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Abstract
Glycosylation may strongly affect protein structure and functions. A high risk of cardiovascular complications seen in patients with end-stage renal disease (ESRD) is, at least partly associated with delayed clot formation, increased clot strength, and delayed cloth lysis. Taking into consideration that fibrinogen mediates these processes, we isolated fibrinogen from the plasma from patients with ESRD on peritoneal dialysis (ESRD-PD), and examined glycosylation of native fibrinogen and its subunits by lectin-based microarray and lectin blotting. Compared to healthy controls, fibrinogen from patients had increased levels of A2BG2 and decreased levels of FA2 glycan. The distribution of glycans on individual chains was also affected, with the γ chain, responsible for physiological functions of fibrinogen (such as coagulation and platelet aggregation), being most prone to these alterations. Increased levels of multi-antennary N-glycans in ESRD-PD patients were also associated with the type of dialysis solutions, whereas an increase in the fucosylation levels was strongly related to the peritoneal membrane damage. Consequently, investigation of fibrinogen glycans can offer better insight into fibrinogen-related complications observed in ESRD-PD patients and, additionally, contribute to prognosis, choice of personalised therapy, determination of peritoneal membrane damage, and the length of utilization of peritoneum for dialysis.
Highlights
Glycoconjugates are complex structures formed after enzyme-catalysed binding of carbohydrates to proteins, lipids, or nucleic acids [1]
Peritoneal dialysis (PD) is a type of treatment for some patients with end-stage renal disease (ESRD) in which the peritoneum is used as a natural membrane through which osmosis and diffusion take place, eliminating the harmful products of metabolism and excess fluid
Altered glycosylation affects fibrinogen properties in hepatic diseases [9,10] and the present study aimed to examine fibrinogen glycosylation in patients with ESRD on peritoneal dialysis (ESRD-PD), as that may help in better understanding of the mechanisms underlying fibrinogen-related changes, and possibly assist in the therapeutic approach
Summary
Glycoconjugates are complex structures formed after enzyme-catalysed binding of carbohydrates to proteins, lipids, or nucleic acids [1]. Lectins are often used to assess the glycan content, as they recognise and interact with individual mono/oligosaccharides or more complex structures (e.g., glycans). These interactions depend on the lectin structure, its binding site and organization, and lectin multivalence [2]. Delayed clot formation, decreased lysis, and increased clot strength, as well as hypercoagulability found in patients with CKD, are to some extent mediated by fibrinogen [6] This key component of the blood clotting process is a 340 kDa homodimer, consisting of two sets of three polypeptide chains (AαBβγ) that are O- and/or N-glycosylated. Fibrinogen is abundantly O-glycosylated at various sites on the Aα chain and only at one site on the Bβ chain [7,8]
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