Abstract
Galectin-1, a mammalian lectin expressed in many tissues, induces death of diverse cell types, including lymphocytes and tumor cells. The galectin-1 T cell death pathway is novel and distinct from other death pathways, including those initiated by Fas and corticosterolds. We have found that galectin-1 binding to human T cell lines triggered rapid translocation of endonuclease G from mitochondria to nuclei. However, endonuclease G nuclear translocation occurred without cytochrome c release from mitochondria, without nuclear translocation of apoptosis-inducing factor, and prior to loss of mitochondrial membrane potential. Galectin-1 treatment did not result in caspase activation, nor was death blocked by caspase inhibitors. However, galectin-1 cell death was inhibited by intracellular expression of galectin-3, and galectin-3 expression inhibited the eventual loss of mitochondrial membrane potential. Galectin-1-induced cell death proceeds via a caspase-independent pathway that involves a unique pattern of mitochondrial events, and different galectin family members can coordinately regulate susceptibility to cell death.
Original language | English (US) |
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Pages (from-to) | 1277-1286 |
Number of pages | 10 |
Journal | Cell Death and Differentiation |
Volume | 11 |
Issue number | 12 |
DOIs | |
State | Published - Dec 2004 |
Externally published | Yes |
Keywords
- Apoptosis
- Endonuclease G
- Galectin
- Human
- T lymphocyte
ASJC Scopus subject areas
- Cell Biology