The DOI matches its Crossref record; 29 of the 29 references it cites were found in a registry or an index.
Redox Imbalance in Cystine/Glutamate Transporter-deficient Mice
Open accessAbstract
Cystine/glutamate transporter, designated as system x(-)(c), mediates cystine entry in exchange for intracellular glutamate in mammalian cells. This transporter consists of two protein components, xCT and 4F2 heavy chain, and the former is predicted to mediate the transport activity. This transporter plays a pivotal role for maintaining the intracellular GSH levels and extracellular cystine/cysteine redox balance in cultured cells. To clarify the physiological roles of this transporter in vivo, we generated and characterized mice lacking xCT. The xCT(-/-) mice were healthy in appearance and fertile. However, cystine concentration in plasma was significantly higher in these mice, compared with that in the littermate xCT(-/-) mice, while there was no significant difference in plasma cysteine concentration. Plasma GSH level in xCT(-/-) mice was lower than that in the xCT(-/-) mice. The embryonic fibroblasts derived from xCT(-/-) mice failed to survive in routine culture medium, and 2-mercaptoethanol was required for survival and growth. When 2-mercaptoethanol was removed from the culture medium, cysteine and GSH in these cells dramatically decreased, and cells started to die within 24 h. N-Acetyl cysteine also rescued xCT(-/-)-derived cells and permitted growth. These results demonstrate that system x(-)(c) contributes to maintaining the plasma redox balance in vivo but is dispensable in mammalian development, although it is vitally important to cells in vitro.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“SLC7A11-deficient mice develop normally and are healthy [79]”
From Ferroptosis: Death by Lipid Peroxidation (2016) · cites this paper as [79]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Free Radicals in the Physiological Control of Cell Function
Dröge, W. (2002) · Physiological Reviews · doi:10.1152/physrev.00018.2001 · Cited by 9,855
Tietze, F. (1969) · Analytical Biochemistry · doi:10.1016/0003-2697(69)90064-5 · Cited by 6,077
Sato, H., Tamba, M., Ishii, T., & Bannai, S. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.17.11455 · Cited by 1,111
Self-citationRole of amino acid transport and countertransport in nutrition and metabolism.
Christensen, H. N. (1990) · Physiological Reviews · doi:10.1152/physrev.1990.70.1.43 · Cited by 1,105
Redox state of glutathione in human plasma
Jones, D. P., Carlson, J. L., Mody, V. C., Cai, J., Lynn, M., & Sternberg, P. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00275-0 · Cited by 587
Sasaki, H., Sato, H., Kuriyama-Matsumura, K., Sato, K., Maebara, K., Wang, H., Tamba, M., Itoh, K., Yamamoto, M. P., & Bannai, S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m208704200 · Cited by 544
Self-citationMansoor, M. A., Svardal, A. M., & Ueland, P. M. (1992) · Analytical Biochemistry · doi:10.1016/0003-2697(92)90456-h · Cited by 503
Transport interaction of L-cystine and L-glutamate in human diploid fibroblasts in culture.
Bannai, S., & Kitamura, E. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)85901-x · Cited by 456
Self-citationJones, D. P., Mody, V. C., Carlson, J. L., Lynn, M. J., & Sternberg, P. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01040-7 · Cited by 392
Role of membrane transport in metabolism and function of glutathione in mammals
Bannai, S., & Tateishi, N. (1986) · The Journal of Membrane Biology · doi:10.1007/bf01870891 · Cited by 386
Self-citationTransport of cystine and cysteine in mammalian cells
Bannai, S. (1984) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/0304-4157(84)90014-5 · Cited by 327
Self-citationCotgreave, I. A., & Moldéus, P. (1986) · Journal of Biochemical and Biophysical Methods · doi:10.1016/0165-022x(86)90102-8 · Cited by 233
Ishii, T., Bannai, S., & Sugita, Y. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)43284-x · Cited by 221
Self-citationOxidation of glutathione and cysteine in human plasma associated with smoking
Moriarty, S. E., Shah, J. H., Lynn, M., Jiang, S., Openo, K., Jones, D. P., & Sternberg, P. (2003) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2003.09.006 · Cited by 193
Transcriptional control of cystine/glutamate transporter gene by amino acid deprivation
Sato, H., Nomura, S., Maebara, K., Sato, K., Tamba, M., & Bannai, S. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.10.009 · Cited by 176
Self-citationDistribution of Cystine/Glutamate Exchange Transporter, System xc−, in the Mouse Brain
Sato, H., Tamba, M., Okuno, S., Sato, K., Keino‐Masu, K., Masu, M., & Bannai, S. (2002) · Journal of Neuroscience · doi:10.1523/jneurosci.22-18-08028.2002 · Cited by 167
Self-citationInduction of cystine transport activity in mouse peritoneal macrophages.
Watanabe, H., & Bannai, S. (1987) · The Journal of Experimental Medicine · doi:10.1084/jem.165.3.628 · Cited by 161
Self-citationCystine Uptake and Glutathione Level in Fetal Brain Cells in Primary Culture and in Suspension
Sagara, J., Miura, K., & Bannai, S. (1993) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1993.tb09801.x · Cited by 146
Self-citationBannai, S. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)43371-0 · Cited by 141
Self-citationSato, H., Fujiwara, K., Sagara, J., & Bannai, S. (1995) · Biochemical Journal · doi:10.1042/bj3100547 · Cited by 128
Self-citationInduction of cystine transport activity in human fibroblasts by oxygen
Bannai, S., Sato, H., Ishii, T., & Sugita, Y. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)51491-5 · Cited by 121
Self-citationHack, V., Breitkreutz, R., Kinscherf, R., Röhrer, H., Bärtsch, P., Taut, F. J. H., Benner, A., & Dröge, W. (1998) · Blood · doi:10.1182/blood.v92.1.59.413a05_59_67 · Cited by 101
Wilcken, D. E. L., Gupta, V. J., & Reddy, S. G. (1980) · Clinical Science · doi:10.1042/cs0580427 · Cited by 96
Sato, H., Kuriyama-Matsumura, K., Hashimoto, T., Sasaki, H., Wang, H., Ishii, T., Mann, G. E., & Bannai, S. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m007216200 · Cited by 89
Self-citationBannai, S., Sato, H., Ishii, T., & Taketani, S. (1991) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/0167-4889(91)90153-o · Cited by 87
Self-citationHildebrandt, W., Alexander, S., Bärtsch, P., & Dröge, W. (2002) · Blood · doi:10.1182/blood.v99.5.1552 · Cited by 84
Hack, V., Schmid, D., Breitkreutz, R., Stahl‐Henning, C., Brings, P., Kinscherf, R., Taut, F. J. H., Holm, E., & Dröge, W. (1997) · The FASEB Journal · doi:10.1096/fasebj.11.1.9034170 · Cited by 68
Plasma cystine concentration and redox state in aging and physical exercise
Hildebrandt, W., Kinscherf, R., Hauer, K. A., Holm, E., & Dröge, W. (2002) · Mechanisms of Ageing and Development · doi:10.1016/s0047-6374(02)00013-1 · Cited by 57
Various forms of plasma cysteine and its metabolites in patients undergoing hemodialysis
Wlodek, P. J., Iciek, M., Miłkowski, A., & Smoleński, O. (2001) · Clinica Chimica Acta · doi:10.1016/s0009-8981(00)00369-7 · Cited by 35
Flagged first, then by citations
Cited by
Sorted by citations
Ferroptosis: mechanisms, biology and role in disease
Jiang, X., Stockwell, B. R., & Conrad, M. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-00324-8 · Cited by 7,973
Ferroptosis: A Regulated Cell Death Nexus Linking Metabolism, Redox Biology, and Disease
Stockwell, B. R., Friedmann Angeli, J. P., Bayir, H., Bush, A. I., Conrad, M., Dixon, S. J., Fulda, S., Gascón, S., Hatzios, S. K., Kagan, V. E., et al. (2017) · Cell · doi:10.1016/j.cell.2017.09.021 · Cited by 7,695
Ferroptosis: molecular mechanisms and health implications
Tang, D., Chen, X., Kang, R., & Kroemer, G. (2020) · Cell Research · doi:10.1038/s41422-020-00441-1 · Cited by 4,495
Ferroptosis: Death by Lipid Peroxidation
Yang, W. S., & Stockwell, B. R. (2016) · Trends in Cell Biology · doi:10.1016/j.tcb.2015.10.014 · Cited by 3,088
Broadening horizons: the role of ferroptosis in cancer
Chen, X., Kang, R., Kroemer, G., & Tang, D. (2021) · Nature Reviews Clinical Oncology · doi:10.1038/s41571-020-00462-0 · Cited by 3,012
Metadata
- Authors
- Sato, H., Shiiya, A., Kimata, M., Maebara, K., Tamba, M., Sakakura, Y., Makino, N., Sugiyama, F., Yagami, K.-I., Moriguchi, T., Takahashi, S., & Bannai, S.
- Affiliations
- Yamagata University (JP)
- University of Tsukuba (JP)
- Ibaraki Prefectural University of Health Sciences (JP)
- Corresponding author
- Sato, Hideyo
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2005-11
- Volume
- 280
- Issue
- 45
- Pages
- 37423-37429
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2097822945
- Cited by
- 422
- References
- 29
- Citations by year
- 2026: 14 · 2025: 28 · 2024: 34 · 2023: 36 · 2022: 27 · 2021: 27 · 2020: 41 · 2019: 30 · 2018: 29 · 2017: 19 · 2016: 16 · 2015: 15 · 2014: 16 · 2013: 11 · 2012: 9
- FWCI
- 4.28
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- University of Tsukuba
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Sulfur Compounds in Biology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- SLC7A11, system xc-, cystine transport, glutathione, redox homeostasis, cysteine, embryonic fibroblasts, 2-mercaptoethanol, N-acetylcysteine, cysteine biosynthesis
- MeSH terms
- Amino Acids, Animals, Cells, Cultured, Cystine, Female, Fibroblasts, Glutathione, Homozygote, Male, Oxidation-Reduction, Gene Deletion, Amino Acid Transport System y+, Cell Proliferation, Mice
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review