Open Access

The lectin-binding pattern of nucleolin and its interaction with endogenous galectin-3

  • Dorota Hoja-Łukowicz1Email author,
  • Sylwia Kedracka-Krok2, 3,
  • Weronika Duda4 and
  • Anna Lityńska1
Cellular & Molecular Biology LettersAn International Journal201419:206

Received: 27 March 2014

Accepted: 13 August 2014

Published: 29 August 2014


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.


Glycosylation of nucleolin Galectin-3 Melanoma Mass spectrometry Confocal microscopy Lectin assay Co-immunoprecipitation