Abstract
We previously identified a novel N-terminally processed form of galectin-1, galectin-1β (Gal-1β) whose expression was induced by ΔFosB. In the present study, the biochemical properties and biological functions of Gal-1β were compared with the full-length form of galectin-1 (Gal-1α). We first purified recombinant mouse Gal-1α and β (rmGal-1α, β) to near homogeneity. The rmGal-1α exists as a monomer under oxidized conditions and forms a dimer under reduced conditions, while the rmGal-1β exists as a monomer regardless of redox conditions. The affinity of rmGal-1β to β-lactose was approximately two-fold lower than that of rmGal-1α under reduced conditions. The viability of Jurkat cells efficiently decreased when they were exposed to rmGal-1α, however, rmGal-1β barely induced such a reduction. In contrast, both rmGal-1α and rmGal-1β exhibited an equivalent capacity to promote axonal regeneration from the dorsal root ganglion explants. Our results suggest that the biochemical properties of rmGal-1β determine its biological functions.
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Abbreviations
- Gal-1:
-
Galectin-1
- AP-1:
-
activator protein-1
- β-ME:
-
β-mercaptoethanol
- CD:
-
circular dichroism
- DRG:
-
dorsal root ganglion
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Acknowledgements
We extend our special thanks to Drs. S Hirano, M Furuichi, Y Tominaga, T Kadoya, S Kanba and Y Ohnishi for helpful discussions, and to Dr. B Quinn for useful comments on this manuscript.
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Miura, T., Takahashi, M., Horie, H. et al. Galectin-1β, a natural monomeric form of galectin-1 lacking its six amino-terminal residues promotes axonal regeneration but not cell death. Cell Death Differ 11, 1076–1083 (2004). https://doi.org/10.1038/sj.cdd.4401462
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DOI: https://doi.org/10.1038/sj.cdd.4401462
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