Oxidative Stress and Advanced Glycation End Products in Hashimoto's Thyroiditis

Thyroid ◽  
2016 ◽  
Vol 26 (4) ◽  
pp. 504-511 ◽  
Author(s):  
Rosaria M. Ruggeri ◽  
Teresa M. Vicchio ◽  
Mariateresa Cristani ◽  
Rosaria Certo ◽  
Daniela Caccamo ◽  
...  
2021 ◽  
pp. 1-7
Author(s):  
Tommaso Aversa ◽  
Rosaria Maddalena Ruggeri ◽  
Domenico Corica ◽  
Maria Teresa Cristani ◽  
Giorgia Pepe ◽  
...  

<b><i>Objective:</i></b> No data are available on advanced glycation end products (AGEs) and their soluble receptor (sRAGE) in pediatric patients with Hashimoto’s thyroiditis (HT). The present study was aimed to simultaneously evaluate serum levels of sRAGE, AGEs, and advanced oxidation protein products (AOPPs) and investigate the relationships between these oxidative stress markers and clinical and biochemical parameters of thyroid function in euthyroid children with HT. <b><i>Design:</i></b> This is a case-control study carried out in a single university hospital center. <b><i>Methods:</i></b> We enrolled 19 newly diagnosed euthyroid HT pediatric patients (3 M, 16 F; median age 12.44 years, range 6.54–15.81 years) and 16 age-, sex-, and BMI-matched healthy controls (5 M, 11 F; median age 12.83 years, range 5.68–15.07 years). None was on levothyroxine treatment. The exclusion criteria were autoimmune, inflammatory, and infection comorbidities. Patients did not differ significantly from controls with regard to lipid or for anthropometric parameters. <b><i>Results:</i></b> sRAGE levels were significantly lower in HT patients (median 414.30 pg/mL, range 307.30–850.30 pg/mL) than in controls (561.30, 273.20–1121.60 pg/mL; <i>p</i> = 0.034). No differences emerged between patients and controls with regard to serum AGEs (124.25 AU/g prot, 71.98–186.72 vs. 133.90, 94.06–200.78 AU/g prot, <i>p</i> = 0.707) and AOPPs (1.13 nmol/mL, 0.62–1.83 vs. 1.17, 0.76–1.42 nmol/mL, <i>p</i> = 0.545). <b><i>Conclusions:</i></b> sRAGE levels were decreased in euthyroid children/adolescents at the onset of HT, suggesting that autoimmunity per se seems to play an important role in such a reduction of sRAGE, irrespective of any functional alteration. Children and adolescents suffering from HT may exhibit increased susceptibility to oxidative damage, even when in euthyroid status.


2015 ◽  
Vol 2015 ◽  
pp. 1-7 ◽  
Author(s):  
A. Hatzioannou ◽  
I. Kanistras ◽  
E. Mantzou ◽  
E. Anastasiou ◽  
M. Peppa ◽  
...  

Advanced glycation end products (AGEs) are formed on proteins after exposure to high concentrations of glucose and modify protein’s immunogenicity. Herein, we investigated whether the modification of thyroglobulin (Tg) by AGEs influences its antigenicity and immunogenicity. Human Tg was incubatedin vitrowith increasing concentrations of D-glucose-6-phosphate in order to produce Tgs with different AGE content (AGE-Tg). Native Tg and AGE-Tgs were used in ELISA to assess the serum antibody reactivity of two patient groups, pregnant women with gestational diabetes (GDM), and patients with Hashimoto’s thyroiditis (HT). We producedin vitroAGE-Tg with low and high AGE content, 13 and 49 AGE units/mg Tg, respectively. All HT patients’ sera presented the same antibody reactivity profile against native Tg and AGE-Tgs, indicating that the modification of Tg by AGEs did not alter its antigenicity. Similarly, the GDM patients’ sera did not discriminate among the two forms of Tg, native or artificially glycated, suggesting that the modification of Tg by AGEs might not alter its immunogenicity. The modification of Tg by AGEs has no obvious effect on neither its antigenicity nor, most likely, its immunogenicity. It seems that other Tg modifications might account for the production of aTgAbs in patients with GDM.


2021 ◽  
Author(s):  
Akio Nakamura ◽  
Ritsuko Kawahrada

Protein glycation is the random, nonenzymatic reaction of sugar and protein induced by diabetes and ageing; this process is quite different from glycosylation mediated by the enzymatic reactions catalysed by glycosyltransferases. Schiff bases form advanced glycation end products (AGEs) via intermediates, such as Amadori compounds. Although these AGEs form various molecular species, only a few of their structures have been determined. AGEs bind to different AGE receptors on the cell membrane and transmit signals to the cell. Signal transduction via the receptor of AGEs produces reactive oxygen species in cells, and oxidative stress is responsible for the onset of diabetic complications. This chapter introduces the molecular mechanisms of disease onset due to oxidative stress, including reactive oxygen species, caused by AGEs generated by protein glycation in a hyperglycaemic environment.


2010 ◽  
Vol 58 (20) ◽  
pp. 11119-11129 ◽  
Author(s):  
Deena Ramful ◽  
Evelyne Tarnus ◽  
Philippe Rondeau ◽  
Christine Robert Da Silva ◽  
Theeshan Bahorun ◽  
...  

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