Journal
CELL DEATH AND DIFFERENTIATION
Volume 11, Issue 12, Pages 1277-1286Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/sj.cdd.4401485
Keywords
galectin; apoptosis; T lymphocyte; endonuclease G; human
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Funding
- NIAID NIH HHS [T32 AI052031, AI20958, R01 AI020958, AI52031] Funding Source: Medline
- NIGMS NIH HHS [GM57158, R01 GM057158, R01 GM063281, GM63281, T32 GM008042, GM08042] Funding Source: Medline
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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 corticosteroids. 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.
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