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Author

Shiro Bannai

Other affiliations: Osaka University
Bio: Shiro Bannai is an academic researcher from University of Tsukuba. The author has contributed to research in topics: Cystine & Glutathione. The author has an hindex of 44, co-authored 91 publications receiving 8536 citations. Previous affiliations of Shiro Bannai include Osaka University.


Papers
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Journal ArticleDOI
TL;DR: It is shown that Nrf2 controls the expression of a group of electrophile- and oxidative stress-inducible proteins and activities, which includes heme oxygenase-1, A170, peroxiredoxin MSP23, and cystine membrane transport (system xc −) activity.

1,367 citations

Journal ArticleDOI
TL;DR: In this paper, the authors have isolated cDNA encoding the transporter for system xc- from mouse activated macrophages by expression in Xenopus oocytes, and the sequence analysis revealed that one is identical with the heavy chain of 4F2 cell surface antigen (4F2hc) and the other is a novel protein of 502 amino acids with 12 putative transmembrane domains.

890 citations

Journal ArticleDOI
TL;DR: The experiments using the mouse embryonic fibroblasts derived from the Nrf2-deficient mice revealed that the induction of xCT gene by electrophilic agents is mediated by NRF2, and it was demonstrated that xCT is a novel member of this protein family.

460 citations

Journal ArticleDOI
TL;DR: It is suggested that neurons maintain their glutathione level by taking up cysteine provided by glial cells, because the culture medium contains cystine, but not cys‐teine.
Abstract: — Glutathione levels in neurons and gllal cells were investigated in a neuronal-glial coculture and in separate cultures. Brain cell suspensions obtained from cerebral hemispheres of fetal rats were cultured, and after 5 days the glutathione content of this cell population, consisting mainly of neurons and astroglial cells, was 23.0 nmol/mg of cell protein, with a significantly high content in glial cells (28.0 nmol/mg of protein) in comparison with neurons (18.8 nmol/mg of protein). When the neurons and glial cells were separated and recultured in fresh medium, neu-ronal glutathione rapidly decreased, whereas glial glutathione remained unchanged. Cysteine is a rate-limiting precursor for glutathione synthesis, and its level was also decreased in neurons, but not in glial cells. Cysteine was taken up rapidly by both neurons and glial cells, but cys-tine was taken up only by glial cells. This accounts for the rapid decrease of glutathione in the cultured neurons, because the culture medium contains cystine, but not cys-teine. It was also found that the cultured glial cells released cysteine into the medium. These results suggest that neurons maintain their glutathione level by taking up cysteine provided by glial cells.

425 citations

Journal ArticleDOI
TL;DR: GSH 1 is a tripeptide with a structure of 7-L-glutamyl-Lcysteinylglycine, which is characterized by the yglUTamyl peptide and the reactive thiol group.
Abstract: Glutathione I occurs in almost all living organisms, and its multifunctional properties have been attracting interest of many biochemists, physiologists, pharmacologists as well as clinical scientists. GSH 1 is a tripeptide with a structure of 7-L-glutamyl-Lcysteinylglycine, which is characterized by the yglutamyl peptide and the reactive thiol group. GSH is synthesized in two steps catalyzed by 7-glutamylcysteine synthetase [EC 6.3.2.2] (reaction 1) and glutathione synthetase [EC 6.3.2.3] (reaction 2), respectively.

348 citations


Cited by
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Journal ArticleDOI
TL;DR: There is growing evidence that aging involves, in addition, progressive changes in free radical-mediated regulatory processes that result in altered gene expression.
Abstract: At high concentrations, free radicals and radical-derived, nonradical reactive species are hazardous for living organisms and damage all major cellular constituents. At moderate concentrations, how...

9,131 citations

Journal ArticleDOI
25 May 2012-Cell
TL;DR: This paper identified the small molecule ferrostatin-1 as a potent inhibitor of ferroptosis in cancer cells and glutamate-induced cell death in organotypic rat brain slices, suggesting similarities between these two processes.

7,192 citations

Journal ArticleDOI
TL;DR: It is demonstrated that the previously reported aggresome-like induced structures containing ubiquitinated proteins in cytosolic bodies are dependent on p62 for their formation and p62 is required both for the formation and the degradation of polyubiquitin-containing bodies by autophagy.

3,676 citations

Journal ArticleDOI
05 Oct 2017-Cell
TL;DR: The mechanisms underlying ferroptosis are reviewed, connections to other areas of biology and medicine are highlighted, and tools and guidelines for studying this emerging form of regulated cell death are recommended.

3,356 citations

01 Jan 2007
TL;DR: In this article, the authors showed that the polyubiquitin-binding protein p62/SQSTM1 is degraded by autophagy by using a 22-residue sequence of p62 containing an evolutionarily conserved motif.
Abstract: Protein degradation by basal constitutive autophagy is important to avoid accumulation of polyubiquitinated protein aggregates and development of neurodegenerative diseases. The polyubiquitin-binding protein p62/SQSTM1 is degraded by autophagy. It is found in cellular inclusion bodies together with polyubiquitinated proteins and in cytosolic protein aggregates that accumulate in various chronic, toxic, and degenerative diseases. Here we show for the first time a direct interaction between p62 and the autophagic effector proteins LC3A and -B and the related -aminobutyrate receptor-associated protein and-aminobutyrate receptor-associated-like proteins. The binding is mediated by a 22-residue sequence of p62 containing an evolutionarily conserved motif. To monitor the autophagic sequestration of p62- and LC3-positive bodies, we developed a novel pH-sensitive fluorescent tag consisting of a tandem fusion of the red, acid-insensitive mCherry and the acid-sensitive green fluorescent proteins. This approach revealed that p62- and LC3-positive bodies are degraded in autolysosomes. Strikingly, even rather large p62-positive inclusion bodies (2 m diameter) become degraded by autophagy. The specific interaction between p62 and LC3, requiring the motif we have mapped, is instrumental in mediating autophagic degradation of the p62-positive bodies. We also demonstrate that the previously reported aggresome-like induced structures containing ubiquitinated proteins in cytosolic bodies are dependent on p62 for their formation. In fact, p62 bodies and these structures are indistinguishable. Taken together, our results clearly suggest that p62 is required both for the formation and the degradation of polyubiquitin-containing bodies by autophagy.

3,172 citations