Cited by 956Advanced Glycation End Products researchImmune Response and InflammationHeat shock proteins research

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HMGB1 in health and disease

Open access

Kang, Rui, Chen, Ruochan, Zhang, Qiuhong, Hou, Wen, Wu, Sha, Cao, Lizhi, Huang, Jin, Yu, Yan, Fan, Xue-gong, Yan, Zhengwen, Sun, Xiaofang, Wang, Haichao, Wang, Qingde, Tsung, Allan, Billiar, Timothy R., Zeh, Herbert J., Lotze, Michael T., Tang, Daolin·2014·Molecular Aspects of Medicine

DOI 10.1016/j.mam.2014.05.001PMC PMC4254084

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Abstract

Complex genetic and physiological variations as well as environmental factors that drive emergence of chromosomal instability, development of unscheduled cell death, skewed differentiation, and altered metabolism are central to the pathogenesis of human diseases and disorders. Understanding the molecular bases for these processes is important for the development of new diagnostic biomarkers, and for identifying new therapeutic targets. In 1973, a group of non-histone nuclear proteins with high electrophoretic mobility was discovered and termed high-mobility group (HMG) proteins. The HMG proteins include three superfamilies termed HMGB, HMGN, and HMGA. High-mobility group box 1 (HMGB1), the most abundant and well-studied HMG protein, senses and coordinates the cellular stress response and plays a critical role not only inside of the cell as a DNA chaperone, chromosome guardian, autophagy sustainer, and protector from apoptotic cell death, but also outside the cell as the prototypic damage associated molecular pattern molecule (DAMP). This DAMP, in conjunction with other factors, thus has cytokine, chemokine, and growth factor activity, orchestrating the inflammatory and immune response. All of these characteristics make HMGB1 a critical molecular target in multiple human diseases including infectious diseases, ischemia, immune disorders, neurodegenerative diseases, metabolic disorders, and cancer. Indeed, a number of emergent strategies have been used to inhibit HMGB1 expression, release, and activity in vitro and in vivo. These include antibodies, peptide inhibitors, RNAi, anti-coagulants, endogenous hormones, various chemical compounds, HMGB1-receptor and signaling pathway inhibition, artificial DNAs, physical strategies including vagus nerve stimulation and other surgical approaches. Future work further investigating the details of HMGB1 localization, structure, post-translational modification, and identification of additional partners will undoubtedly uncover additional secrets regarding HMGB1's multiple functions.

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See all 956

Authors: Kang, R., Chen, R., Zhang, Q., Hou, W., Wu, S., Cao, L., Huang, J., Yu, Y., Fan, X.-G., Yan, Z., Sun, X., Wang, H., Wang, Q., Tsung, A., Billiar, T. R., Zeh, H. J., Lotze, M. T., & Tang, D.
Affiliations: University of Pittsburgh (US)
Central South University (CN)
Sun Yat-sen University (CN)
Third Affiliated Hospital of Guangzhou Medical University (CN)
Feinstein Institute for Medical Research (US)
Corresponding author: Kang, Rui
Tang, Daolin
ORCID: Kang, Rui
Chen, Ruochan
Zhang, Qiuhong
Wu, Sha
Cao, Lizhi
Huang, Jin
Yu, Yan
Yan, Zhengwen
Sun, Xiaofang
Wang, Haichao
Wang, Qingde
Tsung, Allan
Billiar, Timothy R.
Zeh, Herbert J.
Lotze, Michael T.
Tang, Daolin
Venue: Molecular Aspects of Medicine
Publisher: Elsevier BV
Published: 2014-12
Volume: 40
Pages: 1-116
ISSN: 0098-2997 (ISSN-L)
DOI: 10.1016/j.mam.2014.05.001
PMC: PMC4254084
OpenAlex: W2075035271
Cited by: 956
References: 1,872
Citations by year: 2026: 33 · 2025: 64 · 2024: 80 · 2023: 87 · 2022: 119 · 2021: 113 · 2020: 114 · 2019: 83 · 2018: 88 · 2017: 53 · 2016: 67 · 2015: 45 · 2014: 8
FWCI: 7.41
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Molecular Aspects of Medicine (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Funders: National Institutes of Health (R01CA160417, R01CA181450, R01AT005076, R01GM063075)
National Natural Sciences Foundation of China (31171328)
2013 Pancreatic Cancer Action Network–AACR Career Development Award (13-20-25-TANG)
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 › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
Keywords: HMGB1, high mobility group box 1, high mobility group proteins, chromosomal instability, DNA damage response, autophagy, apoptosis, damage-associated molecular patterns, inflammation, immune response, HMGB1 inhibitors, neurodegenerative diseases, cancer, ischemia, post-translational modification
MeSH terms: Disease, Health, Humans, HMGB1 Protein

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