Abstract
The extracellular functions of galectin-7 (p53-induced gene 1) are largely unknown. On the surface of neuroblastoma cells (SK-N-MC), the increased GM 1 density, a result of upregulated ganglioside sialidase activity, is a key factor for the switch from proliferation to differentiation. We show by solid-phase and cell assays that the sugar chain of this ganglioside is a ligand for galectin-7. In serum-supplemented proliferation assays, galectin-7 reduced neuroblastoma cell growth without the appearance of features characteristic for classical apoptosis. The presence of galectin-3 blocked this effect, which mechanistically resembles that of galectin-1. By virtue of carbohydrate binding, galectin-7 thus exerts neuroblastoma growth control similar to galectin-1 despite their structural differences. In addition to p53-linked proapoptotic activity intracellularly, galectin-7, acting as a lectin on the cell surface, appears to be capable of reducing cancer cell proliferation in susceptible systems.
Original language | English (US) |
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Pages (from-to) | 6277-6288 |
Number of pages | 12 |
Journal | Oncogene |
Volume | 22 |
Issue number | 40 |
DOIs | |
State | Published - Sep 18 2003 |
Keywords
- Apoptosis
- Cell growth
- Galectin
- Ganglioside
- Mass spectrometry
- Neuroblastoma
ASJC Scopus subject areas
- Molecular Biology
- Cancer Research
- Genetics