scholarly journals The metal nanoparticle-induced inflammatory response is regulated by SIRT1 through NF-κB deacetylation in aseptic loosening

2017 ◽  
Vol Volume 12 ◽  
pp. 3617-3636 ◽  
Author(s):  
Zhantao Deng ◽  
Jiewen Jin ◽  
Zhenheng Wang ◽  
Yong Wang ◽  
Qian Gao ◽  
...  
Keyword(s):  
Inflammatory Response ◽  
Aseptic Loosening ◽  
Metal Nanoparticle ◽  
Nf Kappa B

scholarly journals The Role of TLR and Chemokine in Wear Particle-Induced Aseptic Loosening

2012 ◽  
Vol 2012 ◽  
pp. 1-9 ◽  
Author(s):  
Qiaoli Gu ◽  
Qin Shi ◽  
Huilin Yang
Keyword(s):  
Inflammatory Response ◽  
Aseptic Loosening ◽  
Osteoclast Differentiation ◽  
Adaptor Protein ◽  
Wear Particle ◽  
Cellular Migration ◽  
Cellular Interaction ◽  
Wear Particles ◽  
Orthopaedic Implants ◽  
Inhibitory Protein

Wear particle-induced periprosthetic osteolysis remains the principal cause of aseptic loosening of orthopaedic implants. Monocytes/macrophages phagocytose wear particles and release cytokines that induce inflammatory response. This response promotes osteoclast differentiation and osteolysis. The precise mechanisms by which wear particles are recognized and induce the accumulation of inflammatory cells in the periprosthetic tissue have not been fully elucidated. Recent studies have shown that toll-like receptors (TLRs) contribute to the cellular interaction with wear particles. Wear particles are recognized by monocytes/macrophages through TLRs coupled with the adaptor protein MyD88. After the initial interaction, wear particles induce both local and systemic migration of monocytes/macrophages to the periprosthetic region. The cellular migration is mediated through chemokines including interleukin-8, macrophage chemotactic protein-1, and macrophage inhibitory protein-1 in the periprosthetic tissues. Interfering with chemokine-receptor axis can inhibit cellular migration and inflammatory response. This paper highlights recent advances in TLR, and chemokine participated in the pathogenesis of aseptic loosening. A comprehensive understanding of the recognition and migration mechanism is critical to the development of measures that prevent wear particle-induced aseptic loosening of orthopaedic implants.

scholarly journals Hyaluronan fragments activate an NF-kappa B/I-kappa B alpha autoregulatory loop in murine macrophages.

1996 ◽  
Vol 183 (5) ◽  
pp. 2373-2378 ◽  
Author(s):  
P W Noble ◽  
C M McKee ◽  
M Cowman ◽  
H S Shin
Keyword(s):  
Molecular Weight ◽  
Dna Binding ◽  
Inflammatory Response ◽  
Time Course ◽  
Inflammatory Responses ◽  
Binding Activity ◽  
Nf Kappa B ◽  
Murine Macrophages ◽  
I Kappa B Alpha ◽  
Dna Binding Activity

Macrophages play an important role in the acute tissue inflammatory response through the release of cytokines and growth factors in response to stimuli such as lipopolysaccharide (LPS). Macrophage inflammatory effector functions are also influenced by interactions with the extracellular matrix (ECM). Such macrophage-ECM interactions may be important in regulating chronic inflammatory responses. Recent evidence has suggested that hyaluronan (HA), a glycosaminoglycan (GAG) component of ECM can induce inflammatory gene expression in murine macrophages. HA exists in its native form as a large polymer, but is found as smaller fragments under inflammatory conditions. The NF-kappa B/I-kappa B transcriptional regulatory system has been shown to be a critical component of the host inflammatory response. We examined the effects of high molecular weight HA and lower molecular weight HA fragments on NF-kappa B activation in mouse macrophages. Only the smaller HA fragments were found to activate NF-kappa B DNA binding activity. After HA stimulation, I-kappa B alpha mRNA was induced and I-kappa B alpha protein levels, which initially decreased, were restored. The induction of I-kappa Balpha expression was not observed for other GAGs. The time course of I-kappa B alpha protein regeneration in response to HA fragments was consistent with an autoregulatory mechanism. In support of this mechanism, in vitro translated murine I-kappa B alpha inhibited HA fragment-induced NF-kappa B DNA binding activity. The NF-kappa B DNA binding complex in HA-stimulated extracts was found to contain p50 and p65 subunits. Activation of the NF-kappa B/I-kappa B system in macrophages by ECM fragments may be an important mechanism for propagating the tissue inflammatory response.

scholarly journals Inhibition of endothelial cell activation by adenovirus-mediated expression of I kappa B alpha, an inhibitor of the transcription factor NF-kappa B.

1996 ◽  
Vol 183 (3) ◽  
pp. 1013-1022 ◽  
Author(s):  
C J Wrighton ◽  
R Hofer-Warbinek ◽  
T Moll ◽  
R Eytner ◽  
F H Bach ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Cell Adhesion ◽  
Inflammatory Response ◽  
Recombinant Adenovirus ◽  
Ectopic Expression ◽  
Specific Inhibitor ◽  
Transcriptional Level ◽  
Nf Kappa B ◽  
Xenograft Rejection ◽  
I Kappa B Alpha

During the inflammatory response, endothelial cells (EC) transiently upregulate a set of genes encoding, among others, cell adhesion molecules and chemotactic cytokines that together mediate the interaction of the endothelium with cells of the immune system. Gene upregulation is mediated predominantly at the transcriptional level and in many cases involves the transcription factor nuclear factor (NF) kappa B. We have tested the concept of inhibiting the inflammatory response by overexpression of a specific inhibitor of NF-kappaB, I kappa B alpha. A recombinant adenovirus expressing I kappa B alpha was constructed (rAd.I kappa B alpha) and used to infect EC of human and porcine origin. Ectopic expression of IkappaBalpha resulted in marked, and in some cases complete, reduction of the expression of several markers of EC activation, including vascular cell adhesion molecule 1, interleukins 1, 6, 8, and tissue factor. Overexpressed I kappa B alpha inhibited NF-kappa B specifically since (a) in electrophoretic mobility shift assay, NF-kappa B but not AP-1 binding activity was inhibited, and (b) von Willebrand factor and prostacyclin secretion that occur independently of NF-kappa B, remained unaffected. Functional studies of leukocyte adhesion demonstrated strong inhibition of HL-60 adhesion to I kappa B alpha-expressing EC. These findings suggest that NF-kappa B could be an attractive target for therapeutic intervention in a variety of inflammatory diseases, including xenograft rejection.

Retinoic acid abrogates LPS-induced inflammatory response via negative regulation of NF-kappa B/miR-21 signaling

2021 ◽  
pp. 1-10
Author(s):  
Queen Intan Nurrahmah ◽  
Radha Madhyastha ◽  
Harishkumar Madhyastha ◽  
Bethasiwi Purbasari ◽  
Masugi Maruyama ◽  
...  
Keyword(s):  
Retinoic Acid ◽  
Inflammatory Response ◽  
Negative Regulation ◽  
Nf Kappa B

P2-191: RATANASAMPIL SUPPRESSES THE HYPOXIA-REOXYGENATION-INDUCED INFLAMMATORY RESPONSE THROUGH INHIBITING NF-KAPPA B ACTIVATION IN MICROGLIA

2006 ◽  
Vol 14 (7S_Part_14) ◽  
pp. P742-P742
Author(s):  
Jie Meng ◽  
Aiqin Zhu ◽  
Junjun Ni ◽  
Hiroshi Nakanishi ◽  
Zhou Wu
Keyword(s):  
Inflammatory Response ◽  
Nf Kappa B ◽  
Hypoxia Reoxygenation

PARTHENOLIDE, AN INHIBITOR OF NF-KAPPA B, REDUCES THE INFLAMMATORY RESPONSE IN HEMORRHAGICK SHOCK IN THE RAT

Shock ◽  
2004 ◽  
Vol 21 (Supplement) ◽  
pp. 27
Author(s):  
Basilia Zingarelli ◽  
Paul Hake ◽  
Timothy Burroughs ◽  
Michael OʼConnor
Keyword(s):  
Inflammatory Response ◽  
Nf Kappa B

Gut permeabillity and nitric oxide: Evidence for an endotoxin mediated inflammatory response in severe acute pancreatitis

2001 ◽  
Vol 120 (5) ◽  
pp. A468-A469
Author(s):  
S RAHMAN ◽  
B AMMORI ◽  
I MARTIN ◽  
G BARCLAY ◽  
M LARVIN ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Acute Pancreatitis ◽  
Inflammatory Response ◽  
Severe Acute Pancreatitis
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