LIVIVO - The Search Portal for Life Sciences

zur deutschen Oberfläche wechseln
Advanced search

Search results

Result 1 - 10 of total 379

Search options

  1. Book: The role of glycosylation in health and disease

    Lauc, Gordan / Trbojević-Akmačić, Irena

    (Advances in experimental medicine and biology ; 1325)

    2021  

    Author's details Gordan Lauc, Irena Trbojević-Akmačić editors
    Series title Advances in experimental medicine and biology ; 1325
    Collection
    Language English
    Size xxv, 376 Seiten, Illustrationen
    Publisher Springer
    Publishing place Cham
    Publishing country United States
    Document type Book
    HBZ-ID HT021085860
    ISBN 978-3-030-70114-7 ; 9783030701154 ; 3-030-70114-X ; 3030701158
    Database Catalogue ZB MED Medicine, Health

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Shelf markLoan statusLocation
    Zs A 3192 -1325- not available for loan Zeitschriften-Lesesaal

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  2. Article ; Online: Can we suppress chronic systemic inflammation and postpone age-related diseases by targeting the IgG glycome?

    Lauc, GordAn

    Expert opinion on therapeutic targets

    2023  , Page(s) 1–9

    Abstract: Introduction: Glycans attached to immunoglobulin G are an important regulator of chronic systemic inflammation, one of the key drivers of aging. As people age, glycans that suppress inflammation are being replaced with inflammation-promoting glycans, ... ...

    Abstract Introduction: Glycans attached to immunoglobulin G are an important regulator of chronic systemic inflammation, one of the key drivers of aging. As people age, glycans that suppress inflammation are being replaced with inflammation-promoting glycans, but the rate of this conversion is highly individual and is affected by genetic, epigenetic, and environmental factors.
    Areas covered: This review summarizes key studies of IgG glycosylation changes in aging and disease, effects of lifestyle and pharmacological interventions, and mechanisms that regulate IgG glycosylation.
    Expert opinion: IgG glycome is an important contributor to the process of aging that can be modulated by both lifestyle and pharmacological interventions. Small molecule drugs that would suppress chronic systemic inflammation by modulation of the IgG glycome are still not available, but since gene network regulating IgG glycosylation has been identified and a high-throughput
    Language English
    Publishing date 2023-10-28
    Publishing country England
    Document type Journal Article
    ZDB-ID 2055208-7
    ISSN 1744-7631 ; 1472-8222
    ISSN (online) 1744-7631
    ISSN 1472-8222
    DOI 10.1080/14728222.2023.2277218
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 5244: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  3. Article ; Online: Response to "Immunoglobulin G glycome and severity of COVID-19: more likely a quantification of bias than a true association".

    Lauc, Gordan

    Glycobiology

    2020  Volume 31, Issue 7, Page(s) 717–718

    MeSH term(s) COVID-19 ; Glycosylation ; Humans ; Immunoglobulin G/metabolism ; SARS-CoV-2
    Chemical Substances Immunoglobulin G
    Language English
    Publishing date 2020-12-17
    Publishing country England
    Document type Journal Article ; Comment
    ZDB-ID 1067689-2
    ISSN 1460-2423 ; 0959-6658
    ISSN (online) 1460-2423
    ISSN 0959-6658
    DOI 10.1093/glycob/cwaa116
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 3150: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  4. Article ; Online: The dynamic brain N-glycome.

    Klarić, Thomas S / Lauc, Gordan

    Glycoconjugate journal

    2022  Volume 39, Issue 3, Page(s) 443–471

    Abstract: The attachment of carbohydrates to other macromolecules, such as proteins or lipids, is an important regulatory mechanism termed glycosylation. One subtype of protein glycosylation is asparagine-linked glycosylation (N-glycosylation) which plays a key ... ...

    Abstract The attachment of carbohydrates to other macromolecules, such as proteins or lipids, is an important regulatory mechanism termed glycosylation. One subtype of protein glycosylation is asparagine-linked glycosylation (N-glycosylation) which plays a key role in the development and normal functioning of the vertebrate brain. To better understand the role of N-glycans in neurobiology, it's imperative we analyse not only the functional roles of individual structures, but also the collective impact of large-scale changes in the brain N-glycome. The systematic study of the brain N-glycome is still in its infancy and data are relatively scarce. Nevertheless, the prevailing view has been that the neuroglycome is inherently restricted with limited capacity for variation. The development of improved methods for N-glycomics analysis of brain tissue has facilitated comprehensive characterisation of the complete brain N-glycome under various experimental conditions on a larger scale. Consequently, accumulating data suggest that it's more dynamic than previously recognised and that, within a general framework, it has a given capacity to change in response to both intrinsic and extrinsic stimuli. Here, we provide an overview of the many factors that can alter the brain N-glycome, including neurodevelopment, ageing, diet, stress, neuroinflammation, injury, and disease. Given this emerging evidence, we propose that the neuroglycome has a hitherto underappreciated plasticity and we discuss the therapeutic implications of this regarding the possible reversal of pathological changes via interventions. We also briefly review the merits and limitations of N-glycomics as an analytical method before reflecting on some of the outstanding questions in the field.
    MeSH term(s) Brain/metabolism ; Glycomics ; Glycosylation ; Polysaccharides/chemistry
    Chemical Substances Polysaccharides
    Language English
    Publishing date 2022-03-25
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 283770-5
    ISSN 1573-4986 ; 0282-0080
    ISSN (online) 1573-4986
    ISSN 0282-0080
    DOI 10.1007/s10719-022-10055-x
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 2171: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  5. Article ; Online: Some additional considerations on: "Finding the sweet spot: glycosylation mediated regulation of intestinal inflammation".

    Monaghan, Tanya M / Kao, Dina / Lauc, Gordan

    Mucosal immunology

    2022  Volume 15, Issue 3, Page(s) 525

    MeSH term(s) Glycosylation ; Humans ; Inflammation
    Language English
    Publishing date 2022-04-06
    Publishing country United States
    Document type Letter ; Comment
    ZDB-ID 2411370-0
    ISSN 1935-3456 ; 1933-0219
    ISSN (online) 1935-3456
    ISSN 1933-0219
    DOI 10.1038/s41385-022-00512-z
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 6796: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  6. Article ; Online: Storage stability and HILIC-UHPLC-FLR analysis of immunoglobulin G N-glycome from saliva.

    Radovani, Barbara / Lauc, Gordan / Gudelj, Ivan

    Analytical and bioanalytical chemistry

    2023  Volume 415, Issue 28, Page(s) 6985–6993

    Abstract: Immunoglobulin G (IgG) is the most abundant antibody in the blood and plays a critical role in host immune defense against infectious agents. Glycosylation is known to modulate the effector functions of IgG and is involved in disease development and ... ...

    Abstract Immunoglobulin G (IgG) is the most abundant antibody in the blood and plays a critical role in host immune defense against infectious agents. Glycosylation is known to modulate the effector functions of IgG and is involved in disease development and progression. It is no surprise that the N-glycome of IgG from plasma has already been proposed as a biomarker for various physiological and pathological conditions. However, because saliva is easy to collect, it could be useful for exploring the functional role of salivary IgG N-glycosylation and its potential as a diagnostic biomarker. Therefore, in this study, we described a method for N-glycome analysis of IgG from saliva samples. Salivary IgG N-glycans were analyzed by ultra-high-performance liquid chromatography based on hydrophilic interactions with fluorescence detection (HILIC-UHPLC-FLR). In addition, we compared IgG N-glycan profiles from saliva with those from plasma, assessed the stability of salivary IgG N-glycan profiles under different storage conditions, and evaluated the effects of using a saliva preservation medium. This study provides an ultrasensitive UHPLC method for the analysis of total IgG N-glycosylation from saliva, gives insight into storage stability of salivary IgG, and highlights its (dis)advantages for further biomarker-related research.
    MeSH term(s) Immunoglobulin G/chemistry ; Saliva ; Chromatography, High Pressure Liquid ; Polysaccharides ; Biomarkers ; Immunoglobulin A, Secretory
    Chemical Substances Immunoglobulin G ; Polysaccharides ; Biomarkers ; Immunoglobulin A, Secretory
    Language English
    Publishing date 2023-04-14
    Publishing country Germany
    Document type Journal Article
    ZDB-ID 201093-8
    ISSN 1618-2650 ; 0016-1152 ; 0372-7920
    ISSN (online) 1618-2650
    ISSN 0016-1152 ; 0372-7920
    DOI 10.1007/s00216-023-04682-y
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Bonn / Germany

    Z 4' 69/97: Show issues
    Archiv 3: Show issues
    Z 9.4: Show issues

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  7. Article: Precision medicine that transcends genomics: Glycans as integrators of genes and environment.

    Lauc, Gordan

    Biochimica et biophysica acta

    2016  Volume 1860, Issue 8, Page(s) 1571–1573

    MeSH term(s) Gene-Environment Interaction ; Genomics ; Humans ; Molecular Medicine ; Polysaccharides
    Chemical Substances Polysaccharides
    Language English
    Publishing date 2016-08
    Publishing country Netherlands
    Document type Editorial
    ZDB-ID 60-7
    ISSN 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    ISSN (online) 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
    ISSN 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    DOI 10.1016/j.bbagen.2016.05.001
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Uc I Zs.247: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  8. Article: Influence of Desialylation on the Drug Binding Affinity of Human Alpha-1-Acid Glycoprotein Assessed by Microscale Thermophoresis.

    Šeba, Tino / Kerep, Robert / Weitner, Tin / Šoić, Dinko / Keser, Toma / Lauc, Gordan / Gabričević, Mario

    Pharmaceutics

    2024  Volume 16, Issue 2

    Abstract: Human serum alpha-1-acid glycoprotein (AAG) is an acute-phase plasma protein involved in the binding and transport of many drugs, especially basic and lipophilic substances. The sialic acid groups that terminate the N-glycan chains of AAG have been ... ...

    Abstract Human serum alpha-1-acid glycoprotein (AAG) is an acute-phase plasma protein involved in the binding and transport of many drugs, especially basic and lipophilic substances. The sialic acid groups that terminate the N-glycan chains of AAG have been reported to change in response to numerous health conditions and may have an impact on the binding of drugs to AAG. In this study, we quantified the binding between native and desialylated AAG and seven drugs from different pharmacotherapeutic groups (carvedilol, diltiazem, dipyridamole, imipramine, lidocaine, propranolol, vinblastine) using microscale thermophoresis (MST). This method was chosen due to its robustness and high sensitivity, allowing precise quantification of molecular interactions based on the thermophoretic movement of fluorescent molecules. Detailed glycan analysis of native and desialylated AAG showed over 98% reduction in sialic acid content for the enzymatically desialylated AAG. The MST results indicate that desialylation generally alters the binding affinity between AAG and drugs, leading to either an increase or decrease in
    Language English
    Publishing date 2024-02-05
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2527217-2
    ISSN 1999-4923
    ISSN 1999-4923
    DOI 10.3390/pharmaceutics16020230
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  9. Article ; Online: Correction to: Regular moderate physical exercise decreases Glycan Age index of biological age and reduces inflammatory potential of Immunoglobulin G.

    Šimunić-Briški, Nina / Dukarić, Vedran / Očić, Mateja / Madžar, Tomislav / Vinicki, Martina / Frkatović-Hodžić, Azra / Knjaz, Damir / Lauc, Gordan

    Glycoconjugate journal

    2024  Volume 41, Issue 1, Page(s) 77–78

    Language English
    Publishing date 2024-01-11
    Publishing country United States
    Document type Published Erratum
    ZDB-ID 283770-5
    ISSN 1573-4986 ; 0282-0080
    ISSN (online) 1573-4986
    ISSN 0282-0080
    DOI 10.1007/s10719-024-10146-x
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 2171: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  10. Article ; Online: Anastrozole and Tamoxifen Impact on IgG Glycome Composition Dynamics in Luminal A and Luminal B Breast Cancers.

    Rapčan, Borna / Fančović, Matko / Pribić, Tea / Kirac, Iva / Gaće, Mihaela / Vučković, Frano / Lauc, Gordan

    Antibodies (Basel, Switzerland)

    2024  Volume 13, Issue 1

    Abstract: This study examines the intricate relationship between protein glycosylation dynamics and therapeutic responses in Luminal A and Luminal B breast cancer subtypes, focusing on anastrozole and tamoxifen impacts. The present methods inadequately monitor and ...

    Abstract This study examines the intricate relationship between protein glycosylation dynamics and therapeutic responses in Luminal A and Luminal B breast cancer subtypes, focusing on anastrozole and tamoxifen impacts. The present methods inadequately monitor and forecast patient reactions to these treatments, leaving individuals vulnerable to the potential adverse effects of these medications. This research investigated glycan structural changes by following patients for up to 9 months. The protocol involved a series of automated steps including IgG isolation, protein denaturation, glycan labelling, purification, and final analysis using capillary gel electrophoresis with laser-induced fluorescence. The results suggested the significant role of glycan modifications in breast cancer progression, revealing distinctive trends in how anastrozole and tamoxifen elicit varied responses. The findings indicate anastrozole's association with reduced sialylation and increased core fucosylation, while tamoxifen correlated with increased sialylation and decreased core fucosylation. These observations suggest potential immunomodulatory effects: anastrozole possibly reducing inflammation and tamoxifen impacting immune-mediated cytotoxicity. This study strongly emphasizes the importance of considering specific glycan traits to comprehend the dynamic mechanisms driving breast cancer progression and the effects of targeted therapies. The nuanced differences observed in glycan modifications between these two treatments underscore the necessity for further comprehensive research aimed at thoroughly evaluating the long-term implications and therapeutic efficacy for breast cancer patients.
    Language English
    Publishing date 2024-02-01
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2661514-9
    ISSN 2073-4468 ; 2073-4468
    ISSN (online) 2073-4468
    ISSN 2073-4468
    DOI 10.3390/antib13010009
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

To top