Galectin-3 binds to CD45 on diffuse large B-cell lymphoma cells to regulate susceptibility to cell death.
Authors:Clark MC, Pang M, Hsu DK, Liu FT, de Vos S, Gascoyne RD, Said J, Baum LG,
Journal:Blood
PubMed ID:23065155
Diffuse large B-cell lymphoma (DLBCL) is the most common non-Hodgkin lymphoma and an aggressive malignancy. Galectin-3 (gal-3), the only antiapoptotic member of the galectin family, is overexpressed in DLBCL. While gal-3 can localize to intracellular sites, gal-3 is secreted by DLBCL cells and binds back to the cell surface in ... More
Reovirus infection or ectopic expression of outer capsid protein micro1 induces apoptosis independently of the cellular proapoptotic proteins Bax and Bak.
Authors:Wisniewski ML, Werner BG, Hom LG, Anguish LJ, Coffey CM, Parker JS,
Journal:J Virol
PubMed ID:20980509
Mammalian orthoreoviruses induce apoptosis in vivo and in vitro; however, the specific mechanism by which apoptosis is induced is not fully understood. Recent studies have indicated that the reovirus outer capsid protein µ1 is the primary determinant of reovirus-induced apoptosis. Ectopically expressed µ1 induces apoptosis and localizes to intracellular membranes. ... More
Interrelated roles for Mcl-1 and BIM in regulation of TRAIL-mediated mitochondrial apoptosis.
Authors:Han J, Goldstein LA, Gastman BR, Rabinowich H
Journal:J Biol Chem
PubMed ID:16478725
The current study demonstrates a novel cross-talk mechanism between the TRAIL receptor death signaling pathway and the mitochondria. This newly identified pathway is regulated at the mitochondrial outer membrane by a complex between the prosurvival Bcl-2 member, Mcl-1 and the BH3-only protein, Bim. Under non-apoptotic conditions, Bim is sequestered by ... More
Assay of caspase activation in situ combined with probing plasma membrane integrity to detect three distinct stages of apoptosis.
Authors:Smolewski P, Grabarek J, Halicka HD, Darzynkiewicz Z
Journal:J Immunol Methods
PubMed ID:12072182
Activation of cysteine-aspartic acid specific proteases (caspases) in situ, in live cells, can be detected using fluorochrome-labeled inhibitors of caspases (FLICA), the reagents that covalently bind to the active center of these enzymes. In the present study, this assay was combined with a probe of plasma membrane capacity to exclude ... More
Interactions of fluorochrome-labeled caspase inhibitors with apoptotic cells: a caution in data interpretation.
Authors:Pozarowski P, Huang X, Halicka DH, Lee B, Johnson G, Darzynkiewicz Z
Journal:Cytometry A
PubMed ID:12938188
BACKGROUND: Fluorochrome-labeled inhibitors of caspases (FLICA, e.g., FAM-VAD-FMK, FITC-VAD-FMK) have been designed as affinity labels of the enzyme active center of caspases Their binding by apoptotic cells was interpreted as reflecting activation of caspases. We have recently observed, however, that their binding is more complex and may involve additional mechanisms. ... More