A5064938738- Glycosylation and Glycoproteins Research
- Diabetes and associated disorders
- Galectins and Cancer Biology
- Pancreatic function and diabetes
- Monoclonal and Polyclonal Antibodies Research
- Carbohydrate Chemistry and Synthesis
- Hyperglycemia and glycemic control in critically ill and hospitalized patients
- Advanced Proteomics Techniques and Applications
- Diabetes Management and Research
- Sepsis Diagnosis and Treatment
- Diabetes Treatment and Management
- Proteoglycans and glycosaminoglycans research
- Pancreatitis Pathology and Treatment
- Pancreatic and Hepatic Oncology Research
- Diabetic Foot Ulcer Assessment and Management
- Epigenetics and DNA Methylation
- Mass Spectrometry Techniques and Applications
- Diet, Metabolism, and Disease
- Lysosomal Storage Disorders Research
- Chronic Lymphocytic Leukemia Research
- Protease and Inhibitor Mechanisms
- Erythrocyte Function and Pathophysiology
- Peptidase Inhibition and Analysis
- Complement system in diseases
- Immune Cell Function and Interaction
University of Zagreb
2016-2025
Genos (Croatia)
2019-2022
University of Split
2008-2022
Science Research Laboratory
2019-2021
University of Edinburgh
2015
All immunoglobulin G molecules carry N-glycans, which modulate their biological activity. Changes in N-glycosylation of IgG associate with various diseases and affect the activity therapeutic antibodies intravenous immunoglobulins. We have developed a novel 96-well protein monolithic plate used it to rapidly isolate from plasma 2298 individuals three isolated human populations. N-glycans were released by PNGase F, labeled 2-aminobenzamide analyzed hydrophilic interaction chromatography...
Fine structural details of glycans attached to the conserved N-glycosylation site significantly not only affect function individual immunoglobulin G (IgG) molecules but also mediate inflammation at systemic level. By analyzing IgG glycosylation in 5,117 individuals from four European populations, we have revealed very complex patterns changes with age. Several (including FA2B, FA2G2, and FA2BG2) changed considerably age combination these three can explain up 58% variance chronological age,...
Objective Glycans attached to the Fc portion of IgG are important modulators effector functions. Interindividual differences in glycome composition large and they associate strongly with different inflammatory autoimmune diseases. IKZF1 , HLA–DQ2A/B BACH2 genetic loci that affect show pleiotropy systemic lupus erythematosus (SLE), indicating a potentially causative role aberrant glycosylation SLE. We undertook this multicenter case–control study determine whether SLE is associated altered...
Abstract Epigenetic alterations may provide important insights into gene-environment interaction in inflammatory bowel disease (IBD). Here we observe epigenome-wide DNA methylation differences 240 newly-diagnosed IBD cases and 190 controls. These include 439 differentially methylated positions (DMPs) 5 regions (DMRs), which study detail using whole genome bisulphite sequencing. We replicate the top DMP ( RPS6KA2 ) DMRs VMP1, ITGB2 TXK an independent cohort. Using paired genetic epigenetic...
Over half of all proteins are glycosylated, and alterations in glycosylation have been observed numerous physiological pathological processes. Attached glycans significantly affect protein function; but, contrary to polypeptides, they not directly encoded by genes, the complex processes that regulate their assembly poorly understood. A novel approach combining genome-wide association high-throughput glycomics analysis 2,705 individuals three population cohorts showed common variants...
Plasma glycans were analyzed in 1008 individuals to evaluate variability and heritability, as well the main environmental determinants that affect glycan structures. By combining HPLC analysis of fluorescently labeled with sialidase digestion, separated into 33 chromatographic peaks quantified. A high level was observed median ratio minimal maximal values 6.17 significant age- gender-specific differences. Heritability estimates for individual varied widely, ranging from very low high....
Protein glycosylation affects nearly all molecular interactions at the cell surface and in intercellular space. Many of physiological variations which are part homeostatic mechanisms influence glycosylation. However, a comprehensive overview changes caused by aging common lifestyle parameters is still lacking. After analyzing N-glycans plasma 1914 individuals from Croatian islands Vis Korčula, we performed analysis dependence different features (position fucose, level galactosylation,...
Glycobiology is an underexplored research area in inflammatory bowel disease (IBD), and glycans are relevant to many etiological mechanisms described IBD. Alterations N-glycans attached the immunoglobulin G (IgG) Fc fragment can affect molecular structure immunological function. Recent genome-wide association studies reveal pleiotropy between IBD IgG glycosylation. This study aims explore glycan changes ulcerative colitis (UC) Crohn's (CD).IgG glycome composition patients with UC (n = 507),...
The biological and clinical relevance of glycosylation is becoming increasingly recognized, leading to a growing interest in large-scale population-based studies. In the past few years, several methods for high-throughput analysis glycans have been developed, but thorough validation standardization these required before significant resources are invested this study, we compared liquid chromatography, capillary gel electrophoresis, two MS quantitative profiling N-glycosylation IgG same data...
Glycan heterogeneity was shown to be associated with numerous diseases and glycan analysis has a great diagnostic potential. Recently, we reported high biological variability of human plasma N-glycome at the level population. The observed variations were larger than changes some diseases; thus, it importance examine temporal constancy before glycosylation could routinely analyzed in laboratories. Plasma samples taken from 12 healthy individuals. blood drawn on seven occasions during 5 days....
Recovery after cardiac surgery is a complex process that has to compensate for both individual variability and extensive tissue damage in the context of systemic inflammation. Protein glycosylation essential many steps inflammatory cascade, but due technological limitations role variation inflammation not been addressed until now. We analysed composition total plasma IgG N-glycomes 107 patients undergoing surgery. In nearly all individuals N-glycome underwent same pattern changes first 72 h,...
Rising awareness of the universal importance protein N-glycosylation governs development further advances in N-glycan analysis. Nowadays it is well known that correct glycosylation essential for proper function, which emanates from its important role many physiological processes. Furthermore, involved inpathophysiology multiple common complex diseases. In vast majority cases, profiles are analyzed enzymatically released glycans, can be derivatized order to enhance sensitivity Techniques...
Poorer glycemic control in type 1 diabetes may alter N-glycosylation patterns on circulating glycoproteins, and these alterations be linked with diabetic kidney disease (DKD). We investigated associations between N-glycans renal function diabetes.Using serum samples from 818 adults who were considered to have extreme annual loss estimated glomerular filtration rate (eGFR; i.e., slope) based retrospective clinical records, among 6,127 the Scottish Diabetes Research Network Type Bioresource...
Plasma protein N-glycan profiling integrates information on enzymatic glycosylation, which is a highly controlled ubiquitous posttranslational modification. Here we investigate the ability of plasma N-glycome to predict incidence type 2 diabetes and cardiovascular diseases (CVDs; i.e., myocardial infarction stroke).Based prospective European Prospective Investigation Cancer (EPIC)-Potsdam cohort (n = 27,548), constructed case-cohorts including random subsample 2,500 participants all...
Glycans expand the structural complexity of proteins by several orders magnitude, resulting in a tremendous analytical challenge when including them biomedical research. Recent glycobiological research is painting picture which glycans represent crucial and functional component majority proteins, with alternative glycosylation lipids being an important regulatory mechanism many biological pathological processes. Since interindividual differences are extensive, large studies needed to map...
A recent genome-wide association study identified hepatocyte nuclear factor 1-α (HNF1A) as a key regulator of fucosylation. We hypothesized that loss-of-function HNF1A mutations causal for maturity-onset diabetes the young (MODY) would display altered fucosylation N-linked glycans on plasma proteins and glycan biomarkers could improve efficiency diagnosis HNF1A-MODY. In pilot comparison 33 subjects with HNF1A-MODY 41 type 2 diabetes, 15 29 measurements differed between two groups. The...
ObjectiveTo determine the extent to which genetic and epigenetic factors contribute variations in glycosylation of immunoglobulin G (IgG) humans. Methods76 N-glycan traits circulating IgG were analyzed by UPLC 220 monozygotic 310 dizygotic twin pairs from TwinsUK. A classical study design was used derive additive genetic, common unique environmental components defining variance these traits. Epigenome-wide association analysis performed using Illumina 27k chip. Results51 76 glycan studied...
The majority of human proteins are post-translationally modified by covalent addition one or more complex oligosaccharides (glycans). Alterations in glycosylation processing associated with numerous diseases and glycans attracting increasing attention both as disease biomarkers targets for novel therapeutic approaches. Using a recently developed high-throughput high-performance liquid chromatography (HPLC) analysis method, we have reported, pilot genome-wide association study 13 glycan...