Calcium binding to HMG1 protein induces DNA looping by the HMG‐box domains

Štros, Michal; Reich, J.; Kolíbalová, Anna

doi:10.1016/0014-5793(94)00364-5

Cited by 38 publications

(27 citation statements)

References 24 publications

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“…#P Ͻ 0.05 vs. control and 1 h. ‡P Ͻ 0.05 vs. control and 6 h; n ϭ 6. lating uric acid that accompanies IRI leads to HMGB1 translocation in endothelial cells, a process that requires an increase in intracellular calcium and the MEK/Erk pathway (53). The importance of calcium is further evident by studies from other labs that showed HMGB1 active release to involve calcium/ calmodulin interaction and calcium-dependent secretory pathways involving CRM1, an interaction further stimulated by ROS (15,23,28,29,32,51,53,63,64,72,85). In addition, the active release of HMGB1 during IRI appears to involve other signaling cascades in nonnecrotic cells including acetylation and possible phosphorylation of HMGB1 (9,27,53), a process that seemingly requires a reduction in deacetylase activity in the nucleus (17).…”

Section: Discussionmentioning

confidence: 99%

HMGB1 in renal ischemic injury

Rabadi

Ghaly

Goligorksy

et al. 2012

American Journal of Physiology-Renal Physiology

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Factors that initiate cellular damage and trigger the inflammatory response cascade and renal injury are not completely understood after renal ischemia-reperfusion injury (IRI). High-mobility group box-1 protein (HMGB1) is a damage-associated molecular pattern molecule that binds to chromatin, but upon signaling undergoes nuclear-cytoplasmic translocation and release from cells. Immunohistochemical and Western blot analysis identified HMGB1 nuclear-cytoplasmic translocation and release from renal cells (particularly vascular and tubular cells) into the venous circulation after IRI. Time course analysis indicated HMGB1 release into the venous circulation progressively increased parallel to increased renal ischemic duration. Ethyl pyruvate (EP) treatment blocked H2O2(oxidative stress)-induced HMGB1 release from human umbilical vein endothelial cells in vitro, and in vivo resulted in nuclear retention and significant blunting of HMGB1 release into the circulation after IRI. EP treatment before IRI improved short-term serum creatinine and albuminuria, proinflammatory cyto-/chemokine release, and long-term albuminuria and fibrosis. The renoprotective effect of EP was abolished when exogenous HMGB1 was injected, suggesting EP's therapeutic efficacy is mediated by blocking HMGB1 translocation and release. To determine the independent effects of circulating HMGB1 after injury, exogenous HMGB1 was administered to healthy animals at pathophysiological dose. HMGB1 administration induced a rapid surge in systemic circulating cyto-/chemokines (including TNF-α, eotaxin, G-CSF, IFN-γ, IL-10, IL-1α, IL-6, IP-10, and KC) and led to mobilization of bone marrow CD34+Flk1+ cells into the circulation. Our results indicate that increased ischemic duration causes progressively enhanced HMGB1 release into the circulation triggering damage/repair signaling, an effect inhibited by EP because of its ability to block HMGB1 nuclear-cytoplasmic translocation.

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Section: Discussionmentioning

confidence: 99%

HMGB1 in renal ischemic injury

Rabadi

Ghaly

Goligorksy

et al. 2012

American Journal of Physiology-Renal Physiology

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“…The expression vector for HMG-1(A-B) didomain (residues 1-176), obtained from M. Bianchi, was transfected into BL21(DE3) cells, and the expressed protein was purified using published protocols (25).…”

Section: Methodsmentioning

confidence: 99%

The Binding Interaction of HMG-1 with the TATA-binding Protein/TATA Complex

Das

Scovell

2001

Journal of Biological Chemistry

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High mobility protein-1 (HMG-1) has been shown to regulate transcription by RNA polymerase II. In the context that it acts as a transcriptional repressor, it binds to the TATA-binding protein (TBP) to form the HMG-1/ TBP/TATA complex, which is proposed to inhibit the assembly of the preinitiation complex. By using electrophoretic mobility shift assays, we show that the acidic C-terminal domain of HMG-1 and the N terminus of human TBP are the domains that are essential for the formation of a stable HMG-1/TBP/TATA complex. HMG-1 binding increases the affinity of TBP for the TATA element by 20-fold, which is reflected in a significant stimulation of the rate of TBP binding, with little effect on the dissociation rate constant. In support of the binding target of HMG-1 being the N terminus of hTBP, the Nterminal polypeptide of human TBP competes with and inhibits HMG-1/TBP/TATA complex formation. Deletion of segments of the N terminus of human TBP was used to map the region(s) where HMG-1 binds. These findings indicate that interaction of HMG-1 with the Q-tract (amino acids 55-95) in hTBP is primarily responsible for stable complex formation. In addition, HMG-1 and the monoclonal antibody, 1C2, specific to the Q-tract, compete for the same site. Furthermore, calf thymus HMG-1 forms a stable complex with the TBP/TATA complex that contains TBP from either human or Drosophila but not yeast. This is again consistent with the importance of the Q-tract for this stable interaction and shows that the interaction extends over many species but does not include yeast TBP.The TATA-binding protein is a universal transcription factor that is essential for eukaryotic transcription by all three RNA polymerases (1-4). For RNA polymerase II transcription, the regulation of TBP 1 binding to the TATA element is considered a principal determinant in promoter activity and therefore a primary target for regulatory factors. TBP can be considered modular in nature, with its highly conserved C terminus being necessary and sufficient for both binding to the TATA box and basal level transcription (5, 6). In addition all activators and repressors that bind to human TBP (hTBP) are reported to bind to the C terminus (2-4). On the other hand, the interactions of regulatory factors with the 159-residue N terminus in hTBP appear much more limited, and its role in transcriptional regulation is not understood. In the only case that is characterized, it was shown that the N terminus down-regulates hTBP binding to the U6 TATA box, mediates cooperative binding with SNAPc to the U6 promoter, and facilitates an enhanced level of RNA polymerase III transcription of the U6 gene (7,8). In addition, a monoclonal antibody specific for the Q-tract of the N terminus of hTBP was shown to inhibit selectively in vitro transcription from TATA-containing, but not TATA-less, promoters that were transcribed by RNA pol II or III. This antibody interaction did not affect TBP binding to the TATA box or inhibit the formation of the TFIIA/TFIIB/TBP/TATA complex, which sugges...

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“…43 Furthermore, in the absence of calcium, HMGB1 DNA binding properties are enhanced. [44][45][46] Recent studies suggest the possible role of elevated cytosolic calcium concentration and calcium/calmodulin-dependent and mitogen-activated protein kinase kinase (MEK)/extracellular signal-regulated kinase (ERK)-dependent regulatory pathways in the nucleocytoplasmic shuttling and release of HMGB1. 39,40 Oh et al showed in monocytes that HMGB1 secretion is induced by a calcium ionophore and inhibited by calcium chelators.…”

Section: Systemic Inflammation: Three Waves Of Danger Signalingmentioning

confidence: 99%

Messengers without Borders

Ratliff

Rabadi

Vasko

et al. 2013

Journal of the American Society of Nephrology

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The list of signals sent by an injured organ to systemic circulation, so-called danger signals, is growing to include multiple metabolites and secreted moieties, thus revealing a highly complex and integrated network of interlinked systemic proinflammatory and proregenerative messages. Emerging new data indicate that, apart from the well established local inflammatory response to AKI, danger signaling unleashes a cascade of precisely timed, interdependent, and intensity-gradated mediators responsible for development of the systemic inflammatory response. This fledgling realization of the importance of the systemic inflammatory response to the localized injury and inflammation is at the core of this brief overview. It has a potential to explain the additive effects of concomitant diseases or preexisting chronic conditions that can prime the systemic inflammatory response and exacerbate it out of proportion to the actual degree of acute kidney damage. Although therapies for ameliorating AKI per se remain limited, a potentially powerful strategy that could reap significant benefits in the future is to modulate the intensity of danger signals and consequently the systemic inflammatory response, while preserving its intrinsic proregenerative stimuli.

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Calcium binding to HMG1 protein induces DNA looping by the HMG‐box domains

Cited by 38 publications

References 24 publications

HMGB1 in renal ischemic injury

HMGB1 in renal ischemic injury

The Binding Interaction of HMG-1 with the TATA-binding Protein/TATA Complex

Messengers without Borders

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