scholarly journals High-mobility group box 1 and the receptor for advanced glycation end products contribute to lung injury during Staphylococcus aureus pneumonia

Critical Care ◽  
2013 ◽  
Vol 17 (6) ◽  
pp. R296 ◽  
Author(s):  
Ahmed Achouiti ◽  
Anne van der Meer ◽  
Sandrine Florquin ◽  
Huan Yang ◽  
Kevin J Tracey ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Lung Injury ◽  
Advanced Glycation End Products ◽  
High Mobility ◽  
High Mobility Group ◽  
Advanced Glycation ◽  
Glycation End Products ◽  
End Products ◽  
Staphylococcus Aureus Pneumonia

scholarly journals Dietary advanced glycation end-products, its pulmonary receptor, and high mobility group box 1 in aspiration lung injury

2014 ◽  
Vol 191 (1) ◽  
pp. 214-223 ◽  
Author(s):  
Peter J. Smit ◽  
Weidun A. Guo ◽  
Bruce A. Davidson ◽  
Barbara A. Mullan ◽  
Jadwiga D. Helinski ◽  
...  
Keyword(s):  
Lung Injury ◽  
Advanced Glycation End Products ◽  
High Mobility ◽  
High Mobility Group ◽  
Advanced Glycation ◽  
Glycation End Products ◽  
End Products ◽  
Pulmonary Receptor

scholarly journals High-mobility group box 1 inhibits HCO3− absorption in medullary thick ascending limb through a basolateral receptor for advanced glycation end products pathway

2015 ◽  
Vol 309 (8) ◽  
pp. F720-F730 ◽  
Author(s):  
David W. Good ◽  
Thampi George ◽  
Bruns A. Watts
Keyword(s):  
Advanced Glycation End Products ◽  
Basolateral Membrane ◽  
High Mobility ◽  
High Mobility Group ◽  
Renal Tubules ◽  
Thick Ascending Limb ◽  
Advanced Glycation ◽  
Medullary Thick Ascending Limb ◽  
Glycation End Products ◽  
End Products

High-mobility group box 1 (HMGB1) is a damage-associated molecule implicated in mediating kidney dysfunction in sepsis and sterile inflammatory disorders. HMGB1 is a nuclear protein released extracellularly in response to infection or injury, where it interacts with Toll-like receptor 4 (TLR4) and other receptors to mediate inflammation. Previously, we demonstrated that LPS inhibits HCO3- absorption in the medullary thick ascending limb (MTAL) through a basolateral TLR4-ERK pathway (Watts BA III, George T, Sherwood ER, Good DW. Am J Physiol Cell Physiol 301: C1296–C1306, 2011). Here, we examined whether HMGB1 could inhibit HCO3- absorption through the same pathway. Adding HMGB1 to the bath decreased HCO3− absorption by 24% in isolated, perfused rat and mouse MTALs. In contrast to LPS, inhibition by HMGB1 was preserved in MTALs from TLR4−/− mice and was unaffected by ERK inhibitors. Inhibition by HMGB1 was eliminated by the receptor for advanced glycation end products (RAGE) antagonist FPS-ZM1 and by neutralizing anti-RAGE antibody. Confocal immunofluorescence showed expression of RAGE in the basolateral membrane domain. Inhibition of HCO3−absorption by HMGB1 through RAGE was additive to inhibition by LPS through TLR4 and to inhibition by Gram-positive bacterial molecules through TLR2. Bath amiloride, which selectively prevents inhibition of MTAL HCO3− absorption mediated through Na+/H+ exchanger 1 (NHE1), eliminated inhibition by HMGB1. We conclude that HMGB1 inhibits MTAL HCO3− absorption through a RAGE-dependent pathway distinct from TLR4-mediated inhibition by LPS. These studies provide new evidence that HMGB1-RAGE signaling acts directly to impair the transport function of renal tubules. They reveal a novel paradigm for sepsis-induced renal tubule dysfunction, whereby exogenous pathogen-associated molecules and endogenous damage-associated molecules act directly and independently to inhibit MTAL HCO3− absorption through different receptor signaling pathways.

Role of Receptors for Advanced Glycation End Products and High-Mobility Group Box 1 in the Outcome of Human T Cell Lymphotropic Type 1 Infection

2019 ◽  
Vol 32 (2) ◽  
pp. 89-94 ◽  
Author(s):  
Nafise Yaghouti ◽  
Reza Boostani ◽  
Asadollah Mohamamdi ◽  
Zohreh Poursina ◽  
Seyed Abdolrahim Rezaee ◽  
...  
Keyword(s):  
T Cell ◽  
Advanced Glycation End Products ◽  
High Mobility ◽  
High Mobility Group ◽  
Advanced Glycation ◽  
Human T Cell ◽  
Glycation End Products ◽  
End Products

Stimulation of erythroleukaemia cell differentiation by extracellular high-mobility group-box protein 1 is independent of the receptor for advanced glycation end-products

2002 ◽  
Vol 363 (3) ◽  
pp. 529-535 ◽  
Author(s):  
Bianca SPARATORE ◽  
Marco PEDRAZZI ◽  
Mario PASSALACQUA ◽  
Deborah GAGGERO ◽  
Mauro PATRONE ◽  
...  
Keyword(s):  
Cell Differentiation ◽  
Advanced Glycation End Products ◽  
High Mobility ◽  
Cell Types ◽  
Dominant Negative ◽  
High Mobility Group ◽  
Advanced Glycation ◽  
Stable Transfectants ◽  
Glycation End Products ◽  
End Products

In several cell types the binding of extracellular high-mobility group-box protein 1 (HMGB1) with the receptor for advanced glycation end-products (RAGE) induces cytoskeletal reorganization and cell motility. To establish whether RAGE is also involved in murine erythroleukaemia (MEL) cell differentiation stimulated by HMGB1, we have demonstrated that these cells express a 51kDa protein identified as RAGE, and then we have produced stable transfectants overexpressing wild-type (wt) RAGE or a dominant negative (dn) RAGE mutant lacking the cytoplasmic domain to analyse the differentiation process in these cells. Several experimental findings indicated that RAGE was not involved in the MEL cell differentiation programme. This was also supported by the identical stimulatory effect exerted by HMGB1 on both wt- or dn-RAGE transfectants. We have also observed that HMGB1 binds a 65kDa protein on the surface of MEL cells, supporting the hypothesis that alternative targets of HMGB1 are expressed on the MEL cell membrane and may be involved as mediators of its signalling.

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