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  1. Article ; Online: Comparison of self-sampling blood collection for N-glycosylation analysis.

    Cvetko, Ana / Tijardović, Marko / Bilandžija-Kuš, Iva / Gornik, Olga

    BMC research notes

    2022  Volume 15, Issue 1, Page(s) 61

    Abstract: Objective: Self-sampling of capillary blood provides easier sample collection, handling, and shipping compared to more invasive blood sampling via venepuncture. Recently, other means of capillary blood collection were introduced to the market, such as ... ...

    Abstract Objective: Self-sampling of capillary blood provides easier sample collection, handling, and shipping compared to more invasive blood sampling via venepuncture. Recently, other means of capillary blood collection were introduced to the market, such as Neoteryx sticks and Noviplex cards. We tested the comparability of these two self-sampling methods, alongside dried blood spots (DBS), with plasma acquired from venepunctured blood in N-glycoprofiling of total proteins. We have also tested the intra-day repeatability of the three mentioned self-sampling methods. Capillary blood collection with Neoteryx, Noviplex and DBS was done following the manufacturers' instructions and N-glycoprofiling of released, fluorescently labelled N-glycans was performed with ultra-performance liquid chromatography.
    Results: Comparability with plasma was assessed by calculating the relative deviance, which was 0.674 for DBS, 0.092 for Neoteryx sticks, and 0.069 for Noviplex cards. In repeatability testing, similar results were obtained, with Noviplex cards and Neoteryx sticks performing substantially better than DBS (CVs = 4.831% and 7.098%, compared to 14.305%, respectively). Our preliminary study on the use of Neoteryx and Noviplex self-sampling devices in glycoanalysis demonstrates their satisfactory performance in both the comparability and repeatability testing, however, they should be further tested in larger collaborations and cohorts.
    MeSH term(s) Blood Specimen Collection ; Chromatography, Liquid ; Dried Blood Spot Testing/methods ; Glycosylation ; Specimen Handling/methods
    Language English
    Publishing date 2022-02-16
    Publishing country England
    Document type Journal Article
    ZDB-ID 2413336-X
    ISSN 1756-0500 ; 1756-0500
    ISSN (online) 1756-0500
    ISSN 1756-0500
    DOI 10.1186/s13104-022-05958-9
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: High-Throughput and Site-Specific N-Glycosylation Analysis of Human Alpha-1-Acid Glycoprotein Offers a Great Potential for New Biomarker Discovery.

    Keser, Toma / Tijardović, Marko / Gornik, Ivan / Lukić, Edita / Lauc, Gordan / Gornik, Olga / Novokmet, Mislav

    Molecular & cellular proteomics : MCP

    2021  Volume 20, Page(s) 100044

    Abstract: Alpha-1-acid glycoprotein (AGP) is an acute phase glycoprotein in blood, which is primarily synthetized in the liver and whose biological role is not completely understood. It consists of 45% carbohydrates that are present in the form of five N-linked ... ...

    Abstract Alpha-1-acid glycoprotein (AGP) is an acute phase glycoprotein in blood, which is primarily synthetized in the liver and whose biological role is not completely understood. It consists of 45% carbohydrates that are present in the form of five N-linked complex glycans. AGP N-glycosylation was shown to be changed in many different diseases, and some changes appear to be disease-specific; thus, it has a great diagnostic and prognostic potential. However, AGP glycosylation was mainly analyzed in small cohorts and without detailed site-specific glycan information. Here, we developed a cost-effective method for a high-throughput and site-specific N-glycosylation LC-MS analysis of AGP which can be applied on large cohorts, aid in search for novel disease biomarkers, and enable better understanding of AGP's role and function in health and disease. The method does not require isolation of AGP with antibodies and affinity chromatography, but AGP is enriched by acid precipitation from 5 μl of bloodplasma in a 96-well format. After trypsinization, AGP glycopeptides are purified using a hydrophilic interaction chromatography-based solid-phase extraction and analyzed by reversed-phase-liquid chromatography-electrospray ionization-MS. We used our method to show for the first time that AGP N-glycan profile is stable in healthy individuals (14 individuals in three time points), which is a requirement for evaluation of its diagnostic potential. Furthermore, we tested our method on a population including individuals with registered hyperglycemia in critical illness (59 cases and 49 controls), which represents a significantly increased risk of developing type 2 diabetes. Individuals at higher risk of diabetes presented increased N-glycan branching on AGP's second glycosylation site and lower sialylation of N-glycans on AGP's third and AGP1's fourth glycosylation site. Although this should be confirmed on a larger prospective cohort, it indicates that site-specific AGP N-glycan profile could help distinguish individuals who are at risk of type 2 diabetes.
    MeSH term(s) Adolescent ; Adult ; Aged ; Biomarkers/blood ; Biomarkers/metabolism ; Chromatography, Reverse-Phase ; Critical Illness ; Female ; Glycosylation ; High-Throughput Screening Assays ; Humans ; Hyperglycemia/blood ; Hyperglycemia/metabolism ; Male ; Middle Aged ; Orosomucoid/analysis ; Orosomucoid/metabolism ; Pilot Projects ; Spectrometry, Mass, Electrospray Ionization ; Tandem Mass Spectrometry ; Young Adult
    Chemical Substances Biomarkers ; Orosomucoid
    Language English
    Publishing date 2021-01-23
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2075924-1
    ISSN 1535-9484 ; 1535-9476
    ISSN (online) 1535-9484
    ISSN 1535-9476
    DOI 10.1074/mcp.RA120.002433
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 5599: Show issues Location:
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  3. Article: Human complement component C3 N-glycome changes in type 1 diabetes complications.

    Šoić, Dinko / Štambuk, Jerko / Tijardović, Marko / Keser, Toma / Lauc, Gordan / Bulum, Tomislav / Lovrenčić, Marijana Vučić / Rebrina, Sandra Vučković / Tomić, Martina / Novokmet, Mislav / Smirčić-Duvnjak, Lea / Gornik, Olga

    Frontiers in endocrinology

    2023  Volume 14, Page(s) 1101154

    Abstract: Aim: Changes in N-glycosylation have been described in numerous diseases and are being considered as biomarkers of ongoing pathological condition. Previous studies demonstrated the interrelation of N-glycosylation and type 1 diabetes (T1D), particularly ...

    Abstract Aim: Changes in N-glycosylation have been described in numerous diseases and are being considered as biomarkers of ongoing pathological condition. Previous studies demonstrated the interrelation of N-glycosylation and type 1 diabetes (T1D), particularly linking serum N-glycan changes with complications accompanying the disease. Moreover, the role of complement component C3 in diabetic nephropathy and retinopathy has been implicated, and C3 N-glycome was found to be altered in young T1D patients. Therefore, we investigated associations between C3 N-glycan profiles and albuminuria and retinopathy accompanying T1D, as well as glycosylation connection with other known T1D complication risk factors.
    Research design and methods: Complement component C3 N-glycosylation profiles have been analyzed from 189 serum samples of T1D patients (median age 46) recruited at a Croatian hospital centre. Using our recently developed high-throughput method, relative abundances of all six of the C3 glycopeptides have been determined. Assessment of C3 N-glycome interconnection with T1D complications, hypertension, smoking status, estimated glomerular filtration rate (eGFR), glycaemic control and duration of the disease was done using linear modelling.
    Results: Significant changes of C3 N-glycome in severe albuminuria accompanying type 1 diabetes were observed, as well as in T1D subjects with hypertension. All except one of the C3 glycopeptides proved to be associated with measured HbA1c levels. One of the glycoforms was shown to be changed in non-proliferative T1D retinopathy. Smoking and eGFR showed no effect on C3 N-glycome. Furthermore, C3 N-glycosylation profile was shown to be independent of disease duration.
    Conclusion: This study empowered the role of C3 N-glycosylation in T1D, showing value in distinguishing subjects with different diabetic complications. Being independent of the disease duration, these changes may be associated with the disease onset, making C3 N-glycome a potential novel marker of the disease progression and severity.
    MeSH term(s) Humans ; Middle Aged ; Diabetes Mellitus, Type 1/complications ; Albuminuria/etiology ; Diabetic Retinopathy/complications ; Polysaccharides ; Glycopeptides
    Chemical Substances Polysaccharides ; Glycopeptides
    Language English
    Publishing date 2023-05-24
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2592084-4
    ISSN 1664-2392
    ISSN 1664-2392
    DOI 10.3389/fendo.2023.1101154
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  4. Article ; Online: N-glycosylation of serum proteins in adult type 1 diabetes mellitus exposes further changes compared to children at the disease onset.

    Nemčić, Matej / Tijardović, Marko / Rudman, Najda / Bulum, Tomislav / Tomić, Martina / Plavša, Branimir / Vučković Rebrina, Sandra / Vučić Lovrenčić, Marijana / Duvnjak, Lea / Morahan, Grant / Gornik, Olga

    Clinica chimica acta; international journal of clinical chemistry

    2023  Volume 543, Page(s) 117298

    Abstract: Objective: Previously we have shown that plasma protein N-glycosylation is changed in children at the onset of type 1 diabetes. In this study, we aim to identify N-glycan changes in adults with T1DM, compare them to those in children, and investigate ... ...

    Abstract Objective: Previously we have shown that plasma protein N-glycosylation is changed in children at the onset of type 1 diabetes. In this study, we aim to identify N-glycan changes in adults with T1DM, compare them to those in children, and investigate their associations with disease duration, complications, glycaemic status, and smoking.
    Methods: Serum protein N-glycans from 200 adults with type 1 diabetes and 298 healthy controls were analysed using ultra-high performance liquid chromatography and divided into 39 directly measured glycan groups from which 16 derived traits were calculated.
    Results: Compared to healthy controls, subjects with type 1 diabetes showed differences in 19 glycan groups and a decrease in monogalactosylated, an increase in digalactosylated, monosialylated, and antennary fucosylated derived traits, from which changes in monogalactosylation and seven directly measured traits overlapped with previously reported in children. Changes in four directly measured and two derived traits previously seen in children were not detected in adults. HbA1c was positively associated with sialylated and highly branched structures, whereas N-glycome was not influenced by disease duration or diabetic complications.
    Conclusions: Our results suggest potential N-glycome involvement in different stages of type 1 diabetes, including processes underlying its development, the disease itself, as well as those occurring after disease establishment.
    MeSH term(s) Humans ; Adult ; Child ; Diabetes Mellitus, Type 1 ; Glycosylation ; Smoking ; Blood Proteins/metabolism ; Polysaccharides
    Chemical Substances Blood Proteins ; Polysaccharides
    Language English
    Publishing date 2023-03-15
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 80228-1
    ISSN 1873-3492 ; 0009-8981
    ISSN (online) 1873-3492
    ISSN 0009-8981
    DOI 10.1016/j.cca.2023.117298
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    In stock of ZB MED Cologne/Königswinter

    Ud II Zs.173: Show issues Location:
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    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
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  5. Article: Intense Physical Exercise Induces an Anti-inflammatory Change in IgG N-Glycosylation Profile.

    Tijardović, Marko / Marijančević, Domagoj / Bok, Daniel / Kifer, Domagoj / Lauc, Gordan / Gornik, Olga / Keser, Toma

    Frontiers in physiology

    2019  Volume 10, Page(s) 1522

    Abstract: Exercise is known to improve many aspects of human health, including modulation of the immune system and inflammatory status. It is generally understood that exercise reduces inflammation, but there are missing links in terms of understanding the ... ...

    Abstract Exercise is known to improve many aspects of human health, including modulation of the immune system and inflammatory status. It is generally understood that exercise reduces inflammation, but there are missing links in terms of understanding the mechanisms as well as the differences between exercise modalities. N-glycosylation of immunoglobulin G (IgG) and total plasma proteins was previously shown to reflect changes in inflammatory pathways, which could provide valuable information to further clarify exercise effects. In order to further expand the understanding of the relationship between physical activity and inflammation, we examined the effect of intense exercise, in the form of repeated sprint training (RST), on IgG and total plasma proteins N-glycosylation in combination with traditionally used inflammation markers: C-reactive protein (CRP), interleukin 6 (IL-6), and leukocyte count. Twenty-nine male physical education students were separated into treatment (RST,
    Language English
    Publishing date 2019-12-20
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2564217-0
    ISSN 1664-042X
    ISSN 1664-042X
    DOI 10.3389/fphys.2019.01522
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  6. Article ; Online: Fucosylated AGP glycopeptides as biomarkers of HNF1A-Maturity onset diabetes of the young.

    Tijardović, Marko / Štambuk, Tamara / Juszczak, Agata / Keser, Toma / Gasperikova, Daniela / Novokmet, Mislav / Tjora, Erling / Pape Medvidović, Edita / Stanik, Juraj / Rasmus Njølstad, Pål / Lauc, Gordan / Owen, Katharine R / Gornik, Olga

    Diabetes research and clinical practice

    2022  Volume 185, Page(s) 109226

    Abstract: Aims: We previously demonstrated that antennary fucosylated N-glycans on plasma proteins are regulated by HNF1A and can identify cases of Maturity-Onset Diabetes of the Young caused by HNF1A variants (HNF1A-MODY). Based on literature data, we further ... ...

    Abstract Aims: We previously demonstrated that antennary fucosylated N-glycans on plasma proteins are regulated by HNF1A and can identify cases of Maturity-Onset Diabetes of the Young caused by HNF1A variants (HNF1A-MODY). Based on literature data, we further postulated that N-glycans with best diagnostic value mostly originate from alpha-1-acid glycoprotein (AGP). In this study we analyzed fucosylation of AGP in subjects with HNF1A-MODY and other types of diabetes aiming to evaluate its diagnostic potential.
    Methods: A recently developed LC-MS method for AGP N-glycopeptide analysis was utilized in two independent cohorts: a) 466 subjects with different diabetes subtypes to test the fucosylation differences, b) 98 selected individuals to test the discriminative potential for pathogenic HNF1A variants.
    Results: Our results showed significant reduction in AGP fucosylation associated to HNF1A-MODY when compared to other diabetes subtypes. Additionally, ROC curve analysis confirmed significant discriminatory potential of individual fucosylated AGP glycopeptides, where the best performing glycopeptide had an AUC of 0.94 (95% CI 0.90-0.99).
    Conclusions: A glycopeptide based diagnostic tool would be beneficial for patient stratification by providing information about the functionality of HNF1A. It could assist the interpretation of DNA sequencing results and be a useful addition to the differential diagnostic process.
    MeSH term(s) Biomarkers ; Diabetes Mellitus, Type 2/diagnosis ; Diabetes Mellitus, Type 2/genetics ; Glycopeptides/genetics ; Hepatocyte Nuclear Factor 1-alpha/genetics ; Hepatocyte Nuclear Factor 1-alpha/metabolism ; Humans ; Mutation ; Polysaccharides/metabolism
    Chemical Substances Biomarkers ; Glycopeptides ; HNF1A protein, human ; Hepatocyte Nuclear Factor 1-alpha ; Polysaccharides
    Language English
    Publishing date 2022-02-02
    Publishing country Ireland
    Document type Journal Article
    ZDB-ID 632523-3
    ISSN 1872-8227 ; 0168-8227
    ISSN (online) 1872-8227
    ISSN 0168-8227
    DOI 10.1016/j.diabres.2022.109226
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 2047: Show issues Location:
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    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  7. Article ; Online: Plasma N-glycome shows continuous deterioration as the diagnosis of insulin resistance approaches.

    Cvetko, Ana / Mangino, Massimo / Tijardović, Marko / Kifer, Domagoj / Falchi, Mario / Keser, Toma / Perola, Markus / Spector, Tim D / Lauc, Gordan / Menni, Cristina / Gornik, Olga

    BMJ open diabetes research & care

    2021  Volume 9, Issue 1

    Abstract: Introduction: Prediction of type 2 diabetes mellitus (T2DM) and its preceding factors, such as insulin resistance (IR), is of great importance as it may allow delay or prevention of onset of the disease. Plasma protein N-glycome has emerged as a ... ...

    Abstract Introduction: Prediction of type 2 diabetes mellitus (T2DM) and its preceding factors, such as insulin resistance (IR), is of great importance as it may allow delay or prevention of onset of the disease. Plasma protein N-glycome has emerged as a promising predictive biomarker. In a prospective longitudinal study, we included patients with a first diagnosis of impaired glucose metabolism (IR or T2DM) to investigate the N-glycosylation's predictive value years before diabetes development.
    Research design and methods: Plasma protein N-glycome was profiled by hydrophilic interaction ultra-performance liquid chromatography in 534 TwinsUK participants free from disease at baseline. This included 89 participants with incident diagnosis of IR or T2DM during the follow-up period (7.14±3.04 years) whose last sample prior to diagnosis was compared using general linear regression with 445 age-matched unrelated controls. Findings were replicated in an independent cohort. Changes in N-glycome have also been presented in connection with time to diagnosis.
    Results: Eight groups of plasma N-glycans were different between incident IR or T2DM cases and controls (p<0.05) after adjusting for multiple testing using Benjamini-Hochberg correction. These differences were noticeable up to 10 years prior to diagnosis and are changing continuously as becoming more expressed toward the diagnosis. The prediction model was built using significant glycan traits, displaying a discriminative performance with an area under the receiver operating characteristic curve of 0.77.
    Conclusions: In addition to previous studies, we showed the diagnostic potential of plasma N-glycome in the prediction of both IR and T2DM development years before the clinical manifestation and indicated the continuous deterioration of N-glycome toward the diagnosis.
    MeSH term(s) Cohort Studies ; Diabetes Mellitus, Type 2/diagnosis ; Humans ; Insulin Resistance ; Longitudinal Studies ; Prospective Studies
    Language English
    Publishing date 2021-09-08
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2732918-5
    ISSN 2052-4897 ; 2052-4897
    ISSN (online) 2052-4897
    ISSN 2052-4897
    DOI 10.1136/bmjdrc-2021-002263
    Database MEDical Literature Analysis and Retrieval System OnLINE

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