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Clinical aspects of protein glycation

100%
Sabina Galiniak S., Izabela Krawczyk-Marć I., Anna Sęk-Mastej A., Natalia Leksa N., Marek Biesiadecki M., Stanisław Orkisz S.
European Journal of Clinical and Experimental Medicine
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2017
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issue 3
263-267
EN
Introduction. Glycation is a post-translational modification of proteins that depends on the non-enzymatic linkage of a ketone or aldehyde group of sugar with a free amino group of protein. Pathological effects of this process are observed in many disease states under conditions of hyperglycemia, in diabetic complications, and neurodegenerative diseases such as multiple sclerosis. Aim. In this paper we present the characteristics of the glycation process, its consequences, as well as a review of current knowledge about the role of glycation in multiple sclerosis. Material and methods. The databases EBSCO, PubMed, ScienceDirect and SpringerLink were used to search the literature. Analysis of the literature. Intermediate glycation products form a number of derivatives that contribute to oxidative stress and structural changes in the proteins, including induction of aggregation or reduction of affinity for drug proteins. Glucose products may contribute to neurodegenerative changes in patients with multiple sclerosis. Determination of protein glycation products can be successfully used to evaluate the course of multiple sclerosis as a diagnostic marker.
2

Advanced glycation end products in the plasma and renal tissues in experimental model of unilateral renal artery stenosis

88%
Brańska J., Kruszewski K., Jarocka I., Tarasik A., Ostrowska H.
Progress in Health Sciences
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2012
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vol. 2
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issue 2
125-129
EN
Purpose: To evaluate whether advanced glycation end products (AGE) levels are increased in the plasma and renal tissues of rats after unilateral renal artery stenosis (RAS). Materials and methods: AGE levels were measured using commercially available ELISA kit in plasma and renal tissue samples obtained from 16 rats with experimental induced RAS for 3 and 28 days and from 6 respective sham-operated control rats. We also analyzed by HPLC the concentration of 4-hydroxynonenal (4-HNE), a known inducer of AGE formation and accumulation. Results: Plasma concentrations of 4-HNE and AGE were significantly increased (p<0.05) after 28 days of RAS. At this time point, the concentration of AGE was markedly increased in the clipped atrophic kidney (by about 10-fold; p<0.05), but it was unchanged in the contralateral kidney of the same rats. No differences in plasma and renal AGE levels were detected at day 3 of RAS. Sham operation did not affect the levels of AGE and 4-HNE at each time point. Conclusions: Increased accumulation of AGE both in the plasma and in the ischemic atrophic kidney suggest that AGE levels can be used as a reliable biomarker for monitoring the development of ischemic nephropathy caused by renal artery stenosis.
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