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  1. Article ; Online: Glycoanalysis of the placental membrane glycoproteins throughout placental development.

    Robajac, Dragana / Masnikosa, Romana / Nemčovič, Marek / Križáková, Martina / Belická Kluková, Ľudmila / Baráth, Peter / Katrlík, Jaroslav / Nedić, Olgica

    Mechanisms of ageing and development

    2019  Volume 183, Page(s) 111151

    Abstract: Structural changes of glycans are observed in different (patho)physiological conditions. Human placental membrane (glyco)proteins were isolated from the first and third trimester placentas of mothers at different ages. By using lectin microarray, we ... ...

    Abstract Structural changes of glycans are observed in different (patho)physiological conditions. Human placental membrane (glyco)proteins were isolated from the first and third trimester placentas of mothers at different ages. By using lectin microarray, we demonstrated that the placental membrane N-glycome contains several N-glycan groups: high mannose, asialylated and sialylated biantennary moieties, bisected, core fucosylated, fucosylated at other positions (bearing terminal and/or antennary Fuc), α2-6 and α2-3 sialylated structures. Employing MALDI-TOF MS enabled identification of over sixty different N-glycan structures in all samples, with 17 moieties exceeding the relative abundance of 2%. The major MS peaks originated from: 1) biantennary complex type N-glycan with a bisecting GlcNAc residue and 2) a core Fuc paucimannosidic and high mannose type structures M3-M9. Age of mothers and the stage of placental development affected N-glycome. The work presented in this article is the first comprehensive mass spectrometric study of the N-glycome of human placental membrane proteins. Our results may be seen as the baseline which can serve for future MALDI MS profiling of the placental membrane N-glycome in different pathophysiological conditions.
    MeSH term(s) Adult ; Female ; Glycoproteins/metabolism ; Humans ; Membrane Proteins/metabolism ; Placenta/metabolism ; Pregnancy ; Pregnancy Proteins/metabolism
    Chemical Substances Glycoproteins ; Membrane Proteins ; Pregnancy Proteins
    Language English
    Publishing date 2019-10-04
    Publishing country Ireland
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 183915-9
    ISSN 1872-6216 ; 0047-6374
    ISSN (online) 1872-6216
    ISSN 0047-6374
    DOI 10.1016/j.mad.2019.111151
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1012: 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)
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  2. Article: Glycoprofiling as a novel tool in serological assays of systemic sclerosis: A comparative study with three bioanalytical methods

    Klukova, Ludmila / Alena Sediva / Alica Vikartovska / Anita Andicsová-Eckstein / Danica Mislovicova / Jan Tkac / Jaroslav Filip / Jaroslav Katrlik / Jaroslav Mosnáček / Jozef Lukáč / Jozef Rovenský / Miroslava Petrikova / Peter Kasak / Richard Imrich / Tomas Bertok

    Analytica chimica acta. 2015 Jan. 01, v. 853

    2015  

    Abstract: Systemic sclerosis (SSc) is an autoimmune disease seriously affecting patient’s quality of life. The heterogeneity of the disease also means that identification and subsequent validation of biomarkers of the disease is quite challenging. A fully ... ...

    Abstract Systemic sclerosis (SSc) is an autoimmune disease seriously affecting patient’s quality of life. The heterogeneity of the disease also means that identification and subsequent validation of biomarkers of the disease is quite challenging. A fully validated single biomarker for diagnosis, prognosis, disease activity and assessment of response to therapy is not yet available. The main aim of this study was to apply an alternative assay protocol to the immunoassay-based analysis of this disease by employment of sialic acid recognizing lectin Sambucus nigra agglutinin (SNA) to glycoprofile serum samples. To our best knowledge this is the first study describing direct lectin-based glycoprofiling of serum SSc samples. Three different analytical methods for glycoprofiling of serum samples relying on application of lectins are compared here from a bioanalytical point of view including traditional ELISA-like lectin-based method (ELLA), novel fluorescent lectin microarrays and ultrasensitive impedimetric lectin biosensors. Results obtained by all three bioanalytical methods consistently showed differences in the level of sialic acid present on glycoproteins, when serum from healthy people was compared to the one from patients having SSc. Thus, analysis of sialic acid content in human serum could be of a diagnostic value for future detection of SSc, but further work is needed to enhance selectivity of assays for example by glycoprofiling of a fraction of human serum enriched in antibodies for individual diagnostics.
    Keywords agglutinins ; analytical chemistry ; analytical methods ; antibodies ; autoimmune diseases ; biomarkers ; biosensors ; blood serum ; diagnostic techniques ; fluorescence ; glycoproteins ; humans ; lectins ; microarray technology ; patients ; people ; prognosis ; quality of life ; Sambucus nigra ; sclerosis ; sialic acids ; therapeutics
    Language English
    Dates of publication 2015-0101
    Size p. 555-562.
    Publishing place Elsevier B.V.
    Document type Article
    ZDB-ID 1483436-4
    ISSN 1873-4324 ; 0003-2670
    ISSN (online) 1873-4324
    ISSN 0003-2670
    DOI 10.1016/j.aca.2014.10.029
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  3. Article ; Online: Glycoprofiling as a novel tool in serological assays of systemic sclerosis: a comparative study with three bioanalytical methods.

    Klukova, Ludmila / Bertok, Tomas / Petrikova, Miroslava / Sediva, Alena / Mislovicova, Danica / Katrlik, Jaroslav / Vikartovska, Alica / Filip, Jaroslav / Kasak, Peter / Andicsová-Eckstein, Anita / Mosnáček, Jaroslav / Lukáč, Jozef / Rovenský, Jozef / Imrich, Richard / Tkac, Jan

    Analytica chimica acta

    2014  Volume 853, Page(s) 555–562

    Abstract: Systemic sclerosis (SSc) is an autoimmune disease seriously affecting patient's quality of life. The heterogeneity of the disease also means that identification and subsequent validation of biomarkers of the disease is quite challenging. A fully ... ...

    Abstract Systemic sclerosis (SSc) is an autoimmune disease seriously affecting patient's quality of life. The heterogeneity of the disease also means that identification and subsequent validation of biomarkers of the disease is quite challenging. A fully validated single biomarker for diagnosis, prognosis, disease activity and assessment of response to therapy is not yet available. The main aim of this study was to apply an alternative assay protocol to the immunoassay-based analysis of this disease by employment of sialic acid recognizing lectin Sambucus nigra agglutinin (SNA) to glycoprofile serum samples. To our best knowledge this is the first study describing direct lectin-based glycoprofiling of serum SSc samples. Three different analytical methods for glycoprofiling of serum samples relying on application of lectins are compared here from a bioanalytical point of view including traditional ELISA-like lectin-based method (ELLA), novel fluorescent lectin microarrays and ultrasensitive impedimetric lectin biosensors. Results obtained by all three bioanalytical methods consistently showed differences in the level of sialic acid present on glycoproteins, when serum from healthy people was compared to the one from patients having SSc. Thus, analysis of sialic acid content in human serum could be of a diagnostic value for future detection of SSc, but further work is needed to enhance selectivity of assays for example by glycoprofiling of a fraction of human serum enriched in antibodies for individual diagnostics.
    MeSH term(s) Adult ; Biosensing Techniques ; Dielectric Spectroscopy ; Electrodes ; Enzymes, Immobilized/chemistry ; Enzymes, Immobilized/metabolism ; Female ; Glycoproteins/blood ; Humans ; Immunoassay ; Middle Aged ; N-Acetylneuraminic Acid/analysis ; Plant Lectins/chemistry ; Plant Lectins/metabolism ; Protein Array Analysis ; Protein Binding ; Ribosome Inactivating Proteins/chemistry ; Ribosome Inactivating Proteins/metabolism ; Sambucus nigra/metabolism ; Scleroderma, Systemic/blood ; Scleroderma, Systemic/metabolism ; Scleroderma, Systemic/pathology
    Chemical Substances Enzymes, Immobilized ; Glycoproteins ; Plant Lectins ; Sambucus nigra lectins ; Ribosome Inactivating Proteins (EC 3.2.2.22) ; N-Acetylneuraminic Acid (GZP2782OP0)
    Language English
    Publishing date 2014-10-27
    Publishing country Netherlands
    Document type Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1483436-4
    ISSN 1873-4324 ; 0003-2670
    ISSN (online) 1873-4324
    ISSN 0003-2670
    DOI 10.1016/j.aca.2014.10.029
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Ultrasensitive impedimetric lectin biosensors with efficient antifouling properties applied in glycoprofiling of human serum samples.

    Bertok, Tomas / Klukova, Ludmila / Sediva, Alena / Kasák, Peter / Semak, Vladislav / Micusik, Matej / Omastova, Maria / Chovanová, Lucia / Vlček, Miroslav / Imrich, Richard / Vikartovska, Alica / Tkac, Jan

    Analytical chemistry

    2013  Volume 85, Issue 15, Page(s) 7324–7332

    Abstract: Ultrasensitive impedimetric lectin biosensors recognizing different glycan entities on serum glycoproteins were constructed. Lectins were immobilized on a novel mixed self-assembled monolayer containing 11-mercaptoundecanoic acid for covalent ... ...

    Abstract Ultrasensitive impedimetric lectin biosensors recognizing different glycan entities on serum glycoproteins were constructed. Lectins were immobilized on a novel mixed self-assembled monolayer containing 11-mercaptoundecanoic acid for covalent immobilization of lectins and betaine terminated thiol to resist nonspecific interactions. Construction of biosensors based on Concanavalin A (Con A), Sambucus nigra agglutinin type I (SNA), and Ricinus communis agglutinin (RCA) on polycrystalline gold electrodes was optimized and characterized with a battery of tools including electrochemical impedance spectroscopy, various electrochemical techniques, quartz crystal microbalance (QCM), Fourier transform infrared (FT-IR) spectroscopy, atomic force microscopy (AFM), and X-ray photoelectron spectroscopy (XPS) and compared with a protein/lectin microarray. The lectin biosensors were able to detect glycoproteins from 1 fM (Con A), 10 fM (Ricinus communis agglutinin (RCA), or 100 fM (SNA) with a linear range spanning 6 (SNA), 7 (RCA), or 8 (Con A) orders of magnitude. Furthermore, a detection limit for the Con A biosensor down to 1 aM was achieved in a sandwich configuration. A nonspecific binding of proteins for the Con A biosensor was only 6.1% (probed with an oxidized invertase) of the signal toward its analyte invertase and a negligible nonspecific interaction of the Con A biosensor was observed in diluted human sera (1000×), as well. The performance of the lectin biosensors was finally tested by glycoprofiling of human serum samples from healthy individuals and those having rheumatoid arthritis, which resulted in a distinct glycan pattern between these two groups.
    MeSH term(s) Biofouling/prevention & control ; Biosensing Techniques/methods ; Glycoproteins/blood ; Glycoproteins/chemistry ; Glycoproteins/metabolism ; Gold/chemistry ; Humans ; Microscopy, Atomic Force ; Models, Molecular ; Plant Lectins/metabolism ; Protein Conformation ; Quartz Crystal Microbalance Techniques ; Surface Properties
    Chemical Substances Glycoproteins ; Plant Lectins ; Gold (7440-57-5)
    Language English
    Publishing date 2013-07-15
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1508-8
    ISSN 1520-6882 ; 0003-2700
    ISSN (online) 1520-6882
    ISSN 0003-2700
    DOI 10.1021/ac401281t
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 4033: 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)
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  5. Article: Ultrasensitive Impedimetric Lectin Biosensors with Efficient Antifouling Properties Applied in Glycoprofiling of Human Serum Samples

    Bertok, Tomas / Chovanová Lucia / Imrich Richard / Kasák Peter / Klukova Ludmila / Micusik Matej / Omastova Maria / Sediva Alena / Semak Vladislav / Tkac Jan / Vikartovska Alica / Vlček Miroslav

    Analytical chemistry. 2013 Aug. 06, v. 85, no. 15

    2013  

    Abstract: Ultrasensitive impedimetric lectin biosensors recognizing different glycan entities on serum glycoproteins were constructed. Lectins were immobilized on a novel mixed self-assembled monolayer containing 11-mercaptoundecanoic acid for covalent ... ...

    Abstract Ultrasensitive impedimetric lectin biosensors recognizing different glycan entities on serum glycoproteins were constructed. Lectins were immobilized on a novel mixed self-assembled monolayer containing 11-mercaptoundecanoic acid for covalent immobilization of lectins and betaine terminated thiol to resist nonspecific interactions. Construction of biosensors based on Concanavalin A (Con A), Sambucus nigra agglutinin type I (SNA), and Ricinus communis agglutinin (RCA) on polycrystalline gold electrodes was optimized and characterized with a battery of tools including electrochemical impedance spectroscopy, various electrochemical techniques, quartz crystal microbalance (QCM), Fourier transform infrared (FT-IR) spectroscopy, atomic force microscopy (AFM), and X-ray photoelectron spectroscopy (XPS) and compared with a protein/lectin microarray. The lectin biosensors were able to detect glycoproteins from 1 fM (Con A), 10 fM (Ricinus communis agglutinin (RCA), or 100 fM (SNA) with a linear range spanning 6 (SNA), 7 (RCA), or 8 (Con A) orders of magnitude. Furthermore, a detection limit for the Con A biosensor down to 1 aM was achieved in a sandwich configuration. A nonspecific binding of proteins for the Con A biosensor was only 6.1% (probed with an oxidized invertase) of the signal toward its analyte invertase and a negligible nonspecific interaction of the Con A biosensor was observed in diluted human sera (1000×), as well. The performance of the lectin biosensors was finally tested by glycoprofiling of human serum samples from healthy individuals and those having rheumatoid arthritis, which resulted in a distinct glycan pattern between these two groups.
    Keywords agglutinins ; atomic force microscopy ; beta-fructofuranosidase ; betaine ; binding proteins ; biosensors ; blood serum ; concanavalin A ; detection limit ; dielectric spectroscopy ; electrochemistry ; electrodes ; Fourier transform infrared spectroscopy ; glycoproteins ; gold ; humans ; microarray technology ; quartz ; rheumatoid arthritis ; Ricinus communis ; Sambucus nigra ; thiols ; X-ray photoelectron spectroscopy
    Language English
    Dates of publication 2013-0806
    Size p. 7324-7332.
    Publishing place American Chemical Society
    Document type Article
    ZDB-ID 1508-8
    ISSN 1520-6882 ; 0003-2700
    ISSN (online) 1520-6882
    ISSN 0003-2700
    DOI 10.1021%2Fac401281t
    Database NAL-Catalogue (AGRICOLA)

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