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author:("He, viale")
1.  CD45 mediated fodrin cleavage during galectin-1 mediated T cell death promotes phagocytic clearance of dying cells 
Disassembly and phagocytic removal of dying cells is critical to maintain immune homeostasis. The factors regulating fragmentation and uptake of dying lymphocytes are not well understood. Degradation of fodrin, a cytoskeletal linker molecule that attaches CD45 to the actin cytoskeleton, has been described in apoptotic cells, although no specific initiator of fodrin degradation has been identified. CD45 is a glycoprotein receptor for galectin-1, an endogenous lectin that can trigger lymphocyte apoptosis. CD45 is not required for membrane changes or DNA degradation during galectin-1 death. However, here we show that fodrin degradation occurs during galectin-1 T cell death, and CD45 is essential for fodrin degradation to occur. In the absence of CD45 and fodrin degradation, cell death is not accompanied by membrane blebbing, indicating that fodrin degradation occurs via a distinct pathway compared to the pathway that initiates apoptotic membrane changes and DNA degradation. Moreover, there is slower phagocytic uptake of cells in which fodrin degradation is blocked relative to cells in which CD45-mediated fodrin degradation occurs. These studies identify a novel role for CD45 in regulating cellular disassembly and promoting phagocytic clearance during galectin-1 induced T cell death.
doi:10.4049/jimmunol.0804329
PMCID: PMC3541008  PMID: 19454697
2.  Galectin-1 induces nuclear translocation of Endonuclease G in caspase- and cytochrome c-independent T cell death1 
Cell death and differentiation  2004;11(12):1277-1286.
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.
doi:10.1038/sj.cdd.4401485
PMCID: PMC1201488  PMID: 15297883
galectin; apoptosis; T lymphocyte; Endonuclease G; human; phosphatidylserine (PS); z-Val-Ala-Asp(OMe)-CH2F (zVAD-fmk); z-Asp-Glu-Val-Asp(OMe)-CH2F (zDEVD-fmk); poly(ADP-ribose)polymerase (PARP); 7-amino-actinomycin D (7AAD); z-Asp-Glu-Val-Asp-7-amino-4-trifluoromethylcoumarin (zDEVD-AFC); mitochondrial membrane potential (Δψm); endonuclease G (EndoG); 10-N-nonyl acridine orange (NAO); Apoptosis inducing factor (AIF); truncated Bid (tBid); propidium iodide (PI); fluorescein isothiocyanate (FITC)

Results 1-2 (2)