The DOI matches its Crossref record; 20 of the 20 references it cites were found in a registry or an index.
A Janus Tale of Two Active High Mobility Group Box 1 (HMGB1) Redox States
Open accessAbstract
High mobility group box 1 (HMGB1), the prototypic damage-associated molecular pattern molecule, is released at sites of inflammation and/or tissue damage. There, it promotes cytokine production and chemokine production/cell migration. New work shows that the redox status of HMGB1 distinguishes its cytokine-inducing and chemokine activity. Reduced all-thiol-HMGB1 has sole chemokine activity, whereas disulfide-HMGB1 has only cytokine activity, and oxidized, denatured HMGB1 has neither. Autophagy (programmed cell survival) and apoptosis (programmed cell death) have been implicated in controlling both innate and adaptive immune functions. Reduced HMGB1 protein promotes autophagy, whereas oxidized HMGB1 promotes apoptosis. Thus, the differential activity of HMGB1 in immunity, inflammation and cell death depends on the cellular redox status within tissues.
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“That said, it should be noted that biological activities of HMGB1 may flip from pro-inflammatory to anti-inflammatory depending on multiple variables including its oxidation state [917–923].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [917]
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1 retracted
Yang, H., Lundbäck, P., Ottosson, L., Erlandsson-Harris, H., Venereau, E., Bianchi, M. E., Al-Abed, Y., Andersson, U., Tracey, K. J., & Antoine, D. J. (2012) · Molecular Medicine · doi:10.2119/molmed.2011.00389 · Cited by 407
RetractedAutophagy and the Integrated Stress Response
Kroemer, G., Mariño, G., & Levine, B. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.09.023 · Cited by 3,506
High-mobility group box 1 protein (HMGB1): nuclear weapon in the immune arsenal
Lotze, M. T., & Tracey, K. J. (2005) · Nature reviews. Immunology · doi:10.1038/nri1594 · Cited by 2,490
Self-citationEaten alive: a history of macroautophagy
Yang, Z., & Klionsky, D. J. (2010) · Nature Cell Biology · doi:10.1038/ncb0910-814 · Cited by 2,155
HMGB1 is a therapeutic target for sterile inflammation and infection
Andersson, U., & Tracey, K. J. (2011) · Annual Review of Immunology · doi:10.1146/annurev-immunol-030409-101323 · Cited by 1,437
PAMP s and DAMP s: signal 0s that spur autophagy and immunity
Tang, D., Kang, R., Coyne, C. B., Zeh, H. J., & Lotze, M. T. (2012) · Immunological Reviews · doi:10.1111/j.1600-065x.2012.01146.x · Cited by 1,327
Self-citationChiba, S., Baghdadi, M., Akiba, H., Yoshiyama, H., Kinoshita, I., Dosaka-Akita, H., Fujioka, Y., Ohba, Y., Gorman, J. V., Colgan, J. D., et al. (2012) · Nature Immunology · doi:10.1038/ni.2376 · Cited by 838
Yang, H., Hreggvidsdottir, H. S., Palmblad, K., Wang, H., Ochani, M., Li, J., Lü, B., Chavan, S. S., Rosas‐Ballina, M., Al‐Abed, Y., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1003893107 · Cited by 812
Mutually exclusive redox forms of HMGB1 promote cell recruitment or proinflammatory cytokine release
Venereau, E., Casalgrandi, M., Schiraldi, M., Antoine, D. J., Cattaneo, A., De Marchis, F., Liu, J., Antonelli, A., Preti, A., Raeli, L., et al. (2012) · Journal of Experimental Medicine · doi:10.1084/jem.20120189 · Cited by 720
HMGB1: A multifunctional alarmin driving autoimmune and inflammatory disease
Harris, H. E., Andersson, U., & Pisetsky, D. S. (2012) · Nature Reviews Rheumatology · doi:10.1038/nrrheum.2011.222 · Cited by 689
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Kang, R., & Tang, D. (2017) · Springer eBooks · doi:10.1007/978-3-319-58106-4_7 · Cited by 1
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Tang, D., & Kang, R. (2016) · InTech eBooks · doi:10.5772/63476 · Cited by 1
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HMGB1 Polymorphisms in Acute Lymphoblastic Leukemia
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Biguetti, C. C., Chaves-Neto, A. H., Elvin, P. T., Fontaine, J. L., Brown, E. L., Hanis, C. L., & Fakhouri, W. D. (2025) · medRxiv · doi:10.1101/2025.06.23.25329883
Chandrashekar, B. L., Arteaga, A., Rios, E., Mora, J., Garlet, G. P., Rodrigues, D. C., & Biguetti, C. C. (2025) · Journal of Applied Oral Science · doi:10.1590/1678-7757-2025-0358
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Mechanistic Insights of Oxidative Stress in Inflammation
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Metadata
- Authors
- Tang, D., Billiar, T. R., & Lotze, M. T.
- Affiliations
- University of Pittsburgh (US)
- Corresponding author
- Tang, Daolin
- Venue
- Molecular Medicine
- Published
- 2012-10
- Volume
- 18
- Issue
- 10
- Pages
- 1360-1362
- ISSN
- 1076-1551 (ISSN-L)
- 1528-3658
- PMC
- PMC3533642
- OpenAlex
- W224680839
- Cited by
- 112
- References
- 20
- Citations by year
- 2026: 3 · 2025: 8 · 2024: 6 · 2023: 6 · 2022: 4 · 2021: 8 · 2020: 7 · 2019: 3 · 2018: 7 · 2017: 9 · 2016: 10 · 2015: 16 · 2014: 13 · 2013: 12
- FWCI
- 8.42
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by-nc-nd
- creativecommons.org/licenses/by/4.0 (tdm)
- Locations
- Molecular Medicine (publishedVersion, cc-by-nc-nd)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- University of Pittsburgh
- National Institutes of Health
- National Cancer Institute (R01CA160417)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Keywords
- HMGB1, redox state, disulfide bonds, damage-associated molecular patterns, chemokine activity, cytokine production, autophagy, apoptosis, inflammation, innate immunity, protein oxidation
- MeSH terms
- Animals, Disease, Humans, Oxidation-Reduction, Reactive Oxygen Species, HMGB1 Protein
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