A5003222189- Glycosylation and Glycoproteins Research
- Monoclonal and Polyclonal Antibodies Research
- Diabetes and associated disorders
- Galectins and Cancer Biology
- Pancreatic function and diabetes
- Epigenetics and DNA Methylation
- Diet, Metabolism, and Disease
- T-cell and B-cell Immunology
- Advanced Proteomics Techniques and Applications
- Mass Spectrometry Techniques and Applications
- Carbohydrate Chemistry and Synthesis
- Chronic Lymphocytic Leukemia Research
- Genomics and Phylogenetic Studies
- Machine Learning in Bioinformatics
- Proteoglycans and glycosaminoglycans research
- Prion Diseases and Protein Misfolding
- RNA modifications and cancer
- Dietary Effects on Health
- Infant Nutrition and Health
- Toxin Mechanisms and Immunotoxins
- Digestive system and related health
- Immune Cell Function and Interaction
- Milk Quality and Mastitis in Dairy Cows
- Inflammatory Bowel Disease
- RNA Research and Splicing
Genos (Croatia)
2015-2024
Science Research Laboratory
2015-2024
Pliva (Croatia)
2008
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,...
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...
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...
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,...
The use of the emerging “omics” technologies for large scale population screening is promising in terms predictive, preventive and personalized medicine. For Parkinson's disease, it essential that an accurate diagnosis obtained disease progression can be monitored. Immunoglobulin G (IgG) has ability to exert both anti-inflammatory pro-inflammatory effects, N-glycosylation fragment crystallizable portion IgG involved this process. This study aimed determine whether glycome could a candidate...
More than half of all known proteins, and almost membrane extra-cellular proteins have oligosaccharide structures or glycans attached to them. Defects in glycosylation pathways are directly involved at least 30 severe human diseases.A multiple center cross-sectional study (China, Croatia, Scotland) was carried out investigate the possible association between hypertension IgG glycosylation. A hydrophilic interaction chromatography fluorescently labeled used analyze N-glycans plasma samples...
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...
Abstract Inflammatory bowel disease (IBD) is characterized by chronic inflammation in the gut. There growing evidence Crohn’s (CD) of existence a preclinical period immunological changes preceding symptom onset that starts years before diagnosis. Gaining insight into this phase will allow prediction and prevention. Analysis serum samples, up to 6 IBD diagnosis (from PREDICTS cohort), revealed identification unique glycosylation signature on circulating antibodies (IgGs) lower galactosylation...
The health state of an individual is closely linked to the glycosylation patterns his or her blood plasma proteins. However, obtaining this information requires cost- and time-efficient analytical methods. We put forward infrared spectroscopy, which allows label-free analysis protein but so far has only been applied Although spectral does not directly provide molecular structure glycans, it sensitive changes therein covers all types glycosidic linkages. Combining single-step ion exchange...
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...
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...
Immunoglobulin G (IgG) is the most abundant serum antibody which structural characteristics and effector functions are modulated through attachment of various sugar moieties called glycans. Composition IgG N-glycome changes with age an individual in different diseases. Variability glycosylation within a population well studied known to be affected by both genetic environmental factors. However, global inter-population differences have never been properly addressed. Here we present...
Young blood plasma is known to confer beneficial effects on various organs in mice and rats. However, it was not whether from young adult pigs rejuvenates old rat tissues at the epigenetic level; alters clock, which a highly accurate molecular biomarker of aging. To address this question, we developed validated six different clocks for that are based DNA methylation values derived n = 613 tissue samples. As indicated by their respective names, pan-tissue clock can be applied profiles all...
Over a half of all proteins are glycosylated, and their proper glycosylation is essential for normal function. Unfortunately, because structural complexity nonlinear branched glycans the absence genetic template synthesis, knowledge about lagging significantly behind or DNA. Using recently developed quantitative high throughput glycan analysis method we quantified components plasma N-glycome in 99 children with attention-deficit hyperactivity disorder (ADHD), 81 child 5 adults autism...
Despite the importance of protein glycosylation in all physiological and pathological processes their potential as diagnostic markers drug targets, glycome children is still unexplored. We analyzed N-linked plasma IgG glycomes 170 adolescents between 6 18 years age. The results showed large biological variability at population level well a number associations different glycans N-glycome younger was found to contain larger proportion complex glycan structures (r = -0.71 for tetrasialylated...
Alpha-1-acid glycoprotein (AGP) is an acute phase in blood, which primarily synthetized the liver and whose biological role not completely understood. It consists of 45% carbohydrates that are present form five N-linked complex glycans. AGP N-glycosylation was shown to be changed many different diseases, some changes appear disease-specific; thus, it has a great diagnostic prognostic potential. However, glycosylation mainly analyzed small cohorts without detailed site-specific glycan...