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2014 ; 40
(ä): 1-116
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HMGB1 in health and disease
#MMPMID25010388
Kang R
; Chen R
; Zhang Q
; Hou W
; Wu S
; Cao L
; Huang J
; Yu Y
; Fan XG
; Yan Z
; Sun X
; Wang H
; Wang Q
; Tsung A
; Billiar TR
; Zeh HJ 3rd
; Lotze MT
; Tang D
Mol Aspects Med
2014[Dec]; 40
(ä): 1-116
PMID25010388
show ga
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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