peroxidation. The heme-responsive transcription factor BTB and CNC homology 1 (BACH1) promotes ferroptosis by repressing the transcription of genes involved in glutathione (GSH) synthesis and intracellular labile iron metabolism, which are key regulatory pathways in ferroptosis. We found that BACH1 re-expression in Bach1-/- immortalized mouse embryonic fibroblasts (iMEFs) can induce ferroptosis upon 2-mercaptoethanol removal, without any ferroptosis inducers. In these iMEFs, GSH synthesis was reduced, and intracellular labile iron levels were increased upon BACH1 re-expression. We used this system to investigate whether the major ferroptosis regulators glutathione peroxidase 4 (Gpx4) and apoptosis-inducing factor mitochondria-associated 2 (Aifm2), the gene for ferroptosis suppressor protein 1, are target genes of BACH1. Neither Gpx4 nor Aifm2 was regulated by BACH1 in the iMEFs. However, we found that BACH1 represses AIFM2 transcription in human pancreatic cancer cells. These results suggest that the ferroptosis regulators targeted by BACH1 may vary across different cell types and animal species. Furthermore, we confirmed that the ferroptosis induced by BACH1 re-expression exhibited a propagating effect. BACH1 re-expression represents a new strategy for inducing ferroptosis after GPX4 or system Xc- suppression, and is expected to contribute to future ferroptosis research.
Supplementary Figure S7 from BACH1 Promotes Pancreatic Cancer Metastasis by Repressing Epithelial Genes and Enhancing Epithelial–Mesenchymal Transition

Masaki Sato, Mitsuyo Matsumoto, Yuriko Saiki, Mahabub Alam, Hironari Nishizawa, Masahiro Rokugo, Andrey Brydun, Shinji Yamada, Mika K. Kaneko, Ryo Funayama, Mamoru Ito, Yukinari Kato, Keiko Nakayama, Michiaki Unno, Kazuhiko Igarashi

2023/03/31

DOI： 10.1158/0008-5472.22425189.v1 　
Supplementary Data from BACH1 Promotes Pancreatic Cancer Metastasis by Repressing Epithelial Genes and Enhancing Epithelial–Mesenchymal Transition

Masaki Sato, Mitsuyo Matsumoto, Yuriko Saiki, Mahabub Alam, Hironari Nishizawa, Masahiro Rokugo, Andrey Brydun, Shinji Yamada, Mika K. Kaneko, Ryo Funayama, Mamoru Ito, Yukinari Kato, Keiko Nakayama, Michiaki Unno, Kazuhiko Igarashi

2023/03/31

DOI： 10.1158/0008-5472.22425213.v1 　
Supplementary Figure S2 from BACH1 Promotes Pancreatic Cancer Metastasis by Repressing Epithelial Genes and Enhancing Epithelial–Mesenchymal Transition

Masaki Sato, Mitsuyo Matsumoto, Yuriko Saiki, Mahabub Alam, Hironari Nishizawa, Masahiro Rokugo, Andrey Brydun, Shinji Yamada, Mika K. Kaneko, Ryo Funayama, Mamoru Ito, Yukinari Kato, Keiko Nakayama, Michiaki Unno, Kazuhiko Igarashi

2023/03/31

DOI： 10.1158/0008-5472.22425207.v1 　
Supplementary Table S1-6 from BACH1 Promotes Pancreatic Cancer Metastasis by Repressing Epithelial Genes and Enhancing Epithelial–Mesenchymal Transition

Masaki Sato, Mitsuyo Matsumoto, Yuriko Saiki, Mahabub Alam, Hironari Nishizawa, Masahiro Rokugo, Andrey Brydun, Shinji Yamada, Mika K. Kaneko, Ryo Funayama, Mamoru Ito, Yukinari Kato, Keiko Nakayama, Michiaki Unno, Kazuhiko Igarashi

2023/03/31

DOI： 10.1158/0008-5472.22425186 　
Supplementary Data from BACH1 Promotes Pancreatic Cancer Metastasis by Repressing Epithelial Genes and Enhancing Epithelial–Mesenchymal Transition

Masaki Sato, Mitsuyo Matsumoto, Yuriko Saiki, Mahabub Alam, Hironari Nishizawa, Masahiro Rokugo, Andrey Brydun, Shinji Yamada, Mika K. Kaneko, Ryo Funayama, Mamoru Ito, Yukinari Kato, Keiko Nakayama, Michiaki Unno, Kazuhiko Igarashi

2023/03/31

DOI： 10.1158/0008-5472.22425213 　
Data from BACH1 Promotes Pancreatic Cancer Metastasis by Repressing Epithelial Genes and Enhancing Epithelial–Mesenchymal Transition

Masaki Sato, Mitsuyo Matsumoto, Yuriko Saiki, Mahabub Alam, Hironari Nishizawa, Masahiro Rokugo, Andrey Brydun, Shinji Yamada, Mika K. Kaneko, Ryo Funayama, Mamoru Ito, Yukinari Kato, Keiko Nakayama, Michiaki Unno, Kazuhiko Igarashi

2023/03/31

DOI： 10.1158/0008-5472.c.6511968 　
Data from BACH1 Promotes Pancreatic Cancer Metastasis by Repressing Epithelial Genes and Enhancing Epithelial–Mesenchymal Transition

Masaki Sato, Mitsuyo Matsumoto, Yuriko Saiki, Mahabub Alam, Hironari Nishizawa, Masahiro Rokugo, Andrey Brydun, Shinji Yamada, Mika K. Kaneko, Ryo Funayama, Mamoru Ito, Yukinari Kato, Keiko Nakayama, Michiaki Unno, Kazuhiko Igarashi

2023/03/31

DOI： 10.1158/0008-5472.c.6511968.v1 　
Heme-dependent induction of mitophagy program during differentiation of murine erythroid cells. International-journal Peer-reviewed

Masatoshi Ikeda, Hiroki Kato, Hiroki Shima, Mitsuyo Matsumoto, Eijiro Furukawa, Yan Yan, Ruiqi Liao, Jian Xu, Akihiko Muto, Tohru Fujiwara, Hideo Harigae, Emery H Bresnick, Kazuhiko Igarashi

Experimental hematology　118　21-30　2022/12/05

DOI： 10.1016/j.exphem.2022.11.007 　

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Although establishment and maintenance of mitochondria are essential for the production of massive amounts of heme in erythroblasts, mitochondria must be degraded upon terminal differentiation to red blood cells (RBCs), thus creating a biphasic regulatory process. Previously, we reported that iron deficiency in mice promotes mitochondrial retention in RBCs, suggesting that a proper amount of iron and/or heme is necessary for the degradation of mitochondria during erythroblast maturation. Because the transcription factor GATA1 regulates autophagy in erythroid cells, which involves mitochondrial clearance (mitophagy), we investigated the relationship between iron or heme and mitophagy by analyzing the expression of genes related to GATA1 and autophagy and the impact of iron or heme restriction on the amount of mitochondria. We found that heme promotes the expression of GATA1-regulated mitophagy-related genes and the induction of mitophagy. GATA1 might induce the expression of the autophagy-related genes Atg4d and Stk11 for mitophagy through a heme-dependent mechanism in murine erythroleukemia (MEL) cells and a genetic rescue system with G1E-ER-GATA1 erythroblast cells derived from Gata1-null murine embryonic stem cells. These results provide evidence for a biphasic mechanism in which mitochondria are essential for heme generation, and the heme generated during differentiation promotes mitophagy and mitochondrial disposal. This mechanism provides a molecular framework for understanding this fundamentally important cell biological process.
Iron in Cancer Progression: Does BACH1 Promote Metastasis by Altering Iron Homeostasis? Peer-reviewed

Kazuhiko Igarashi, Hironari Nishizawa, Mitsuyo Matsumoto

Subcellular Biochemistry　67-80　2022/10/28
Publisher: Springer International Publishing
DOI： 10.1007/978-3-031-07634-3_2 　

ISSN： 0306-0225

eISSN： 2542-8810
Harnessing the Therapeutic Potential of the Nrf2/Bach1 Signaling Pathway in Parkinson's Disease.

Ahuja M, Kaidery NA, Dutta D, Attucks OC, Kazakov EH, Gazaryan I, Matsumoto M, Igarashi K, Sharma SM, Bobby Thomas

Antioxidants (Basel, Switzerland)　2022/09/09

DOI： 10.3390/antiox11091780 　

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Parkinson's disease (PD) is the second most common neurodegenerative movement disorder characterized by a progressive loss of dopaminergic neurons in the substantia nigra pars compacta. Although a complex interplay of multiple environmental and genetic factors has been implicated, the etiology of neuronal death in PD remains unresolved. Various mechanisms of neuronal degeneration in PD have been proposed, including oxidative stress, mitochondrial dysfunction, neuroinflammation, α-synuclein proteostasis, disruption of calcium homeostasis, and other cell death pathways. While many drugs individually targeting these pathways have shown promise in preclinical PD models, this promise has not yet translated into neuroprotective therapies in human PD. This has consequently spurred efforts to identify alternative targets with multipronged therapeutic approaches. A promising therapeutic target that could modulate multiple etiological pathways involves drug-induced activation of a coordinated genetic program regulated by the transcription factor, nuclear factor E2-related factor 2 (Nrf2). Nrf2 regulates the transcription of over 250 genes, creating a multifaceted network that integrates cellular activities by expressing cytoprotective genes, promoting the resolution of inflammation, restoring redox and protein homeostasis, stimulating energy metabolism, and facilitating repair. However, FDA-approved electrophilic Nrf2 activators cause irreversible alkylation of cysteine residues in various cellular proteins resulting in side effects. We propose that the transcriptional repressor of BTB and CNC homology 1 (Bach1), which antagonizes Nrf2, could serve as a promising complementary target for the activation of both Nrf2-dependent and Nrf2-independent neuroprotective pathways. This review presents the current knowledge on the Nrf2/Bach1 signaling pathway, its role in various cellular processes, and the benefits of simultaneously inhibiting Bach1 and stabilizing Nrf2 using non-electrophilic small molecules as a novel therapeutic approach for PD.
BACH1 Expression Is Promoted by Tank Binding Kinase 1 (TBK1) in Pancreatic Cancer Cells to Increase Iron and Reduce the Expression of E-Cadherin. International-journal Peer-reviewed

Liang Liu, Mitsuyo Matsumoto, Miki Matsui-Watanabe, Kyoko Ochiai, Bert K K Callens, Long Chi Nguyen, Yushi Kozuki, Miho Tanaka, Hironari Nishizawa, Kazuhiko Igarashi

Antioxidants (Basel, Switzerland)　11　(8)　2022/07/27

DOI： 10.3390/antiox11081460 　

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BTB and CNC homology 1 (BACH1) represses the expression of genes involved in the metabolism of iron, heme and reactive oxygen species and promotes metastasis of various cancers including pancreatic ductal adenocarcinoma (PDAC). However, it is not clear how BACH1 is regulated in PDAC cells. Knockdown of Tank binding kinase 1 (TBK1) led to reductions of BACH1 mRNA and protein amounts in AsPC-1 human PDAC cells. Gene expression analysis of PDAC cells with knockdown of TBK1 or BACH1 suggested the involvement of TBK1 and BACH1 in the regulation of iron homeostasis. Ferritin mRNA and proteins were both increased upon BACH1 knockdown in AsPC-1 cells. Flow cytometry analysis showed that AsPC-1 cells with BACH1 knockout or knockdown contained lower labile iron than control cells, suggesting that BACH1 increased labile iron by repressing the expression of ferritin genes. We further found that the expression of E-cadherin was upregulated upon the chelation of intracellular iron content. These results suggest that the TBK1-BACH1 pathway promotes cancer cell metastasis by increasing labile iron within cells.
mTORC1-independent translation control in mammalian cells by methionine adenosyltransferase 2A and S-adenosylmethionine. International-journal Peer-reviewed

Mahabub Alam, Hiroki Shima, Yoshitaka Matsuo, Nguyen Chi Long, Mitsuyo Matsumoto, Yusho Ishii, Nichika Sato, Takato Sugiyama, Risa Nobuta, Satoshi Hashimoto, Liang Liu, Mika K Kaneko, Yukinari Kato, Toshifumi Inada, Kazuhiko Igarashi

The Journal of biological chemistry　298　(7)　102084-102084　2022/05/27

DOI： 10.1016/j.jbc.2022.102084 　

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Methionine adenosyltransferase (MAT) catalyzes the synthesis of S-adenosylmethionine (SAM). As the sole methyl-donor for methylation of DNA, RNA, and proteins, SAM levels affect gene expression by changing methylation patterns. Expression of MAT2A, the catalytic subunit of isozyme MAT2, is positively correlated with proliferation of cancer cells; however, how MAT2A promotes cell proliferation is largely unknown. Given that the protein synthesis is induced in proliferating cells and that RNA and protein components of translation machinery are methylated, we tested here whether MAT2 and SAM are coupled with protein synthesis. By measuring ongoing protein translation via puromycin labeling, we revealed that MAT2A depletion or chemical inhibition reduced protein synthesis in HeLa and Hepa1 cells. Furthermore, overexpression of MAT2A enhanced protein synthesis, indicating that SAM is limiting under normal culture conditions. In addition, MAT2 inhibition did not accompany reduction in mechanistic target of rapamycin complex 1 activity but nevertheless reduced polysome formation. Polysome-bound RNA sequencing revealed that MAT2 inhibition decreased translation efficiency of some fraction of mRNAs. MAT2A was also found to interact with the proteins involved in rRNA processing and ribosome biogenesis; depletion or inhibition of MAT2 reduced 18S rRNA processing. Finally, quantitative mass spectrometry revealed that some translation factors were dynamically methylated in response to the activity of MAT2A. These observations suggest that cells possess an mTOR-independent regulatory mechanism that tunes translation in response to the levels of SAM. Such a system may acclimate cells for survival when SAM synthesis is reduced, whereas it may support proliferation when SAM is sufficient.
Bach1 derepression is neuroprotective in a mouse model of Parkinson's disease. International-journal Peer-reviewed

Manuj Ahuja, Navneet Ammal Kaidery, Otis C Attucks, Erin McDade, Dmitry M Hushpulian, Arsen Gaisin, Irina Gaisina, Young Hoon Ahn, Sergey Nikulin, Andrey Poloznikov, Irina Gazaryan, Masayuki Yamamoto, Mitsuyo Matsumoto, Kazuhiko Igarashi, Sudarshana M Sharma, Bobby Thomas

Proceedings of the National Academy of Sciences of the United States of America　118　(45)　2021/11/09

DOI： 10.1073/pnas.2111643118 　

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Parkinson's disease (PD) is a progressive neurodegenerative movement disorder characterized by the loss of nigrostriatal dopaminergic neurons. Mounting evidence suggests that Nrf2 is a promising target for neuroprotective interventions in PD. However, electrophilic chemical properties of the canonical Nrf2-based drugs cause irreversible alkylation of cysteine residues on cellular proteins resulting in side effects. Bach1 is a known transcriptional repressor of the Nrf2 pathway. We report that Bach1 levels are up-regulated in PD postmortem brains and preclinical models. Bach1 knockout (KO) mice were protected against 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP)-induced dopaminergic neurotoxicity and associated oxidative damage and neuroinflammation. Functional genomic analysis demonstrated that the neuroprotective effects in Bach1 KO mice was due to up-regulation of Bach1-targeted pathways that are associated with both Nrf2-dependent antioxidant response element (ARE) and Nrf2-independent non-ARE genes. Using a proprietary translational technology platform, a drug library screen identified a substituted benzimidazole as a Bach1 inhibitor that was validated as a nonelectrophile. Oral administration of the Bach1 inhibitor attenuated MPTP neurotoxicity in pre- and posttreatment paradigms. Bach1 inhibitor-induced neuroprotection was associated with the up-regulation of Bach1-targeted pathways in concurrence with the results from Bach1 KO mice. Our results suggest that genetic deletion as well as pharmacologic inhibition of Bach1 by a nonelectrophilic inhibitor is a promising therapeutic approach for PD.
Lipid peroxidation and the subsequent cell death transmitting from ferroptotic cells to neighboring cells. International-journal Peer-reviewed

Hironari Nishizawa, Mitsuyo Matsumoto, Guan Chen, Yusho Ishii, Keisuke Tada, Masafumi Onodera, Hiroki Kato, Akihiko Muto, Kozo Tanaka, Kazuhiko Igarashi

Cell death & disease　12　(4)　332-332　2021/03/29

DOI： 10.1038/s41419-021-03613-y 　

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Ferroptosis regulated cell death due to the iron-dependent accumulation of lipid peroxide. Ferroptosis is known to constitute the pathology of ischemic diseases, neurodegenerative diseases, and steatohepatitis and also works as a suppressing mechanism against cancer. However, how ferroptotic cells affect surrounding cells remains elusive. We herein report the transfer phenomenon of lipid peroxidation and cell death from ferroptotic cells to nearby cells that are not exposed to ferroptotic inducers (FINs). While primary mouse embryonic fibroblasts (MEFs) and NIH3T3 cells contained senescence-associated β-galactosidase (SA-β-gal)-positive cells, they were decreased upon induction of ferroptosis with FINs. The SA-β-gal decrease was inhibited by ferroptotic inhibitors and knockdown of Atg7, pointing to the involvement of lipid peroxidation and activated autophagosome formation during ferroptosis. A transfer of cell culture medium of cells treated with FINs, type 1 or 2, caused the reduction in SA-β-gal-positive cells in recipient cells that had not been exposed to FINs. Real-time imaging of Kusabira Orange-marked reporter MEFs cocultured with ferroptotic cells showed the generation of lipid peroxide and deaths of the reporter cells. These results indicate that lipid peroxidation and its aftereffects propagate from ferroptotic cells to surrounding cells, even when the surrounding cells are not exposed to FINs. Ferroptotic cells are not merely dying cells but also work as signal transmitters inducing a chain of further ferroptosis.
Chromatin Protein PC4 Orchestrates B Cell Differentiation by Collaborating with IKAROS and IRF4. International-journal Peer-reviewed

Kyoko Ochiai, Mari Yamaoka, Amrutha Swaminathan, Hiroki Shima, Hitoshi Hiura, Mitsuyo Matsumoto, Daisuke Kurotaki, Jun Nakabayashi, Ryo Funayama, Keiko Nakayama, Takahiro Arima, Tomokatsu Ikawa, Tomohiko Tamura, Roger Sciammas, Philippe Bouvet, Tapas K Kundu, Kazuhiko Igarashi

Cell reports　33　(12)　108517-108517　2020/12/22

DOI： 10.1016/j.celrep.2020.108517 　

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The chromatin protein positive coactivator 4 (PC4) has multiple functions, including chromatin compaction. However, its role in immune cells is largely unknown. We show that PC4 orchestrates chromatin structure and gene expression in mature B cells. B-cell-specific PC4-deficient mice show impaired production of antibody upon antigen stimulation. The PC4 complex purified from B cells contains the transcription factors (TFs) IKAROS and IRF4. IKAROS protein is reduced in PC4-deficient mature B cells, resulting in de-repression of their target genes in part by diminished interactions with gene-silencing components. Upon activation, the amount of IRF4 protein is not increased in PC4-deficient B cells, resulting in reduction of plasma cells. Importantly, IRF4 reciprocally induces PC4 expression via a super-enhancer. PC4 knockdown in human B cell lymphoma and myeloma cells reduces IKAROS protein as an anticancer drug, lenalidomide. Our findings establish PC4 as a chromatin regulator of B cells and a possible therapeutic target adjoining IKAROS in B cell malignancies.
Longitudinal plasma amino acid profiling with maternal genomic background throughout human pregnancy Peer-reviewed

Matsuyuki Shirota, Daisuke Saigusa, Riu Yamashita, Yasutake Kato, Mitsuyo Matsumoto, Junya Yamagishi, Noriko Ishida, Kazuki Kumada, Yuji Oe, Hisaaki Kudo, Junji Yokozawa, Yoko Kuroki, Ikuko Motoike, Fumiki Katsuoka, Masao Nagasaki, Seizo Koshiba, Keiko Nakayama, Osamu Tanabe, Jun Yasuda, Shigeo Kure, Kengo Kinoshita, Hirohito Metoki, Shinichi Kuriyama, Nobuo Yaegashi, Masayuki Yamamoto, Junichi Sugawara

Medical Mass Spectrometry　4　(1)　36-49　2020/06
Infection perturbs Bach2- and Bach1-dependent erythroid lineage 'choice' to cause anemia. International-journal Peer-reviewed

Hiroki Kato, Ari Itoh-Nakadai, Mitsuyo Matsumoto, Yusho Ishii, Miki Watanabe-Matsui, Masatoshi Ikeda, Risa Ebina-Shibuya, Yuki Sato, Masahiro Kobayashi, Hironari Nishizawa, Katsushi Suzuki, Akihiko Muto, Tohru Fujiwara, Yasuhito Nannya, Luca Malcovati, Mario Cazzola, Seishi Ogawa, Hideo Harigae, Kazuhiko Igarashi

Nature immunology　19　(10)　1059-1070　2018/10

DOI： 10.1038/s41590-018-0202-3 　

ISSN： 1529-2908

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Elucidation of how the differentiation of hematopoietic stem and progenitor cells (HSPCs) is reconfigured in response to the environment is critical for understanding the biology and disorder of hematopoiesis. Here we found that the transcription factors (TFs) Bach2 and Bach1 promoted erythropoiesis by regulating heme metabolism in committed erythroid cells to sustain erythroblast maturation and by reinforcing erythroid commitment at the erythro-myeloid bifurcation step. Bach TFs repressed expression of the gene encoding the transcription factor C/EBPβ, as well as that of its target genes encoding molecules important for myelopoiesis and inflammation; they achieved the latter by binding to their regulatory regions also bound by C/EBPβ. Lipopolysaccharide diminished the expression of Bach TFs in progenitor cells and promoted myeloid differentiation. Overexpression of Bach2 in HSPCs promoted erythroid development and inhibited myelopoiesis. Knockdown of BACH1 or BACH2 in human CD34+ HSPCs impaired erythroid differentiation in vitro. Thus, Bach TFs accelerate erythroid commitment by suppressing the myeloid program at steady state. Anemia of inflammation and myelodysplastic syndrome might involve reduced activity of Bach TFs.
Correction: Distinct requirements for energy metabolism in mouse primordial germ cells and their reprogramming to embryonic germ cells (Proceedings of the National Academy of Sciences of the United States of America (2017) 114 (8289-8294) DOI: 10.1073/pna

Hayashi Y, Otsuka K, Ebina M, Igarashi K, Takehara A, Matsumoto M, Kanai A, Igarashi K, Soga T, Matsui Y

Proceedings of the National Academy of Sciences of the United States of America　115　(30)　2018/07/24
Publisher: Proceedings of the National Academy of Sciences of the United States of America
DOI： 10.1073/pnas.1811451115 　

ISSN： 0027-8424

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© 2018 National Academy of Sciences. All rights reserved. Correction to Supporting Information for “Distinct requirements for energy metabolism in mouse primordial germ cells and their reprogramming to embryonic germ cells,” by Yohei Hayashi, Kei Otsuka, Masayuki Ebina, Kaori Igarashi, Asuka Takehara, Mitsuyo Matsumoto, Akio Kanai, Kazuhiko Igarashi, Tomoyoshi Soga, and Yasuhisa Matsui, which was first published July 17, 2017; 10.1073/pnas.1620915114 (Proc Natl Acad Sci USA 114: 8289–8294). The authors note that, in the SI Appendix, the units "fmol/mm3" in the Fig. S2 legend, Fig. S4, Fig. S5, and Dataset S1 should have instead appeared as "nmol/mm3." The authors also note that in Fig. S4A, row 3, column 2, the tick marks along the vertical axis appeared incorrectly. The SI Appendix has been corrected online.
Bach2 promotes B cell receptor–induced proliferation of b lymphocytes and represses cyclin-dependent kinase inhibitors Peer-reviewed

Yuichi Miura, Mizuho Morooka, Nicolas Sax, Rahul Roychoudhuri, Ari Itoh-Nakadai, Andrey Brydun, Ryo Funayama, Keiko Nakayama, Susumu Satomi, Mitsuyo Matsumoto, Kazuhiko Igarashi, Akihiko Muto

Journal of Immunology　200　(8)　2882-2893　2018/04/15
Publisher: American Association of Immunologists
DOI： 10.4049/jimmunol.1601863 　

ISSN： 1550-6606 0022-1767
Phosphorylation of BACH1 switches its function from transcription factor to mitotic chromosome regulator and promotes its interaction with HMMR. International-journal Peer-reviewed

Jie Li, Hiroki Shima, Hironari Nishizawa, Masatoshi Ikeda, Andrey Brydun, Mitsuyo Matsumoto, Hiroki Kato, Yuriko Saiki, Liang Liu, Miki Watanabe-Matsui, Kenji Iemura, Kozo Tanaka, Takuma Shiraki, Kazuhiko Igarashi

The Biochemical journal　475　(5)　981-1002　2018/03/15
Publisher: Portland Press Ltd
DOI： 10.1042/BCJ20170520 　

ISSN： 1470-8728 0264-6021
The mTOR-Bach2 Cascade Controls Cell Cycle and Class Switch Recombination during B Cell Differentiation Peer-reviewed

Toru Tamahara, Kyoko Ochiai, Akihiko Muto, Yukinari Kato, Nicolas Sax, Mitsuyo Matsumoto, Takeyoshi Koseki, Kazuhiko Igarashi

MOLECULAR AND CELLULAR BIOLOGY　37　(24)　2017/12

DOI： 10.1128/MCB.00418-17 　

ISSN： 0270-7306

eISSN： 1098-5549
S-Adenosylmethionine Synthesis Is Regulated by Selective N-6-Adenosine Methylation and mRNA Degradation Involving METTL16 and YTHDC1 Peer-reviewed

Hiroki Shima, Mitsuyo Matsumoto, Yuma Ishigami, Masayuki Ebina, Akihiko Muto, Yuho Sato, Sayaka Kumagai, Kyoko Ochiai, Tsutomu Suzuki, Kazuhiko Igarashi

CELL REPORTS　21　(12)　3354-3363　2017/12

DOI： 10.1016/j.celrep.2017.11.092 　

ISSN： 2211-1247
Inflammatory responses induce an identity crisis of alveolar macrophages, leading to pulmonary alveolar proteinosis Peer-reviewed

Risa Ebina-Shibuya, Mitsuyo Matsumoto, Makoto Kuwahara, Kyoung-Jin Jang, Manabu Sugai, Yoshiaki Ito, Ryo Funayama, Keiko Nakayama, Yuki Sato, Naoto Ishii, Yasunobu Okamura, Kengo Kinoshita, Kohei Kometani, Tomohiro Kurosaki, Akihiko Muto, Masakazu Ichinose, Masakatsu Yamashita, Kazuhiko Igarashi

JOURNAL OF BIOLOGICAL CHEMISTRY　292　(44)　18098-18112　2017/11

DOI： 10.1074/jbc.M117.808535 　

ISSN： 0021-9258

eISSN： 1083-351X
Reductions in the mitochondrial ABC transporter Abcb10 affect the transcriptional profile of heme biosynthesis genes. International-journal Peer-reviewed

Alexandra Seguin, Naoko Takahashi-Makise, Yvette Y Yien, Nicholas C Huston, Jared C Whitman, Gabriel Musso, Jared A Wallace, Thomas Bradley, Hector A Bergonia, Martin D Kafina, Mitsuyo Matsumoto, Kazuhiko Igarashi, John D Phillips, Barry H Paw, Jerry Kaplan, Diane M Ward

The Journal of biological chemistry　292　(39)　16284-16299　2017/09/29

DOI： 10.1074/jbc.M117.797415 　

ISSN： 0021-9258

eISSN： 1083-351X
Distinct requirements for energy metabolism in mouse primordial germ cells and their reprogramming to embryonic germ cells Peer-reviewed

Yohei Hayashi, Kei Otsuka, Masayuki Ebina, Kaori Igarashi, Asuka Takehara, Mitsuyo Matsumoto, Akio Kanai, Kazuhiko Igarashi, Tomoyoshi Soga, Yasuhisa Matsui

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA　114　(31)　8289-8294　2017/08

DOI： 10.1073/pnas.1620915114 　

ISSN： 0027-8424
A Bach2-Cebp Gene Regulatory Network for the Commitment of Multipotent Hematopoietic Progenitors Peer-reviewed

Ari Itoh-Nakadai, Mitsuyo Matsumoto, Hiroki Kato, Junichi Sasaki, Yukihiro Uehara, Yuki Sato, Risa Ebina-Shibuya, Mizuho Morooka, Ryo Funayama, Keiko Nakayama, Kyoko Ochiai, Akihiko Muto, Kazuhiko Igarashi

CELL REPORTS　18　(10)　2401-2414　2017/03

DOI： 10.1016/j.celrep.2017.02.029 　

ISSN： 2211-1247
The double knockout of Bach1 and Bach2 in mice reveals shared compensatory mechanisms in regulating alveolar macrophage function and lung surfactant homeostasis. International-journal Peer-reviewed

Risa Ebina-Shibuya, Miki Watanabe-Matsui, Mitsuyo Matsumoto, Ari Itoh-Nakadai, Ryo Funayama, Keiko Nakayama, Akihiko Muto, Kazuhiko Igarashi

Journal of biochemistry　160　(6)　333-344　2016/12

DOI： 10.1093/jb/mvw041 　

ISSN： 0021-924X

eISSN： 1756-2651
Genetic heterogeneity in 26 infants with a hypomyelinating leukodystrophy Peer-reviewed

Natsuko Arai-Ichinoi, Mitsugu Uematsu, Ryo Sato, Tasuku Suzuki, Hiroki Kudo, Atsuo Kikuchi, Naomi Hino-Fukuyo, Mitsuyo Matsumoto, Kazuhiko Igarashi, Kazuhiro Haginoya, Shigeo Kure

HUMAN GENETICS　135　(1)　89-98　2016/01

DOI： 10.1007/s00439-015-1617-7 　

ISSN： 0340-6717

eISSN： 1432-1203
The artificial loss of Runx1 reduces the expression of quiescence-associated transcription factors in CD4(+) T lymphocytes Peer-reviewed

Won Fen Wong, Kazuyoshi Kohu, Takeshi Nagashima, Ryo Funayama, Mitsuyo Matsumoto, Elaheh Movahed, Grace Min Yi Tan, Tee Cian Yeow, Chung Yeng Looi, Mineo Kurokawa, Motomi Osato, Kazuhiko Igarashi, Keiko Nakayama, Masanobu Satake

MOLECULAR IMMUNOLOGY　68　(2)　223-233　2015/12

DOI： 10.1016/j.molimm.2015.08.012 　

ISSN： 0161-5890
多層的オミックス解析による肝再生分子メカニズムの解明

佐藤好宏, 加藤恭丈, 松本光代, 蝦名真行, 海野倫明, 五十嵐和彦

Organ Biology　22　(3)　74-74　2015/10
Publisher: (一社)日本臓器保存生物医学会
ISSN： 1340-5152

eISSN： 2188-0204
Methionine Adenosyltransferase II-dependent Histone H3K9 Methylation at the COX-2 Gene Locus Peer-reviewed

Yohei Kera, Yasutake Katoh, Mineto Ohta, Mitsuyo Matsumoto, Teruko Takano-Yamamoto, Kazuhiko Igarashi

JOURNAL OF BIOLOGICAL CHEMISTRY　288　(19)　13592-13601　2013/05

DOI： 10.1074/jbc.M112.429738 　

ISSN： 0021-9258

eISSN： 1083-351X
Individual transcriptional activity of estrogen receptors in primary breast cancer and its clinical significance Peer-reviewed

Tatsuyuki Gohno, Yuko Seino, Toru Hanamura, Toshifumi Niwa, Mitsuyo Matsumoto, Nobuo Yaegashi, Hanako Oba, Masafumi Kurosumi, Hiroyuki Takei, Yuri Yamaguchi, Shin-ichi Hayashi

CANCER MEDICINE　1　(3)　328-337　2012/12

DOI： 10.1002/cam4.41 　

ISSN： 2045-7634
3-Dimensional Microarray Analysis of Estrogen Signal-related Genes in Breast Cancer Tissues Peer-reviewed

Mitsuyo Matsumoto, Hiroko Sakamoto, Yuri Yamaguchi, Yuko Seino, Hiroyuki Takei, Masafumi Kurosumi, Hironobu Sasano, Nobuo Yaegashi, Shin-Ichi Hayashi

ANTICANCER RESEARCH　29　(10)　3971-3975　2009/10

ISSN： 0250-7005
Local biosynthesis of estrogen in human endometrial carcinoma through tumor-stromal cell interactions. Peer-reviewed

Takahashi-Shiga N, Utsunomiya H, Miki Y, Nagase S, Kobayashi R, Matsumoto M, Niikura H, Ito K, Yaegashi N

Clinical cancer research : an official journal of the American Association for Cancer Research　15　(19)　6028-6034　2009/10

DOI： 10.1158/1078-0432.CCR-09-1013 　

ISSN： 1078-0432
Midkine and its clinical significance in endometrial carcinoma Peer-reviewed

Kojiro Tanabe, Mitsuyo Matsumoto, Shinya Ikematsu, Satoru Nagase, Atsushi Hatakeyama, Tadao Takano, Hitoshi Niikura, Kiyoshi Ito, Kenji Kadomatsu, Shin-ichi Hayashi, Nobuo Yaegashi

CANCER SCIENCE　99　(6)　1125-1130　2008/06

DOI： 10.1111/j.1349-7006.2008.00796.x 　

ISSN： 1347-9032
Aromatase localization in human endometrial carcinoma: The potential effects of arcinoma-stromal cell Interactions

N. Takahashi, H. Utsunomiya, R. Kobayashi, M. Matsumoto, K. Yoshinaga, S. Nagase, T. Takano, H. Niikura, K. Ito, N. Yaegashi

JOURNAL OF CLINICAL ONCOLOGY　26　(15)　2008/05

ISSN： 0732-183X
Expression of retinoic acid receptors in human endometrial carcinoma Peer-reviewed

Kojiro Tanabe, Hiroki Utsunomiya, Mitsutoshi Tamura, Hitoshi Niikura, Tadao Takano, Kohsuke Yoshinaga, Satoru Nagase, Takashi Suzuki, Kiyoshi Ito, Mitsuyo Matsumoto, Shin-ichi Hayashi, Nobuo Yaegashi

CANCER SCIENCE　99　(2)　267-271　2008/02

DOI： 10.1111/j.1349-7006.2007.00684.x 　

ISSN： 1349-7006
Expression of retinoic acid receptors in human endometrial carcinoma Peer-reviewed

Kojiro Tanabe, Hiroki Utsunomiya, Mitsutoshi Tamura, Hitoshi Niikura, Tadao Takano, Kohsuke Yoshinaga, Satoru Nagase, Takashi Suzuki, Kiyoshi Ito, Mitsuyo Matsumoto, Shin-Ichi Hayashi, Nobuo Yaegashi

Cancer Science　99　(2)　267-271　2008/02

DOI： 10.1111/j.1349-7006.2007.00684.x 　

ISSN： 1347-9032 1349-7006
Three-dimensional Microarray for the Prediction of Response to Hormonal Therapy in Breast Cancer Peer-reviewed

Mitsuyo MATSUMOTO, Atsushi HATAKEYAMA, Hiroko SAKAMOTO, Yuri YAMAGUCHI, Hironobu SASANO, Nobuo YAEGASHI, Shin-ichi HAYASHI, Department of Medical Technology School of Health Sciences Tohoku University:Department of Ginecology School of Medicine Tohoku University, Department of Medical Technology School of Health Sciences Tohoku University, Biomedical Business Incubation Division Olympus Co., Research Institute for Clinical Oncology Saitama Cancer Center, Department of Pathology School of Medicine Tohoku University, Department of Ginecology School of Medicine Tohoku University, Department of Medical Technology School of Health Sciences Tohoku University

Bulletin of School of Health Sciences, Tohoku University　16　(1)　19-25　2007
Publisher:
ISSN： 1348-8899
Inhibitory effects of epigallocatechin gallate on the propagation of bovine coronavirus in Madin-Darby bovine kidney cells Peer-reviewed

Mitsuyo Matsumoto, Takao Mukai, Satoru Furukawa, Hitoshi Ohori

Animal Science Journal　76　(5)　507-512　2005/10

DOI： 10.1111/j.1740-0929.2005.00297.x 　

ISSN： 1344-3941
電気分解陽極水による牛コロナウイルスの不活化 Peer-reviewed

松本光代, 大塚美奈, 鈴木祐子, 福井宏行, 町田季衣子, 向井孝夫, 大堀均

日本畜産学会報　76　(1)　59-65　2005
Publisher: (公社)日本畜産学会
DOI： 10.2508/chikusan.76.59 　

ISSN： 1346-907X

eISSN： 1880-8255
Binding of Bifidobacterium bifidum and Lactobacillus reuteri to the carbohydrate moieties of intestinal glycolipids recognized by peanut agglutinin Peer-reviewed

T Mukai, S Kaneko, M Matsumoto, H Ohori

INTERNATIONAL JOURNAL OF FOOD MICROBIOLOGY　90　(3)　357-362　2004/02

DOI： 10.1016/S0168-1605(03)00317-9 　

ISSN： 0168-1605
Inhibition of binding of Helicobacter pylori to the glycolipid receptors by probiotic Lactobacillus reuteri Peer-reviewed

T Mukai, T Asasaka, E Sato, K Mori, M Matsumoto, H Ohori

FEMS IMMUNOLOGY AND MEDICAL MICROBIOLOGY　32　(2)　105-110　2002/01

DOI： 10.1016/S0928-8244(01)00284-X 　

ISSN： 0928-8244

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Misc. 80

がん細胞の多様性と脆弱性をつくる遺伝子制御とその破綻鉄代謝制御系によって編まれる癌の悪性化と脆弱性

松本光代, 中村和樹, 六郷正博

日本生化学会大会プログラム・講演要旨集　98回　2S18a-03　2025/11
Publisher: (公社)日本生化学会
鉄が切り拓く新たな生命科学のフロンティアがん病態におけるBACH1鉄代謝制御サーキットの循環的因果関係

五十嵐和彦, 中村和樹, Jingyao Pang, 柘植駿一, 松本光代

日本生化学会大会プログラム・講演要旨集　98回　2S08e-05　2025/11
Publisher: (公社)日本生化学会
AsPC-1膵がん細胞におけるフェリチン過剰発現による鉄代謝およびフェロトーシス(Responses of iron metabolism and ferroptosis to ferritin overexpression in AsPC-1 pancreatic cancer cells)

Pang Jingyao, 松本光代, 西澤弘成, 秋山拓己, 五十嵐和彦

日本生化学会大会プログラム・講演要旨集　98回　3P-203　2025/11
Publisher: (公社)日本生化学会
Development of Vasohibin-2 targeted Chimeric Artificial Nucleic Acids for suppression of pancreatic cancer malignancy

町田光翼, 稲垣雅仁, 松本光代, 荒木保幸, 佐藤靖史, 和田健彦, 和田健彦

日本化学会春季年会講演予稿集(Web)　105th　2025
Construction and evaluation of cancer cell-selective drug delivery system: Development of highly efficient intracellular transfection systems based on oligoarginine combined with PAD derivatives

石川航大, 加藤ひらり, 荒木保幸, 松本光代, 中瀬生彦, 和田健彦, 和田健彦

日本化学会春季年会講演予稿集(Web)　105th　2025
Development of Chimeric Artificial Nucleic Acids (CANA) with Catalytic Target RNA Cleavage Functions Toward the Pancreatic Cancer Therapeutics: VI: Effects of junction positions and complex stabilities on cleavage efficiencies

木野実音, 五十嵐優希, 稲垣雅仁, 松本光代, 堀内結翔, 荒木保幸, 西嶋政樹, 三瓶悠, 山吉麻子, 五十嵐和彦, 和田健彦, 和田健彦

日本化学会春季年会講演予稿集(Web)　105th　2025
転写因子Bach1による膵癌進展機構の解明

柘植駿一, 島弘希, 松本光代, 濱田晋, 正宗淳, 五十嵐和彦

日本分子生物学会年会プログラム・要旨集(Web)　48th　2025
Intracellular iron metabolism by the transcription factor BACH1 and iron-deficient cell death in head and neck cancer

日本癌学会学術総会抄録集(Web)　83rd　2024
BACH1 and TBK1 synergistically promote epithelial-mesenchymal transition via iron

日本癌学会学術総会抄録集(Web)　83rd　2024
BACH1遺伝子ネットワークによる鉄流通と抗老化フェロトーシスシグナルの制御

五十嵐和彦, 西澤弘成, 中村和樹, 松本光代

日本分子生物学会年会プログラム・要旨集(Web)　47th　2024
Construction and Evaluation of Cancer Cell Selective Drug Delivery System: III: Development pancreatic cancer of a selective drug delivery system to suppress the malignant progression

日本化学会春季年会講演予稿集(Web)　104th　2024
Construction of Chimeric Artificial Nucleic Acids (CANA) toward Pancreatic Cancer Treatments by Inhibition of Transcription Factor BACH1: III: Establishment of Molecular Design Strategy Based on In Vitro Analysis

堀内結翔, 石渡望, 藤田一寿, 西嶋政樹, 三瓶悠, 荒木保幸, 松本光代, 松本光代, 山吉麻子, 五十嵐和彦, 和田健彦

日本化学会春季年会講演予稿集(Web)　104th　2024
細胞内環境応答型新規人工核酸を活用した虚血性疾患選択的薬効発現触媒的核酸医薬法の開発

藤田一寿, 堀内結翔, 松本光代, 稲垣雅仁, 林宏典, 荒木保幸, 西嶋政樹, 児玉栄一, 和田健彦

日本核酸医薬学会誌(Web)　28　(1)　2024
Construction of Chimeric Artificial Nucleic Acids (CANA) toward Pancreatic Cancer Treatments by Inhibition of Transcription Factor BACH 1: IV: Establishment of Molecular Design Strategy Based on In vitro and in vivo Analysis

日本核酸医薬学会年会講演要旨集(CD-ROM)　9th　2024
A Construction of Chimeric Artificial Nucleic Acids (CANA) forward Inhibition of Pancreatic Cancer Transcription Factor BACH1: IV:-Effects of Junction Position on Complex Stability and Cleavage Efficiency-

五十嵐優希, 堀内結翔, 松本光代, 松本光代, 荒木保幸, 西嶋政樹, 三瓶悠, 山吉麻子, 五十嵐和彦, 和田健彦

日本化学会春季年会講演予稿集(Web)　104th　ROMBUNNO.D341-4am-13 (WEB ONLY)　2024
BACH1 promotes metastasis of pancreatic cancer

佐藤正規, 大塚英郎, 水間正道, 松本光代, 斎木由利子, 大沼忍, 中川圭, 亀井尚, 五十嵐和彦, 海野倫明

日本がん転移学会学術集会・総会プログラム抄録集　32nd　2023
Functional analysis of transcription factor NRF3 as a novel tumor growth factor in pancreatic cancer

佐藤克哉, 道原琢登, 山元康平, 佐藤健, 松本光代, 五十嵐和彦, 和久剛, 小林聡

日本分子生物学会年会プログラム・要旨集(Web)　46th　2023
B細胞におけるBACH転写因子のタンパク質量比による転写調節機構の解明

倉澤岳志, 武藤哲彦, 松本光代, 落合恭子, 村山和隆, 五十嵐和彦

日本生化学会大会(Web)　96th　2023
BACH1 promotes epithelial-mesenchymal transition by enhancing cellular labile iron level in pancreatic cancer cell

日本癌学会学術総会抄録集(Web)　81st　P-3144　2022/09
Publisher: (一社)日本癌学会
ISSN： 0546-0476
The avoidance of cell death by BACH1 in head and neck cancer cells

日本分子生物学会年会プログラム・要旨集(Web)　45th　2022
Insights into the mechanism of epithelial-mesenchymal transition regulated by the TBK1-BACH1 axis in pancreatic cancer cell

松本光代, 松本光代, LIU Liang, 田中美帆, 島弘季, 五十嵐和彦, 五十嵐和彦

日本分子生物学会年会プログラム・要旨集(Web)　45th　2022
Regulatory mechanisms of iron metabolism in B cell immune responses by the transcription factor BACH2

日本分子生物学会年会プログラム・要旨集(Web)　45th　2022
メチオニンアデノシルトランスフェラーゼ2Aによる哺乳類細胞のmTORC1非依存的な翻訳制御機構(mTORC1-independent translational regulation of mammalian cells by methionine adenosyltransferase 2A)

Mahabub Alam, Shima Hiroki, Nguyen Long C., Matsumoto Mitsuyo, Sugiyama Takato, Nobuta Risa, Hashimoto Satoshi, Matsuo Yoshitaka, Inada Toshifumi, Igarashi Kazuhiko

日本生化学会大会プログラム・講演要旨集　94回　[2T15a-666)]　2021/11
Publisher: (公社)日本生化学会
ビリベルジン結合型シアノバクテリオクロムを用いたフェロトーシス高感受性細胞の検出

中嶋一真, 西澤弘成, 成川礼, 松本光代, 五十嵐和彦

日本生化学会大会(Web)　94th　[P-498]　2021/11
Publisher: (公社)日本生化学会
転写因子BACH1が活性化するフェロトーシス細胞由来抗老化シグナルモデル

西澤弘成, 松本光代, 五十嵐和彦

日本生化学会大会(Web)　94th　[2T13a-487)]　2021/11
Publisher: (公社)日本生化学会
幹細胞から赤血球への通り道メチオニン代謝によるエピゲノム調節をかいした赤血球造血制御(Methionine metabolism controls erythropoiesis by epigenetic regulation)

加藤浩貴, Long Nugyen, 石井悠翔, 松本光代, 三枝大輔, 舟山亮, 岡江寛明, 藤原亨, 武藤哲彦, 中山啓子, 有馬隆博, Scadden David, 五十嵐和彦, 張替秀郎

日本血液学会学術集会　83回　PSY-4　2021/09
Publisher: (一社)日本血液学会
エピゲノムによるがんの表現型多様性及び可塑性の制御 BACH1遺伝子制御ネットワークによる膵癌細胞の多様性と転移の制御

五十嵐和彦, 西澤弘成, 松本光代

日本癌学会総会記事　80th　[S13-3]　2021/09
Publisher: (一社)日本癌学会
ISSN： 0546-0476
BACH1による鉄代謝と上皮間葉転換のクロストーク

五十嵐和彦, 西澤弘成, 松本光代

日本酸化ストレス学会学術集会プログラム・抄録集　74th (CD-ROM)　2021
Methionine metabolism controls erythropoiesis by epigenetic regulation

加藤浩貴, 加藤浩貴, 加藤浩貴, NGUYEN Long, 石井悠翔, 石井悠翔, 松本光代, 三枝大輔, 舟山亮, 岡江寛明, 藤原亨, 武藤哲彦, 中山啓子, 有馬隆博, SCADDEN David, 五十嵐和彦, 張替秀郎

日本血液学会学術集会抄録(Web)　83rd　2021
遺伝情報を調節するメチル化連動システム S-アデノシルメチオニン代謝系による遺伝子発現の調節機構

五十嵐和彦, Nguyen Long Chi, 石井悠翔, 加藤浩貴, 落合恭子, 松本光代, 島弘季

日本生化学会大会プログラム・講演要旨集　93回　[3S02m-03]　2020/09
Publisher: (公社)日本生化学会
TBK1-BACH1 pathway controls iron metaboilsm

劉亮, 松本光代, 松井(渡部)美紀, 西澤弘成, 五十嵐和彦

日本生化学会大会(Web)　93rd　[1Z07-459)]　2020/09
Publisher: (公社)日本生化学会
ヘムシグナルによる転写因子BACH2のリン酸化と相互作用因子の制御

松井美紀, 角屋駿, 島弘季, 武藤哲彦, 松本光代, 白水美香子, 村山和隆, 五十嵐和彦

日本生化学会大会プログラム・講演要旨集　92回　[3T15m-03]　2019/09
Publisher: (公社)日本生化学会
膵癌におけるBACH1の機能

佐藤正規, 大塚英郎, 松本光代, 齋木由利子, 三浦孝之, 有明恭平, 益田邦洋, 石田晶玄, 水間正道, 林洋毅, 森川孝則, 中川圭, 元井冬彦, 内藤剛, 石田孝宣, 亀井尚, 五十嵐和彦, 海野倫明

日本外科学会定期学術集会抄録集　119回　SF-065　2019/04
Publisher: (一社)日本外科学会
膵癌におけるBACH1の機能

佐藤正規, 大塚英郎, 松本光代, 齋木由利子, 三浦孝之, 有明恭平, 益田邦洋, 石田晶玄, 水間正道, 林洋毅, 森川孝則, 中川圭, 元井冬彦, 内藤剛, 石田孝宣, 亀井尚, 五十嵐和彦, 海野倫明

日本外科学会定期学術集会抄録集　119回　SF-8　2019/04
Publisher: (一社)日本外科学会
TBK1による転写抑制因子Bach2の調節機構の解明

角屋駿, 松井美紀[渡部], 武藤哲彦, 島弘季, 松本光代, 五十嵐和彦

日本生化学会大会プログラム・講演要旨集　91回　[1T12e-236)]　2018/09
Publisher: (公社)日本生化学会
生体金属のMagical Powerとその研究最前線形質細胞分化におけるヘムシグナルと天然変性タンパク質Bach2

松井美紀, 角屋駿, 島弘季, 武藤哲彦, 松本光代, 白水美香子, 村山和隆, 五十嵐和彦

日本生化学会大会プログラム・講演要旨集　91回　[3S09m-03]　2018/09
Publisher: (公社)日本生化学会
RNAのメチル化恒常性:Methylstat RNAメチル化によるS-アデノシルメチオニン量の制御機構とその意義

島弘季, 松本光代, 五十嵐和彦

日本生化学会大会プログラム・講演要旨集　91回　[3S06a-02]　2018/09
Publisher: (公社)日本生化学会
Bach1は筋芽細胞を活性化し筋の再生を促進する

鈴木一史, 松本光代, 加藤恭丈, 永富良一, 奥野洋史, 井樋栄二, 五十嵐和彦

日本整形外科学会雑誌　92　(8)　S1742-S1742　2018/08
Publisher: (公社)日本整形外科学会
ISSN： 0021-5325
転写因子Bach1による酸化ストレス依存メラノーマ細胞増殖抑制機序

松本光代, ブリドン・アンドレイ, 熊谷さやか, 五十嵐和彦

生命科学系学会合同年次大会　2017年度　[1P-1046]　2017/12
Publisher: 生命科学系学会合同年次大会運営事務局
全能性獲得と消失の分子機構の理解に向けてマウス始原生殖細胞の発生分化における代謝特性変換の制御機構の解析

林陽平, 大塚慧, 蝦名真行, 五十嵐香織, 竹原雅子花, 松本光代, 金井昭夫, 五十嵐和彦, 曽我朋義, 松居靖久

生命科学系学会合同年次大会　2017年度　[3PW22-3]　2017/12
Publisher: 生命科学系学会合同年次大会運営事務局
Bach1によるフェロトーシス誘導と細胞老化抑制による細胞運命の二極化

西澤弘成, 松本光代, 進藤智彦, 三枝大輔, 蝦名真行, 下川宏明, 五十嵐和彦

生命科学系学会合同年次大会　2017年度　[3PT19-0396)]　2017/12
Publisher: 生命科学系学会合同年次大会運営事務局
ヘムシグナルによる天然変性タンパク質Bach2の制御機構と生理学的意義の解明

松井美紀, 島弘季, 武藤哲彦, 松本光代, 村山和隆, 五十嵐和彦

生命科学系学会合同年次大会　2017年度　[4P2T15-0632)]　2017/12
Publisher: 生命科学系学会合同年次大会運営事務局
転写因子Bach1及びBach2の環境変化に応じた赤血球-ミエロイド分化制御(Bach1 and Bach2 orchestrate erythro-myeloid differentiation responding to environmental changes)

Kato Hiroki, Itoh Ari, Matsumoto Mitsuyo, Shibuya Risa, Sato Yuki, Kobayashi Masahiro, Muto Akihiko, Fujiwara Tohru, Harigae Hideo, Igarashi Kazuhiko

臨床血液　58　(9)　1489-1489　2017/09
Publisher: (一社)日本血液学会-東京事務局
ISSN： 0485-1439

eISSN： 1882-0824
肝再生を考慮した肝切除基礎から臨床へ多層的オミックス解析による門脈塞栓後代償性肝肥大の分子メカニズムの解明

佐藤好宏, 大塚英郎, 深瀬耕二, 加藤恭丈, 松本光代, 蝦名真行, 有明恭平, 益田邦洋, 水間正道, 坂田直昭, 中川圭, 林洋毅, 森川孝則, 元井冬彦, 内藤剛, 五十嵐和彦, 海野倫明

日本外科学会定期学術集会抄録集　117回　WS-6　2017/04
Publisher: (一社)日本外科学会
Transcription Factor Bach1 and Bach2 Operate Erythro-Myeloid Competitive Differentiation By Responding to Environmental Changes

Hiroki Kato, Ari Itoh-Nakadai, Mitsuyo Matsumoto, Risa Ebina-Shibuya, Yuki Sato, Masahiro Kobayashi, Akihiko Muto, Tohru Fujiwara, Hideo Harigae, Kazuhiko Igarashi

BLOOD　128　(22)　2016/12

ISSN： 0006-4971

eISSN： 1528-0020
S-アデノシルメチオニン合成酵素MAT2Aの発現は3'UTRアデニンメチル化が介するmRNA安定性により制御される

島弘季, 松本光代, 蝦名真行, 武藤哲彦, 熊谷さやか, 五十嵐和彦, CREST、AMED

日本生化学会大会プログラム・講演要旨集　89回　[1T15-254)]　2016/09
Publisher: (公社)日本生化学会
転写因子Bach1によるフェロトーシスの促進機能

西澤弘成, 松本光代, 五十嵐和彦

日本生化学会大会プログラム・講演要旨集　89回　[2T05-035)]　2016/09
Publisher: (公社)日本生化学会
活性化B細胞の遺伝子ネットワークのシングルセル解析

武藤哲彦, Sax Nicolas, 松本光代, 五十嵐和彦

日本生化学会大会プログラム・講演要旨集　89回　[2T16-372)]　2016/09
Publisher: (公社)日本生化学会
細胞外環境を転写とエピゲノムへ統合する分子機構 Inner Myeloidの遺伝子制御ネットワークとその環境応答機構

五十嵐和彦, 加藤浩貴, 張替秀郎, 武藤哲彦, 松本光代, 伊藤亜里, AMED-CREST

日本生化学会大会プログラム・講演要旨集　89回　[2S01-2]　2016/09
Publisher: (公社)日本生化学会
門脈結紮後代償性肝肥大における細胞周期関連遺伝子の発現制御機構と、転写因子FOXM1の機能解析

佐藤好宏, 大塚英郎, 深瀬耕二, 加藤恭丈, 松本光代, 元井冬彦, 内藤剛, 江川新一, 五十嵐和彦, 海野倫明

日本消化器外科学会総会　71回　P1-3　2016/07
Publisher: (一社)日本消化器外科学会
門脈結紮後の代償性肝肥大における、FOXM1による細胞周期関連遺伝子の活性化の意義

佐藤好宏, 大塚英郎, 加藤恭丈, 松本光代, 蝦名真行, 前田晋平, 有明恭平, 川口桂, 益田邦洋, 石田晶玄, 深瀬耕二, 水間正道, 坂田直昭, 中川圭, 林洋毅, 森川孝則, 元井冬彦, 内藤剛, 五十嵐和彦, 海野倫明

日本外科学会定期学術集会抄録集　116回　PS-180　2016/04
Publisher: (一社)日本外科学会
マルチオミクス解析を通したマウス始原生殖細胞の代謝特性の解析

林陽平, 林陽平, 林陽平, 蝦名真行, 五十嵐香織, 大塚慧, 竹原雅子花, 松本光代, 五十嵐和彦, 金井昭夫, 曽我朋義, 松居靖久, 松居靖久, 松居靖久

日本分子生物学会年会プログラム・要旨集(Web)　39th　2016
S-アデノシルメチオニン合成酵素MAT2Aの発現は3'UTRアデニンメチル化が介するmRNA安定性により制御される

島弘季, 松本光代, 武藤哲彦, 熊谷さやか, 五十嵐和彦

日本生化学会大会・日本分子生物学会年会合同大会講演要旨集　88回・38回　[3T25-13(3P0747)]　2015/12
Publisher: (公社)日本生化学会
多層的オミックス解析による肝再生分子メカニズムの解明

佐藤好宏, 加藤恭丈, 松本光代, 蝦名貴行, 海野倫明, 五十嵐和彦

日本生化学会大会・日本分子生物学会年会合同大会講演要旨集　88回・38回　[3P1029]-[3P1029]　2015/12
Publisher: (公社)日本生化学会
Transcription Factor Bach1 and Bach2 Control Common Myeloid Progenitor Cell Differentiation Under Infectious Stimuli

Hiroki Kato, Ari Itoh-Nakadai, Risa Ebina-Shibuya, Masahiro Kobayashi, Mitsuyo Matsumoto, Akihiko Muto, Tohru Fujiwara, Hideo Harigae, Kazuhiko Igarashi

BLOOD　126　(23)　2015/12

ISSN： 0006-4971

eISSN： 1528-0020
眼疾患と遺伝子緑内障のゲノム解析次世代医療・個別化医療に向けて

布施昇男, 清水愛, 木村雅恵, 高野良真, 石棟, 宮澤晃子, 国松志保, 劉孟林, 渡邉亮, 安田正幸, 横山悠, 檜森紀子, 津田聡, 山本耕太郎, 中澤徹, 安田純, 勝岡史城, 小島要, 成相直樹, 松本光代, 元池育子, 長崎正朗, 木下賢吾, 五十嵐和彦, 山本雅之, 新堀哲也, 青木洋子, 松原洋一, 舟山亮, 長嶋剛史, 中山啓子, 眞島行彦, 船山智代, 田中光一, 原田高幸, 阿部春樹, 福地健郎, 安田典子, 出田秀尚, 鄭暁東, 白石敦, 大橋裕一, 石田誠夫, 原岳, 金森章泰, 山田裕子, 中村誠, 酒井寛, Richards Julia E

日本眼科学会雑誌　118　(3)　216-240　2014/03
Publisher: (公財)日本眼科学会
ISSN： 0029-0203
Bach1によるPparγ遺伝子発現抑制を介した脂肪細胞分化阻害

松本光代, 松本光代, 白木琢磨, BURYDUN Andrey, 舟山亮, 西田有一郎, 中山啓子, 八重樫伸生, 五十嵐和彦

日本分子生物学会年会プログラム・要旨集(Web)　35th　2012
P2-3-5 非侵襲的に腫瘍進展の定量的評価が可能な卵巣がん腹膜播種モデルマウスの作成(Group59 卵巣腫瘍・基礎3,一般演題)

豊島将文, 松本光代, 鈴木史彦, 永瀬智, 八重樫伸生

日本産科婦人科學會雜誌　64　(2)　598-598　2012
Publisher: 日本産科婦人科学会
ISSN： 0300-9165
ER転写活性の定量的評価と乳癌患者個別化への応用の検討

郷野辰幸, 清野祐子, 花村徹, 松本光代, 大庭華子, 黒住昌史, 武井寛幸, 山口ゆり, 丹羽俊文, 林純一

日本乳癌学会総会プログラム抄録集　19回　386-386　2011/09
Publisher: (一社)日本乳癌学会
Bach1の転写制御標的遺伝子の同定

松本光代, 松本光代, BRYDUN Andrey, 中目亜矢子, 舟山亮, 西田有一郎, 中山啓子, 八重樫伸生, 五十嵐和彦

日本分子生物学会年会プログラム・要旨集(Web)　34th　2011
新規エストロゲン応答遺伝子の発現解析と乳癌個別化の検討(Examination of the expression analysis of novel estrogen responsive genes and individualization of breast cancer)

郷野辰幸, 清野祐子, 松本光代, 大庭華子, 黒住昌史, 丹羽俊文, 山口ゆり, 林慎一

日本癌学会総会記事　68回　324-324　2009/08
Publisher: (一社)日本癌学会
ISSN： 0546-0476
子宮頸部円錐切除術術後の妊娠・分娩に関する検討

松本光代, 寺内文敏, 井谷よしみ, 下村貴子, 芥川修, 佐川泰一, 西洋孝, 井坂惠一

日本産科婦人科学会雑誌　61　(2)　450-450　2009/02
Publisher: (公社)日本産科婦人科学会
ISSN： 0300-9165
P2-44 子宮内膜癌細胞株を用いたエストロゲン合成・代謝機構の解明と新規内分泌療法の検討(Group38 子宮体部悪性腫瘍6,一般演題,第61回日本産科婦人科学会学術講演会)

高橋尚美, 宇都宮裕貴, 松本光代, 伊藤潔, 八重樫伸生

日本産科婦人科學會雜誌　61　(2)　540-540　2009
Publisher: 日本産科婦人科学会
ISSN： 0300-9165
ERのリガンド非依存性活性化を呈するエストロゲン枯渇耐性乳癌細胞株の樹立(Establishment of estrogen-depletion resistant breast cancer cell lines showing ligand-independent activation of ER)

今野広海, 白山知子, 山口ゆり, 清野祐子, 松本光代, 丹羽俊文, 林慎一

日本癌学会総会記事　67回　225-225　2008/09
Publisher: (一社)日本癌学会
ISSN： 0546-0476
ERE-GFPアッセイによる原発性乳がんのエストロゲン受容体転写解析とその臨床病理学的因子との関係(Analysis of transcriptional activity of ER by ERE-GFP assay in primary breast cancer and its clinical significance)

松本光代, 清野祐子, 山口ゆり, 武井寛幸, 黒住昌史, 八重樫伸生, 林慎一

日本癌学会総会記事　67回　108-108　2008/09
Publisher: 日本癌学会
ISSN： 0546-0476
乳癌のエストロゲンシグナルとCancer-Associated Fibroblast(CAF)の機能

山口ゆり, 松本光代, 大庭華子, 清野祐子, 清野祐子, 武井寛之, 黒住昌史, 林慎一

日本内分泌学会雑誌　84　(2)　2008

ISSN： 0029-0661
P4-107 子宮体癌-間質細胞におけるエストロゲンを介した相互作用の解析(Group106 子宮体部悪性腫瘍8,一般演題,第60回日本産科婦人科学会学術講演会)

松本光代, 伊藤潔, 新倉仁, 笹野公伸, 八重樫伸生, 林慎一

日本産科婦人科學會雜誌　60　(2)　820-820　2008
Publisher: 日本産科婦人科学会
ISSN： 0300-9165
P1-128 子宮体癌におけるミッドカインの発現と臨床的意義(Group15 子宮体部悪性腫瘍1,一般演題,第60回日本産科婦人科学会学術講演会)

田辺康次郎, 松本光代, 池松真也, 永瀬智, 高野忠夫, 新倉仁, 伊藤潔, 林慎一, 八重樫伸生

日本産科婦人科學會雜誌　60　(2)　539-539　2008
Publisher: 日本産科婦人科学会
ISSN： 0300-9165
核内レセプターを標的としたホルモン依存性癌の診断と治療の展開(Function of Nuclear Steroid Receptor and its Clinical Application to Hormone-dependent Cancer Development of diagnosis and therapy for hormone dependent cancers targeting nuclear receptor)

林慎一, 松本光代, 山口ゆり

日本癌学会総会記事　66回　30-30　2007/08
Publisher: (一社)日本癌学会
ISSN： 0546-0476
エストロゲン依存性癌の新規診断法開発

松本光代, 松本光代, 山口ゆり, 坂本宙子, 武井寛幸, 新倉仁, 伊藤潔, 鈴木貴, 笹野公伸, 八重樫伸生, 林慎一

生化学　2007

ISSN： 0037-1017
微小環境に依存した子宮体癌のエストロゲン受容体活性化の解析

松本光代, 山口ゆり, 鈴木貴, 笹野公伸, 伊藤潔, 八重樫伸生, 林慎一

日本癌学会総会記事　65回　356-356　2006/09
Publisher: 日本癌学会
ISSN： 0546-0476
乳癌の微小環境によるエストロゲンシグナルと増殖促進作用

山口ゆり, 武井寛幸, 末益公人, 島田佳弘, 小林康人, 黒住昌史, 清野祐子, 松本光代, 松本光代, 林慎一

日本癌学会学術総会記事　65th　2006
3次元マイクロアレイを用いた乳癌治療反応性診断システムの開発

松本光代, 坂本宙子, 山口ゆり, 清野祐子, 武井寛幸, 末益公人, 黒住昌史, 笹野公伸, 八重樫伸生, 林慎一

日本癌学会総会記事　64回　401-401　2005/09
Publisher: 日本癌学会
ISSN： 0546-0476
乳癌の微小環境による増殖促進作用とエストロゲンシグナルの制御機構の解析

YAMAGUCHI YURI, TAKEI HIROYUKI, SUEMASU KIMITO, KOBAYASHI YASUHITO, KUROSUMI MASAFUMI, HARADA NOBUHIRO, MATSUMOTO MITSUYO, SEINO YUKO, HAYASHI SHIN'ICHI

日本癌学会学術総会記事　64th　59　2005/08/15
牛ウイルス性・下痢粘膜病ウイルス(BVDV)coreタンパク質の核酸結合能の検討,及びin vitroでの機能解明

山端洋平, 松本光代, 向井孝夫, 大堀均

日本畜産学会大会講演要旨集　103回　96-96　2004/03
Publisher: (公社)日本畜産学会
ISSN： 1342-4688
in vitroにおける抗ウシコロナウイルス(BCV)剤の検索

松本光代, 向井孝夫, 古川令, 大堀均

日本畜産学会大会講演要旨集　103回　96-96　2004/03
Publisher: (公社)日本畜産学会
ISSN： 1342-4688
牛ウイルス性下痢-粘膜病ウイルス(BVDV)高産生および低産生細胞の作出

沼澤香穂里, 松本光代, 中張憲一, 向井孝夫, 大堀均

日本畜産学会大会講演要旨集　101回　142-142　2003/03
Publisher: (公社)日本畜産学会
ISSN： 1342-4688
牛ウイルス性下痢・粘膜病ウイルス(BVDV)複製過程の解明

山端洋平, 松本光代, 鹿島悠幹, 向井孝夫, 大堀均

日本畜産学会大会講演要旨集　101回　142-142　2003/03
Publisher: (公社)日本畜産学会
ISSN： 1342-4688
ラクトフェリンによる牛ウイルス性下痢-粘膜病ウイルス(BVDV)の感染阻害効果

松本光代, 沼澤香穂里, 山端洋平, 田中ゆか, 向井孝夫, 大堀均

日本畜産学会大会講演要旨集　100回　87-87　2002/03
Publisher: (公社)日本畜産学会
ISSN： 1342-4688
牛ウイルス性下痢-粘膜病ウイルス(BVDV)膜E2タンパク質の大腸菌における発現

松本光代, 藤井智明, 筑紫泰代, 沼沢香穂里, 穂刈聡, 三木真弓, 向井孝夫, 大堀均

日本畜産学会大会講演要旨集　98回　179-179　2001/03
Publisher: (公社)日本畜産学会
ISSN： 1342-4688

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Books and Other Publications 1

Biosynthesis and Action of Estrogen in Gynecological Cancers

Hayashi S, Suzuki T, Ito K, Matsumoto M, Sasano H, Yaegashi N

Research Signpost, India　2007

Research Projects 10

大腸癌における腸内細菌叢‐鉄代謝‐BACH1軸を介したフェロトーシス制御機構の解明

佐藤好宏, 五十嵐和彦, 唐澤秀明, 玉原亨, 松本光代

Offer Organization: 日本学術振興会

System: 科学研究費助成事業

Category: 基盤研究(C)

Institution: 東北大学

2026/04/01 - 2029/03/31
転写因子BACH1と鉄による膵臓癌上皮間葉転換と幹細胞性の促進機構の解明

松本光代

Offer Organization: 日本学術振興会

System: 科学研究費助成事業

Category: 基盤研究(B)

Institution: 東北大学

2022/04/01 - 2026/03/31

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前年度、我々は膵臓癌細胞におけるBACH1の減少が細胞内遊離鉄を減少させ上皮系細胞のマーカーであるE-カドヘリンの発現を亢進させることを報告し、その中で、BACH1の発現がキナーゼの１つであるTBK1によって上昇することを示した。癌の悪性化を促進するBACH1量の制御機構の解明は重要な課題であり、TBK1という手掛かりを得たことから、本年度は更なる機序の解明に努めた。その結果、肝臓癌細胞株であるHepa1細胞やBリンパ球様のNamalwa細胞といった細胞種において、TBK1がBACH1タンパク質をリン酸化依存的にも、また非依存的にもそれぞれ異なった機序において分解することが分かった。これは膵臓癌で見られた現象とは逆であり、TBK1によるBACH1の制御機構が複雑であることが判明し、これを報告した（Int. J. Mol. Sci. 2024, 25, 4141）。他方、以前の研究において我々はBACH1がフェロトーシス（鉄依存性細胞死）の誘導剤であるErastinの感受性を上げることを報告し、BACH1がフェロトーシス促進因子であることを示してきたが、今回、BACH1欠損マウス線維芽細胞にドキシサイクリン依存的にBACH1発現量を上昇させる系を構築することで、BACH1がフェロトーシス誘導因子であることを証明した（J Biochem. 2023,174:239-252）。このことは、BACH1を減少させた膵臓癌細胞の細胞内遊離鉄が減少するという事実と合わせて考えると、悪性因子であるBACH1が、フェロトーシス誘導剤を用いた治療においてはアキレス腱となり得る可能性を示唆した。
転写因子BACH1と鉄による膵臓癌上皮間葉転換と幹細胞性の促進機構の解明

松本光代

Offer Organization: 日本学術振興会

System: 科学研究費助成事業基盤研究(B)

Category: 基盤研究(B)

Institution: 東北大学

2022/04/01 - 2026/03/31
Development of anti-cancer strategy by exploiting BACH1 addiction

Offer Organization: Japan Society for the Promotion of Science

System: Grants-in-Aid for Scientific Research Fund for the Promotion of Joint International Research (Fostering Joint International Research (B))

Category: Fund for the Promotion of Joint International Research (Fostering Joint International Research (B))

Institution: Tohoku University

2020/10/27 - 2025/03/31
上皮間葉移行とフェロトーシス感受性により規定されるRAS変異癌の悪性化と脆弱性

松本光代

Offer Organization: 日本学術振興会

System: 科学研究費助成事業基盤研究(C)

Category: 基盤研究(C)

Institution: 東北大学

2019/04/01 - 2022/03/31
Identification of the mechanism by which SAM synthesis inhibition induces erythroblast maturation

Kato Hiroki, Matsumoto Mitsuyo

Offer Organization: Japan Society for the Promotion of Science

System: Grants-in-Aid for Scientific Research Grant-in-Aid for Research Activity Start-up

Category: Grant-in-Aid for Research Activity Start-up

Institution: Tohoku University

2017/08/25 - 2019/03/31

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Anemia, which is caused by the disorder of red blood cell production, is the diseases with the highest prevalence among all diseases in the world. Although erythropoietin is the only effective drug for anemia, most of the anemia patients from hematopoietic diseases are not fully responsive for erythropoietin. Epigenetic modification related substrates should have important roles in the regulations of hematopoiesis by regulating gene expressions and we have recently identified that one of these substrates have important roles in erythropoiesis. In this study, we have investigated the functions of the substrate in erythropoiesis and revealed that the substrate related metabolic processes can be one of the new therapeutic targets for anemia.
The effect of BACH1 on malignant transformation of tumor

Matsumoto Mitsuyo, SATO masaki, IGARASHI kazuhiko

Offer Organization: Japan Society for the Promotion of Science

System: Grants-in-Aid for Scientific Research Grant-in-Aid for Scientific Research (C)

Category: Grant-in-Aid for Scientific Research (C)

Institution: Tohoku University

2016/04/01 - 2019/03/31

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BTB and CNC homolog 1 (BACH1) promotes transformation, cell proliferation and tumor formation in a model of activated RAS transfected-mouse embryonic fibroblasts (MEFs). We focused on the role of BACH1 in the pancreatic ductal adenocarcinoma (PDAC) more than 90% of which has KRAS mutation. Although BACH1 did not affect cell proliferation and tumor growth, but promoted migration ability and invasion ability in vitro and metastasis in vivo. We revealed that BACH1 repressed directly the expression of multiple epithelial-related genes as its mechanism. We showed also BACH1 is a poor prognostic factor on PDAC.
Methods rewriting epigenome as the target of methyonine adenosyltransferase II

KATOH Yasutake, MORITA Masanobu, NAGASHIMA Takeshi, SAIGUSA Daisuke, MATSUMOTO Mitsuyo, IGARASHI Kazuhiko

Offer Organization: Japan Society for the Promotion of Science

System: Grants-in-Aid for Scientific Research Grant-in-Aid for Scientific Research (C)

Category: Grant-in-Aid for Scientific Research (C)

Institution: Tohoku University

2013/04/01 - 2016/03/31

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Methionine adenosyltransferase (MAT) catalyzes S-adenosylmethionine (SAM) synthesis, which is utilized as a methyl donor in transmethylation reactions. MATII, a MAT isozyme, is composed of the catalytic α and regulatory β subunits. Both of the subunits are recruited to a subset of target genes of Bach1 and MafK to facilitate their repression. However, it has been unclear how the nuclear accumulation of MATII subunits is regulated. Using overexpression and bimolecular fluorescence complementation, we found that MATIIβ promoted the nuclear localization of the α subunit and that resulting heterooligomer was present predominantly in nuclear compartment. A single serine residue of α subunit was required for its interaction with β subunit and efficient nuclear accumulation.These results suggest that β subunit defines nulcear-specific MAT isozyme by facilitating nuclear import of its catalytic subunit.
The investigation of function of repressor Bach1 in microenvironment of the tumor and the application to a mouse model for cancer stem cell transplantation.

MATSUMOTO Mitsuyo

Offer Organization: Japan Society for the Promotion of Science

System: Grants-in-Aid for Scientific Research Grant-in-Aid for Young Scientists (B)

Category: Grant-in-Aid for Young Scientists (B)

Institution: Tohoku University

2010 - 2012

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We planned the construction of a Bach1^<-/-> immune-deficient mouse as a good recipient mouse model for engraftment and metastatic of human transplantable tumor cells. Therefore, we aimed to investigate the mechanism and role of Bach1 in fibroblast cell. To identify novel target genes of Bach1 in fibroblast cell, we performed ChIP-seq, DNA microarray, qPCR and western blotting analysis. These results suggest that Bach1 acts as a repressor of Pparγgene transcription in immortalized MEF (iMEF). Bach1^<-/-> iMEF more easily differentiated to adipocytes when treated with insuline, IBMX, dexamethasone and Pparγ ligand in vitro. Bach1 might play a role in adipose differentiation of fibroblast cell by modulating the actions of Pparγ.
Estrogen signaling ability in human endometrial cancer and breastcancer through the cancer-stromal interaction.

MATSUMOTO Mitsuyo

Offer Organization: Japan Society for the Promotion of Science

System: Grants-in-Aid for Scientific Research Grant-in-Aid for Young Scientists (B)

Category: Grant-in-Aid for Young Scientists (B)

Institution: Tohoku University

2007 - 2009

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The estrogen pathway plays an important role in the etiology of human endometrial cancer and breast cancer. However, there is not report that evaluated estrogen responsiveness of specimens from individual patients. We established new reporter analysis system for detection of estrogen signal activity in primary tumor cells. Our results underscore the importance of tailoring therapy to individual patients with estrogen-dependent tumor, and our assay provide a way to accomplish this.

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