Galectin-1β, a natural monomeric form of galectin-1 lacking its six amino-terminal residues promotes axonal regeneration but not cell death

T. Miura, M. Takahashi, H. Horie, H. Kurushima, D. Tsuchimoto, K. Sakumi, Y. Nakabeppu

Research output: Contribution to journalArticle

30 Citations (Scopus)

Abstract

We previously identified a novel N-terminally processed form of galectin-1, galectin-1(Gal-1β) whose expression was induced by ΔFosB. In the present study, the biochemical properties and biological functions of Gal-1were 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.

Original languageEnglish
Pages (from-to)1076-1083
Number of pages8
JournalCell Death and Differentiation
Volume11
Issue number10
DOIs
Publication statusPublished - Oct 2004

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cell Biology

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