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  1. Article ; Online: The pleiotropic role of galectin-3 in melanoma progression: Unraveling the enigma.

    Mohammed, Norhan B B / Antonopoulos, Aristotelis / Dell, Anne / Haslam, Stuart M / Dimitroff, Charles J

    Advances in cancer research

    2022  Volume 157, Page(s) 157–193

    Abstract: Melanoma is a highly aggressive skin cancer with poor outcomes associated with distant metastasis. Intrinsic properties of melanoma cells alongside the crosstalk between melanoma cells and surrounding microenvironment determine the tumor behavior. ... ...

    Abstract Melanoma is a highly aggressive skin cancer with poor outcomes associated with distant metastasis. Intrinsic properties of melanoma cells alongside the crosstalk between melanoma cells and surrounding microenvironment determine the tumor behavior. Galectin-3 (Gal-3), a ß-galactoside-binding lectin, has emerged as a major effector in cancer progression, including melanoma behavior. Data from melanoma models and patient studies reveal that Gal-3 expression is dysregulated, both intracellularly and extracellularly, throughout the stages of melanoma progression. This review summarizes the most recent data and hypotheses on Gal-3 and its tumor-modulating functions, highlighting its role in driving melanoma growth, invasion, and metastatic colonization. It also provides insight into potential Gal-3-targeted strategies for melanoma diagnosis and treatment.
    MeSH term(s) Humans ; Galectin 3/metabolism ; Melanoma/pathology ; Tumor Microenvironment
    Chemical Substances Galectin 3
    Language English
    Publishing date 2022-08-08
    Publishing country United States
    Document type Review ; Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 127-2
    ISSN 2162-5557 ; 0065-230X
    ISSN (online) 2162-5557
    ISSN 0065-230X
    DOI 10.1016/bs.acr.2022.06.001
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Glyco-engineered MDCK cells display preferred receptors of H3N2 influenza absent in eggs used for vaccines.

    Kikuchi, Chika / Antonopoulos, Aristotelis / Wang, Shengyang / Maemura, Tadashi / Karamanska, Rositsa / Lee, Chiara / Thompson, Andrew J / Dell, Anne / Kawaoka, Yoshihiro / Haslam, Stuart M / Paulson, James C

    Nature communications

    2023  Volume 14, Issue 1, Page(s) 6178

    Abstract: Evolution of human H3N2 influenza viruses driven by immune selection has narrowed the receptor specificity of the hemagglutinin (HA) to a restricted subset of human-type (Neu5Acα2-6 Gal) glycan receptors that have extended poly-LacNAc (Galβ1-4GlcNAc) ... ...

    Abstract Evolution of human H3N2 influenza viruses driven by immune selection has narrowed the receptor specificity of the hemagglutinin (HA) to a restricted subset of human-type (Neu5Acα2-6 Gal) glycan receptors that have extended poly-LacNAc (Galβ1-4GlcNAc) repeats. This altered specificity has presented challenges for hemagglutination assays, growth in laboratory hosts, and vaccine production in eggs. To assess the impact of extended glycan receptors on virus binding, infection, and growth, we have engineered N-glycan extended (NExt) cell lines by overexpressing β3-Ν-acetylglucosaminyltransferase 2 in MDCK, SIAT, and hCK cell lines. Of these, SIAT-NExt cells exhibit markedly increased binding of H3 HAs and susceptibility to infection by recent H3N2 virus strains, but without impacting final virus titers. Glycome analysis of these cell lines and allantoic and amniotic egg membranes provide insights into the importance of extended glycan receptors for growth of recent H3N2 viruses and relevance to their production for cell- and egg-based vaccines.
    MeSH term(s) Animals ; Dogs ; Humans ; Influenza, Human/prevention & control ; Influenza A Virus, H3N2 Subtype ; Madin Darby Canine Kidney Cells ; Influenza Vaccines ; Polysaccharides/metabolism ; Hemagglutinin Glycoproteins, Influenza Virus
    Chemical Substances Influenza Vaccines ; Polysaccharides ; Hemagglutinin Glycoproteins, Influenza Virus
    Language English
    Publishing date 2023-10-04
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-023-41908-0
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Measurement of erythrocyte membrane mannoses to assess splenic function.

    Cao, Huan / Mathur, Abhinav / Robertson, Charlotte / Antonopoulos, Aristotelis / Henderson, Sadie / Girard, Louis-Pierre / Wong, Jin Hien / Davie, Adam / Wright, Sonja / Brewin, John / Rees, David C / Dell, Anne / Haslam, Stuart M / Vickers, Mark A

    British journal of haematology

    2022  Volume 198, Issue 1, Page(s) 155–164

    Abstract: Red blood cells (RBCs) lose plasma membrane in the spleen as they age, but the cells and molecules involved are yet to be identified. Sickle cell disease and infection by Plasmodium falciparum cause oxidative stress that induces aggregates of cross- ... ...

    Abstract Red blood cells (RBCs) lose plasma membrane in the spleen as they age, but the cells and molecules involved are yet to be identified. Sickle cell disease and infection by Plasmodium falciparum cause oxidative stress that induces aggregates of cross-linked proteins with N-linked high-mannose glycans (HMGs). These glycans can be recognised by mannose-binding lectins, including the mannose receptor (CD206), expressed on macrophages and specialised phagocytic endothelial cells in the spleen to mediate the extravascular haemolysis characteristic of these diseases. We postulated this system might also mediate removal of molecules and membrane in healthy individuals. Surface expression of HMGs on RBCs from patients who had previously undergone splenectomy was therefore assessed: high levels were indeed observable as large membrane aggregates. Glycomic analysis by mass spectrometry identified a mixture of Man
    MeSH term(s) Endothelial Cells ; Erythrocyte Membrane ; Humans ; Mannose ; Polysaccharides ; Splenectomy
    Chemical Substances Polysaccharides ; Mannose (PHA4727WTP)
    Language English
    Publishing date 2022-04-12
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 80077-6
    ISSN 1365-2141 ; 0007-1048
    ISSN (online) 1365-2141
    ISSN 0007-1048
    DOI 10.1111/bjh.18164
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Vulpeculin: a novel and abundant lipocalin in the urine of the common brushtail possum,

    Loxley, Grace M / Hooks, David O / Antonopoulos, Aristotelis / Dell, Anne / Haslam, Stuart M / Linklater, Wayne L / Hurst, Jane L / Beynon, Robert J

    Open biology

    2020  Volume 10, Issue 10, Page(s) 200218

    Abstract: Lipocalins are a family of secreted proteins. They are capable of binding small lipophilic compounds and have been extensively studied for their role in chemosignalling in rodent urine. Urine of the common brushtail possum ( ...

    Abstract Lipocalins are a family of secreted proteins. They are capable of binding small lipophilic compounds and have been extensively studied for their role in chemosignalling in rodent urine. Urine of the common brushtail possum (
    MeSH term(s) Animals ; Biomarkers/urine ; Chromatography, Liquid ; Computational Biology/methods ; Databases, Chemical ; Databases, Genetic ; Gene Expression ; Lipocalins/pharmacokinetics ; Lipocalins/urine ; Mass Spectrometry/methods ; Phylogeny ; Polysaccharides ; Proteins/chemistry ; Proteinuria ; Trichosurus/urine
    Chemical Substances Biomarkers ; Lipocalins ; Polysaccharides ; Proteins
    Language English
    Publishing date 2020-10-07
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2630944-0
    ISSN 2046-2441 ; 2046-2441
    ISSN (online) 2046-2441
    ISSN 2046-2441
    DOI 10.1098/rsob.200218
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article: Serum IgA1 shows increased levels of

    Lomax-Browne, Hannah J / Robertson, Claire / Antonopoulos, Aristotelis / Leathem, Anthony J C / Haslam, Stuart M / Dell, Anne / Dwek, Miriam V

    Interface focus

    2019  Volume 9, Issue 2, Page(s) 20180079

    Abstract: ... The ... ...

    Abstract The lectin
    Language English
    Publishing date 2019-02-15
    Publishing country England
    Document type Journal Article
    ISSN 2042-8898
    ISSN 2042-8898
    DOI 10.1098/rsfs.2018.0079
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Discovery of O-Linked Carbohydrate on HIV-1 Envelope and Its Role in Shielding against One Category of Broadly Neutralizing Antibodies.

    Silver, Zachary A / Antonopoulos, Aristotelis / Haslam, Stuart M / Dell, Anne / Dickinson, Gordon M / Seaman, Michael S / Desrosiers, Ronald C

    Cell reports

    2020  Volume 30, Issue 6, Page(s) 1862–1869.e4

    Abstract: Approximately 50% of the mass of the Envelope (Env) glycoprotein surface subunit (gp120) of human immunodeficiency virus type 1 (HIV-1) is composed of N-linked carbohydrate. Until now, the dogma has been that HIV-1 lacks O-linked carbohydrate on Env. ... ...

    Abstract Approximately 50% of the mass of the Envelope (Env) glycoprotein surface subunit (gp120) of human immunodeficiency virus type 1 (HIV-1) is composed of N-linked carbohydrate. Until now, the dogma has been that HIV-1 lacks O-linked carbohydrate on Env. Here we show that a subset of patient-derived HIV-1 isolates contain O-linked carbohydrate on the variable 1 (V1) domain of Env gp120. We demonstrate the presence of this O-glycosylation both on virions and on gp120 expressed as a secreted protein. Further, we establish that these O-linked glycans can confer a more than 1,000-fold decrease in neutralization sensitivity (IC
    MeSH term(s) Broadly Neutralizing Antibodies/metabolism ; HIV Antibodies/immunology ; HIV-1/immunology ; Humans
    Chemical Substances Broadly Neutralizing Antibodies ; HIV Antibodies
    Language English
    Publishing date 2020-02-01
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2649101-1
    ISSN 2211-1247 ; 2211-1247
    ISSN (online) 2211-1247
    ISSN 2211-1247
    DOI 10.1016/j.celrep.2020.01.056
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: Site-specific characterization of SARS-CoV-2 spike glycoprotein receptor-binding domain.

    Antonopoulos, Aristotelis / Broome, Steven / Sharov, Victor / Ziegenfuss, Christopher / Easton, Richard L / Panico, Maria / Dell, Anne / Morris, Howard R / Haslam, Stuart M

    Glycobiology

    2020  Volume 31, Issue 3, Page(s) 181–187

    Abstract: The novel coronavirus SARS-CoV-2, the infective agent causing COVID-19, is having a global impact both in terms of human disease as well as socially and economically. Its heavily glycosylated spike glycoprotein is fundamental for the infection process, ... ...

    Abstract The novel coronavirus SARS-CoV-2, the infective agent causing COVID-19, is having a global impact both in terms of human disease as well as socially and economically. Its heavily glycosylated spike glycoprotein is fundamental for the infection process, via its receptor-binding domains interaction with the glycoprotein angiotensin-converting enzyme 2 on human cell surfaces. We therefore utilized an integrated glycomic and glycoproteomic analytical strategy to characterize both N- and O- glycan site-specific glycosylation within the receptor-binding domain. We demonstrate the presence of complex-type N-glycans with unusual fucosylated LacdiNAc at both sites N331 and N343 and a single site of O-glycosylation on T323.
    MeSH term(s) Angiotensin-Converting Enzyme 2/chemistry ; Angiotensin-Converting Enzyme 2/metabolism ; Binding Sites/genetics ; COVID-19/metabolism ; COVID-19/virology ; Carbohydrate Conformation ; Carbohydrate Sequence ; Glycomics ; Glycosylation ; HEK293 Cells ; Host Microbial Interactions ; Humans ; Pandemics ; Protein Binding ; Protein Interaction Domains and Motifs ; Proteomics ; Receptors, Virus/chemistry ; Receptors, Virus/metabolism ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; SARS-CoV-2/chemistry ; SARS-CoV-2/genetics ; SARS-CoV-2/metabolism ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; Spike Glycoprotein, Coronavirus/chemistry ; Spike Glycoprotein, Coronavirus/genetics ; Spike Glycoprotein, Coronavirus/metabolism
    Chemical Substances Receptors, Virus ; Recombinant Proteins ; Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2 ; ACE2 protein, human (EC 3.4.17.23) ; Angiotensin-Converting Enzyme 2 (EC 3.4.17.23)
    Keywords covid19
    Language English
    Publishing date 2020-09-11
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1067689-2
    ISSN 1460-2423 ; 0959-6658
    ISSN (online) 1460-2423
    ISSN 0959-6658
    DOI 10.1093/glycob/cwaa085
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: Analysis of N- and O-Linked Glycosylation: Differential Glycosylation after Rat Spinal Cord Injury.

    Osimanjiang, Wupu / Roballo, Kelly C Santos / Houck, Brenda D / Ito, Mai / Antonopoulos, Aristotelis / Dell, Anne / Haslam, Stuart M / Bushman, Jared S

    Journal of neurotrauma

    2020  Volume 37, Issue 18, Page(s) 1954–1962

    Abstract: Glycosylation is a fundamental cellular process that has a dramatic impact on the functionality of glycoconjugates such as proteins or lipids and mediates many different biological interactions including cell migration, cellular signaling, and synaptic ... ...

    Abstract Glycosylation is a fundamental cellular process that has a dramatic impact on the functionality of glycoconjugates such as proteins or lipids and mediates many different biological interactions including cell migration, cellular signaling, and synaptic interactions in the nervous system. In spinal cord injury (SCI), all of these cellular processes are altered, but the potential contributions of glycosylation changes to these alterations has not been thoroughly investigated. We studied the glycosylation of injured spinal cord tissue from rats that received a contusion SCI. The N- and O-linked glycosylation was assessed at 3 and 14 days post-injury (DPI), and compared with uninjured control and time-matched sham spinal tissue. Matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF MS) and tandem MS (MS/MS) were performed to analyze carbohydrate structures. Results revealed diverse and abundant glycosylation in all groups, with some carbohydrate structures differentially produced in SCI animals compared with uninjured controls and shams. One such change occurred in the abundance of the Sda structure, Neu5Ac-α-(2,3)-[GalNAc-β-(1,4)-]Gal-β-(1,4)-GlcNAc, which was increased in SCI samples compared with shams and non-injured controls. Immunohistochemistry (IHC) and western blot were performed on SCI and sham samples using the CT1 antibody, which recognizes the terminal trisaccharide of Sda with high specificity. Both of these metrics confirmed elevated Sda structure in SCI tissue, where IHC further showed that Sda is expressed mainly by microglia. The results of these studies suggest that SCI causes a significant alteration in N- and O-linked glycosylation.
    MeSH term(s) Animals ; Glycosylation ; Male ; Mass Spectrometry/methods ; Mass Spectrometry/standards ; Microglia/metabolism ; Microglia/pathology ; Rats ; Rats, Sprague-Dawley ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization/methods ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization/standards ; Spinal Cord Injuries/metabolism ; Spinal Cord Injuries/pathology
    Language English
    Publishing date 2020-06-26
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 645092-1
    ISSN 1557-9042 ; 0897-7151
    ISSN (online) 1557-9042
    ISSN 0897-7151
    DOI 10.1089/neu.2019.6974
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Discovery of O-Linked Carbohydrate on HIV-1 Envelope and Its Role in Shielding against One Category of Broadly Neutralizing Antibodies

    Zachary A. Silver / Aristotelis Antonopoulos / Stuart M. Haslam / Anne Dell / Gordon M. Dickinson / Michael S. Seaman / Ronald C. Desrosiers

    Cell Reports, Vol 30, Iss 6, Pp 1862-1869.e

    2020  Volume 4

    Abstract: Summary: Approximately 50% of the mass of the Envelope (Env) glycoprotein surface subunit (gp120) of human immunodeficiency virus type 1 (HIV-1) is composed of N-linked carbohydrate. Until now, the dogma has been that HIV-1 lacks O-linked carbohydrate on ...

    Abstract Summary: Approximately 50% of the mass of the Envelope (Env) glycoprotein surface subunit (gp120) of human immunodeficiency virus type 1 (HIV-1) is composed of N-linked carbohydrate. Until now, the dogma has been that HIV-1 lacks O-linked carbohydrate on Env. Here we show that a subset of patient-derived HIV-1 isolates contain O-linked carbohydrate on the variable 1 (V1) domain of Env gp120. We demonstrate the presence of this O-glycosylation both on virions and on gp120 expressed as a secreted protein. Further, we establish that these O-linked glycans can confer a more than 1,000-fold decrease in neutralization sensitivity (IC50) to V3-glycan broadly neutralizing antibodies. These findings uncover a structural modification to the HIV-1 Env and suggest a functional role in promoting viral escape from one category of broadly neutralizing antibodies. : Silver et al. demonstrate that certain HIV-1 isolates possess O-linked carbohydrate on their Envelope glycoprotein. These sugars allow the virus to evade V3-glycan broadly neutralizing antibodies. This work identifies a post-translational modification to the HIV-1 Envelope and sheds light on its role in shielding against the host antibody response. Keywords: HIV-1, Envelope, gp120, V1 domain, O-glycosylation, broadly neutralizing antibodies, immune evasion, escape mechanism
    Keywords Biology (General) ; QH301-705.5
    Subject code 570
    Language English
    Publishing date 2020-02-01T00:00:00Z
    Publisher Elsevier
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  10. Article: Discrimination of varietal wines according to their volatiles.

    Dourtoglou, Vassilis / Antonopoulos, Aristotelis / Dourtoglou, Thalia / Lalas, Stavros

    Food chemistry

    2014  Volume 159, Page(s) 181–187

    Abstract: A method is being proposed in order to discriminate bottled wines of different varieties when no other information is known. The advantages of the method consist in the fact that anyone who wants to certify the variety, which is written on the label or ... ...

    Abstract A method is being proposed in order to discriminate bottled wines of different varieties when no other information is known. The advantages of the method consist in the fact that anyone who wants to certify the variety, which is written on the label or the area of origin, can use such a technique to achieve the conformity. Additionally, the method can be easily applied by laboratories equipped with a GC. The differentiation has been achieved by using only seven of the total extracted volatiles, mainly higher alcohols and higher alcohol esters, namely 3-methyl-1-butanol, 2,3-butanediol, ethyl lactate, 3-methyl-1-butyl acetate, 2-phenylethanol, phenyl ethyl acetate and p-hydroxy phenyl ethanol. These key compounds are not relevant to a single variety. The proposed method does not take into account variables such as the year of vintage and fermentation procedures (agitation, temperature).
    MeSH term(s) Alcohols/analysis ; Chromatography, Gas ; Fermentation ; Humans ; Wine/analysis
    Chemical Substances Alcohols
    Language English
    Publishing date 2014-09-15
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 243123-3
    ISSN 1873-7072 ; 0308-8146
    ISSN (online) 1873-7072
    ISSN 0308-8146
    DOI 10.1016/j.foodchem.2014.03.032
    Database MEDical Literature Analysis and Retrieval System OnLINE

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