title: The lectin-binding pattern of nucleolin and its interaction with endogenous galectin-3.
abstract: Unlike nuclear nucleolin, surface-expressed and cytoplasmic nucleolin exhibit Tn antigen. Here, we show localization-dependent differences in the glycosylation and proteolysis patterns of nucleolin. Our results provide evidence for different paths of nucleolin proteolysis in the nucleus, in the cytoplasm, and on the cell surface. We found that full-length nucleolin and some proteolytic fragments coexist within live cells and are not solely the result of the preparation procedure. Extranuclear nucleolin undergoes N- and O-glycosylation, and unlike cytoplasmic nucleolin, membrane-associated nucleolin is not fucosylated. Here, we show for the first time that nucleolin and endogenous galectin-3 exist in the same complexes in the nucleolus, the cytoplasm, and on the cell surface of melanoma cells. Assessments of the interaction of nucleolin with galectin-3 revealed nucleolar co-localization in interphase, suggesting that galectin-3 may be involved in DNA organization and ribosome biogenesis.
authors.affiliation: Department of Glycoconjugate Biochemistry, Institute of Zoology, Jagiellonian University, 9 Gronostajowa Street, 30-387, Kraków, Poland, dorota.hoja-lukowicz@uj.edu.pl.
authors.forename: Dorota
authors.initials: D
authors.lastname: Hoja-Łukowicz
authors.forename: Sylwia
authors.initials: S
authors.lastname: Kedracka-Krok
authors.forename: Weronika
authors.initials: W
authors.lastname: Duda
authors.forename: Anna
authors.initials: A
authors.lastname: Lityńska
mesh_terms: D015153:Blotting, Western; D002458:Cell Fractionation; D045744:Cell Line, Tumor; D002462:Cell Membrane / Q000378:metabolism; D002466:Cell Nucleolus / Q000378:metabolism; D002467:Cell Nucleus / Q000378:metabolism; D003593:Cytoplasm / Q000378:metabolism; D037502:Galectin 3 / Q000378:metabolism*; D006031:Glycosylation; D006801:Humans; D037102:Lectins / Q000378:metabolism*; D013058:Mass Spectrometry; D008545:Melanoma / Q000378:metabolism / Q000473:pathology; D018613:Microscopy, Confocal; D010750:Phosphoproteins / Q000378:metabolism*; D011485:Protein Binding; D059748:Proteolysis; D016601:RNA-Binding Proteins / Q000378:metabolism*; D000097796:Nucleolin
chemical_list: D037502:Galectin 3; D037102:Lectins; D010750:Phosphoproteins; D016601:RNA-Binding Proteins; D000097796:Nucleolin