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  1. Article ; Online: The Exosome-like Vesicles of

    Natali, Lautaro / Luna Pizarro, Gabriel / Moyano, Sofía / de la Cruz-Thea, Benjamin / Musso, Juliana / Rópolo, Andrea S / Eichner, Norbert / Meister, Gunter / Musri, Melina M / Feliziani, Constanza / Touz, María C

    International journal of molecular sciences

    2023  Volume 24, Issue 11

    Abstract: The genetically related assemblages of the intestinal protozoa ... ...

    Abstract The genetically related assemblages of the intestinal protozoa parasite
    MeSH term(s) Humans ; Animals ; Giardia/genetics ; Parasites ; RNA/metabolism ; Exosomes/genetics ; Exosomes/metabolism ; Giardiasis/parasitology ; RNA, Transfer/metabolism ; RNA, Ribosomal/metabolism
    Chemical Substances RNA (63231-63-0) ; RNA, Transfer (9014-25-9) ; RNA, Ribosomal
    Language English
    Publishing date 2023-05-31
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms24119559
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Exosome Biogenesis in the Protozoa Parasite

    Moyano, Sofía / Musso, Juliana / Feliziani, Constanza / Zamponi, Nahuel / Frontera, Lorena Soledad / Ropolo, Andrea Silvana / Lanfredi-Rangel, Adriana / Lalle, Marco / Touz, María

    Cells

    2019  Volume 8, Issue 12

    Abstract: ...

    Abstract :
    MeSH term(s) Animals ; Blotting, Western ; Dynamic Light Scattering ; Endosomal Sorting Complexes Required for Transport/metabolism ; Exosomes/metabolism ; Exosomes/ultrastructure ; Giardia lamblia/metabolism ; Giardia lamblia/ultrastructure ; Microscopy, Electron
    Chemical Substances Endosomal Sorting Complexes Required for Transport
    Language English
    Publishing date 2019-12-09
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2661518-6
    ISSN 2073-4409 ; 2073-4409
    ISSN (online) 2073-4409
    ISSN 2073-4409
    DOI 10.3390/cells8121600
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Lactoferrin and lactoferricin endocytosis halt Giardia cell growth and prevent infective cyst production.

    Frontera, Lorena S / Moyano, Sofía / Quassollo, Gonzalo / Lanfredi-Rangel, Adriana / Rópolo, Andrea S / Touz, María C

    Scientific reports

    2018  Volume 8, Issue 1, Page(s) 18020

    Abstract: Lactoferrin (LF) is an 80 KDa iron-binding glycoprotein that plays a significant role in the innate immune system and is considered to be an important microbicide molecule. It has been suggested to be effective in the treatment of giardiasis, an ... ...

    Abstract Lactoferrin (LF) is an 80 KDa iron-binding glycoprotein that plays a significant role in the innate immune system and is considered to be an important microbicide molecule. It has been suggested to be effective in the treatment of giardiasis, an intestinal disease caused by the protozoan parasite G. lamblia. However, the molecular mechanisms by which LF exerts its effect on this parasite are unknown. Most of the microbicidal activity of human or bovine LF (hLF or bLF) has been associated with the N-terminal region of the mature LF - lactoferricin (LFcin). LFcin is produced by pepsin cleavage of the native protein in vitro and likely in vivo. In this work, we analyse the participation of the endocytic machinery of G. lamblia in the internalization of bLF and bLFcin and their effects on cell homeostasis. Our results show that, when bLF or bLFcin are internalized by receptor-mediated endocytosis, cell growth stops, and morphological changes are produced in the trophozoites, which ultimately will produce immature cysts. Our findings contribute to disclose the fine mechanism by which bLF and bLFcin may function as an antigiardial molecule and why they have therapeutic potential to eradicate giardiasis.
    MeSH term(s) Animals ; Cattle ; Cell Proliferation/drug effects ; Cells, Cultured ; Cysts/metabolism ; Cysts/parasitology ; Cysts/pathology ; Cysts/prevention & control ; Dose-Response Relationship, Drug ; Endocytosis/physiology ; Giardia/drug effects ; Giardia/growth & development ; Giardia/metabolism ; Giardiasis/parasitology ; Giardiasis/pathology ; Humans ; Lactoferrin/pharmacokinetics ; Lactoferrin/pharmacology ; Protein Binding ; Receptors, LDL/metabolism
    Chemical Substances LTF protein, human ; Receptors, LDL ; lactoferricin B (146897-68-9) ; Lactoferrin (EC 3.4.21.-)
    Language English
    Publishing date 2018-12-21
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/s41598-018-36563-1
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article: Vestiges of Ent3p/Ent5p function in the giardial epsin homolog.

    Feliziani, Constanza / Valdez Taubas, Javier / Moyano, Sofía / Quassollo, Gonzalo / Poprawski, Joanna E / Wendland, Beverly / Touz, Maria C

    Biochimica et biophysica acta

    2016  Volume 1863, Issue 4, Page(s) 749–759

    Abstract: An accurate way to characterize the functional potential of a protein is to analyze recognized protein domains encoded by the genes in a given group. The epsin N-terminal homology (ENTH) domain is an evolutionarily conserved protein module found ... ...

    Abstract An accurate way to characterize the functional potential of a protein is to analyze recognized protein domains encoded by the genes in a given group. The epsin N-terminal homology (ENTH) domain is an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated trafficking. In this work, we investigate the function of the single ENTH-containing protein from the protist Giardia lamblia by testing its function in Saccharomyces cerevisiae. This protein, named GlENTHp (for G. lamblia ENTH protein), is involved in Giardia in endocytosis and in protein trafficking from the ER to the vacuoles, fulfilling the function of the ENTH proteins epsin and epsinR, respectively. There are two orthologs of epsin, Ent1p and Ent2p, and two orthologs of epsinR, Ent3p and Ent5p in S. cerevisiae. Although the expression of GlENTHp neither complemented growth in the ent1Δent2Δ mutant nor restored the GFP-Cps1 vacuolar trafficking defect in ent3Δent5Δ, it interfered with the normal function of Ent3/5 in the wild-type strain. The phenotype observed is linked to a defect in Cps1 localization and α-factor mating pheromone maturation. The finding that GlENTHp acts as dominant negative epsinR in yeast cells reinforces the phylogenetic data showing that GlENTHp belongs to the epsinR subfamily present in eukaryotes prior to their evolution into different taxa.
    MeSH term(s) Adaptor Proteins, Vesicular Transport/chemistry ; Adaptor Proteins, Vesicular Transport/genetics ; Adaptor Proteins, Vesicular Transport/physiology ; Amino Acid Sequence ; Animals ; Evolution, Molecular ; Genes, Dominant ; Giardia lamblia/genetics ; Humans ; Organisms, Genetically Modified ; Protein Structure, Tertiary/genetics ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae Proteins/chemistry ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/physiology ; Sequence Homology
    Chemical Substances Adaptor Proteins, Vesicular Transport ; Ent3 protein, S cerevisiae ; Ent5 protein, S cerevisiae ; Saccharomyces cerevisiae Proteins ; epsin
    Language English
    Publishing date 2016-04
    Publishing country Netherlands
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    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.bbamcr.2016.02.001
    Database MEDical Literature Analysis and Retrieval System OnLINE

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