Fibrinogen Fucosylation as a Prognostic Marker of End-Stage Renal Disease in Patients on Peritoneal Dialysis
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...
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creator | Baralic, Marko Gligorijevic, Nikola Brkovic, Voin Katrlik, Jaroslav Pazitna, Lucia Sunderic, Milos Miljus, Goran Penezic, Ana Dobrijevic, Zorana Lausevic, Mirjana Nedic, Olgica Robajac, Dragana |
description | 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 gamma 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. |
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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 gamma 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.</description><identifier>ISSN: 2218-273X</identifier><identifier>EISSN: 2218-273X</identifier><identifier>DOI: 10.3390/biom10081165</identifier><identifier>PMID: 32784866</identifier><language>eng</language><publisher>BASEL: Mdpi</publisher><subject>Aged ; Aged, 80 and over ; Anticoagulants ; Binding sites ; Biochemistry & Molecular Biology ; Biomarkers - blood ; carbohydrates ; Cardiovascular diseases ; Continuous ambulatory peritoneal dialysis ; End-stage renal disease ; Enzymes ; ESRD ; Female ; Fibrinogen ; Fibrinogen - chemistry ; Fibrinogen - metabolism ; fibrinogen chains ; Fucose - metabolism ; Glycoproteins ; Glycosylation ; Health aspects ; Humans ; Kidney diseases ; Kidney Failure, Chronic - blood ; Kidney Failure, Chronic - metabolism ; Kidney Failure, Chronic - pathology ; lectin-based microarray ; Lectins ; Lectins - blood ; Lectins - chemistry ; Life Sciences & Biomedicine ; Lysis ; Male ; Middle Aged ; N-glycans ; Patient outcomes ; Peritoneal Dialysis ; Peritoneum ; Peritonitis ; Platelet aggregation ; Polysaccharides ; Polysaccharides - blood ; Polysaccharides - chemistry ; Polysaccharides - metabolism ; Prognosis ; Protein Array Analysis ; Protein structure ; Proteins ; Science & Technology ; Software</subject><ispartof>Biomolecules (Basel, Switzerland), 2020-08, Vol.10 (8), p.1165, Article 1165</ispartof><rights>COPYRIGHT 2020 MDPI AG</rights><rights>2020. This work is licensed under http://creativecommons.org/licenses/by/3.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2020 by the authors. 2020</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>true</woscitedreferencessubscribed><woscitedreferencescount>9</woscitedreferencescount><woscitedreferencesoriginalsourcerecordid>wos000577923000001</woscitedreferencesoriginalsourcerecordid><citedby>FETCH-LOGICAL-c506t-df5b8a500bffe38a891c04d23c4e5075bb4a0d1fb01187f77dd67cbe3cacee723</citedby><cites>FETCH-LOGICAL-c506t-df5b8a500bffe38a891c04d23c4e5075bb4a0d1fb01187f77dd67cbe3cacee723</cites><orcidid>0000-0001-5585-9793 ; 0000-0002-4652-7719 ; 0000-0003-2042-0056 ; 0000-0002-6423-4645 ; 0000-0002-0940-9481 ; 0000-0002-8691-2486 ; 0000-0002-2876-9298</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7466146/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7466146/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,315,728,781,785,865,886,2103,2115,27929,27930,28253,53796,53798</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/32784866$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Baralic, Marko</creatorcontrib><creatorcontrib>Gligorijevic, Nikola</creatorcontrib><creatorcontrib>Brkovic, Voin</creatorcontrib><creatorcontrib>Katrlik, Jaroslav</creatorcontrib><creatorcontrib>Pazitna, Lucia</creatorcontrib><creatorcontrib>Sunderic, Milos</creatorcontrib><creatorcontrib>Miljus, Goran</creatorcontrib><creatorcontrib>Penezic, Ana</creatorcontrib><creatorcontrib>Dobrijevic, Zorana</creatorcontrib><creatorcontrib>Lausevic, Mirjana</creatorcontrib><creatorcontrib>Nedic, Olgica</creatorcontrib><creatorcontrib>Robajac, Dragana</creatorcontrib><title>Fibrinogen Fucosylation as a Prognostic Marker of End-Stage Renal Disease in Patients on Peritoneal Dialysis</title><title>Biomolecules (Basel, Switzerland)</title><addtitle>BIOMOLECULES</addtitle><addtitle>Biomolecules</addtitle><description>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 gamma 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.</description><subject>Aged</subject><subject>Aged, 80 and over</subject><subject>Anticoagulants</subject><subject>Binding sites</subject><subject>Biochemistry & Molecular Biology</subject><subject>Biomarkers - blood</subject><subject>carbohydrates</subject><subject>Cardiovascular diseases</subject><subject>Continuous ambulatory peritoneal dialysis</subject><subject>End-stage renal disease</subject><subject>Enzymes</subject><subject>ESRD</subject><subject>Female</subject><subject>Fibrinogen</subject><subject>Fibrinogen - chemistry</subject><subject>Fibrinogen - metabolism</subject><subject>fibrinogen chains</subject><subject>Fucose - metabolism</subject><subject>Glycoproteins</subject><subject>Glycosylation</subject><subject>Health aspects</subject><subject>Humans</subject><subject>Kidney diseases</subject><subject>Kidney Failure, Chronic - 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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 gamma 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.</abstract><cop>BASEL</cop><pub>Mdpi</pub><pmid>32784866</pmid><doi>10.3390/biom10081165</doi><tpages>12</tpages><orcidid>https://orcid.org/0000-0001-5585-9793</orcidid><orcidid>https://orcid.org/0000-0002-4652-7719</orcidid><orcidid>https://orcid.org/0000-0003-2042-0056</orcidid><orcidid>https://orcid.org/0000-0002-6423-4645</orcidid><orcidid>https://orcid.org/0000-0002-0940-9481</orcidid><orcidid>https://orcid.org/0000-0002-8691-2486</orcidid><orcidid>https://orcid.org/0000-0002-2876-9298</orcidid><oa>free_for_read</oa></addata></record> |
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subjects | Aged Aged, 80 and over Anticoagulants Binding sites Biochemistry & Molecular Biology Biomarkers - blood carbohydrates Cardiovascular diseases Continuous ambulatory peritoneal dialysis End-stage renal disease Enzymes ESRD Female Fibrinogen Fibrinogen - chemistry Fibrinogen - metabolism fibrinogen chains Fucose - metabolism Glycoproteins Glycosylation Health aspects Humans Kidney diseases Kidney Failure, Chronic - blood Kidney Failure, Chronic - metabolism Kidney Failure, Chronic - pathology lectin-based microarray Lectins Lectins - blood Lectins - chemistry Life Sciences & Biomedicine Lysis Male Middle Aged N-glycans Patient outcomes Peritoneal Dialysis Peritoneum Peritonitis Platelet aggregation Polysaccharides Polysaccharides - blood Polysaccharides - chemistry Polysaccharides - metabolism Prognosis Protein Array Analysis Protein structure Proteins Science & Technology Software |
title | Fibrinogen Fucosylation as a Prognostic Marker of End-Stage Renal Disease in Patients on Peritoneal Dialysis |
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