scholarly journals Advanced glycation end products regulate anabolic and catabolic activities via NLRP3-inflammasome activation in human nucleus pulposus cells

2017 ◽  
Vol 21 (7) ◽  
pp. 1373-1387 ◽  
Author(s):  
Yu Song ◽  
Yan Wang ◽  
Yukun Zhang ◽  
Wen Geng ◽  
Wei Liu ◽  
...  
Keyword(s):  
Nucleus Pulposus ◽  
Advanced Glycation End Products ◽  
Nlrp3 Inflammasome ◽  
Inflammasome Activation ◽  
Advanced Glycation ◽  
Nucleus Pulposus Cells ◽  
Nlrp3 Inflammasome Activation ◽  
Glycation End Products ◽  
End Products

scholarly journals Activation of NLRP3 Inflammasome by Advanced Glycation End Products Promotes Pancreatic Islet Damage

2017 ◽  
Vol 2017 ◽  
pp. 1-11 ◽  
Author(s):  
Xiang Kong ◽  
Ai-Ling Lu ◽  
Xin-Ming Yao ◽  
Qiang Hua ◽  
Xiao-Yong Li ◽  
...  
Keyword(s):  
Type 2 Diabetes ◽  
Pancreatic Islet ◽  
Advanced Glycation End Products ◽  
Nlrp3 Inflammasome ◽  
Inflammasome Activation ◽  
Advanced Glycation ◽  
Age Related ◽  
Glycation End Products ◽  
End Products

Accumulation of advanced glycation end products (AGEs) contributes to ageing and age-related diseases, especially type 2 diabetes. The NLRP3 inflammasome, as a vital component of the innate immune system, is implicated in the pathogenesis of type 2 diabetes. However, the role of the NLRP3 inflammasome in AGE-induced pancreatic islet damage remains largely unclear. Results showed that administration of AGEs (120 mg/kg for 6 weeks) in C57BL/6J mice induced an abnormal response to glucose (as measured by glucose tolerance and insulin release), pancreaticβ-cell ultrastructural lesion, and cell death. These effects were associated with an excessive superoxide anion level, significant increased protein expression levels for NADPH oxidase 2 (NOX2), thioredoxin-interacting protein (TXNIP), NLRP3, and cleaved IL-1β, enhanced caspase-1 activity, and a significant increase in the levels of TXNIP–NLRP3 protein interaction. Ablation of the NLRP3 inflammasome or treatment with antioxidantN-acetyl-cysteine (NAC) clearly ameliorated these effects. In conclusion, our results reveal a possible mechanism for AGE-induced pancreatic islet damage upon NLRP3 inflammasome activation.

scholarly journals Advanced glycation end products in degenerative nucleus pulposus with diabetes

2013 ◽  
Vol 32 (2) ◽  
pp. 238-244 ◽  
Author(s):  
Tsung-Ting Tsai ◽  
Natalie Yi-Ju Ho ◽  
Ying-Ting Lin ◽  
Po-Liang Lai ◽  
Tsai-Sheng Fu ◽  
...  
Keyword(s):  
Nucleus Pulposus ◽  
Advanced Glycation End Products ◽  
Advanced Glycation ◽  
Glycation End Products ◽  
End Products

scholarly journals Advanced glycation end products impair NLRP3 inflammasome–mediated innate immune responses in macrophages

2017 ◽  
Vol 292 (50) ◽  
pp. 20437-20448 ◽  
Author(s):  
Seunghwan Son ◽  
Inhwa Hwang ◽  
Seung Hyeok Han ◽  
Jeon-Soo Shin ◽  
Ok Sarah Shin ◽  
...  
Keyword(s):  
Immune Responses ◽  
Advanced Glycation End Products ◽  
Nlrp3 Inflammasome ◽  
Innate Immune ◽  
Innate Immune Responses ◽  
Advanced Glycation ◽  
Glycation End Products ◽  
End Products

Advanced glycation end-products downregulating intervertebral disc cell production of proteoglycans in vitro

2006 ◽  
Vol 5 (4) ◽  
pp. 324-329 ◽  
Author(s):  
Kimiaki Yokosuka ◽  
Jin Soo Park ◽  
Kotaro Jimbo ◽  
Kei Yamada ◽  
Kimiaki Sato ◽  
...  
Keyword(s):  
Intervertebral Disc ◽  
Nucleus Pulposus ◽  
Disc Degeneration ◽  
Advanced Glycation End Products ◽  
Immunohistochemical Analysis ◽  
Enzyme Linked Immunosorbent Assay ◽  
Advanced Glycation ◽  
Collagen Types ◽  
Glycation End Products ◽  
End Products

Object The authors sought to clarify the role, if any, of advanced glycation end-products (AGEs) in disc degeneration. Methods Intervertebral discs were analyzed for the presence of AGEs and of their receptor (RAGE) by immunohistochemical analysis. Reverse transcriptase polymerase chain reaction (RT-PCR) was performed to detect any RAGE gene expression, and real-time PCR was used to quantify messenger RNA (mRNA) levels of aggrecan and collagen types I and II in nucleus pulposus cells treated with AGEs. Aggrecan protein concentration was determined by enzyme-linked immunosorbent assay. Immunohistochemical analysis revealed that AGEs and RAGE were localized in the nucleus pulposus of the intervertebral disc. Advanced glycation end-products were found to significantly suppress the expression of aggrecan at both mRNA and protein levels in a dose- and time-dependent manner. The levels of collagen types I and II remained unchanged after treatments with AGEs. Conclusions These results suggest that the accumulation of AGEs and their interaction with their receptor in the nucleus pulposus might result in the downregulation of aggrecan production responsible for disc degeneration.

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