Nuclear localized protein-1 (Nulp1) increases cell death of human osteosarcoma cells and binds the X-linked inhibitor of apoptosis protein

2008 ◽  
Vol 366 (2) ◽  
pp. 432-437 ◽  
Author(s):  
Håkan Steen ◽  
Dan Lindholm
Keyword(s):  
Cell Death ◽  
Inhibitor Of Apoptosis ◽  
Osteosarcoma Cells ◽  
Inhibitor Of Apoptosis Protein ◽  
Human Osteosarcoma ◽  
Human Osteosarcoma Cells ◽  
Apoptosis Protein

scholarly journals Pseudomonas aeruginosaDelays Kupffer Cell Death via Stabilization of the X-Chromosome-Linked Inhibitor of Apoptosis Protein

2007 ◽  
Vol 179 (1) ◽  
pp. 505-513 ◽  
Author(s):  
Alix Ashare ◽  
Martha M. Monick ◽  
Amanda B. Nymon ◽  
John M. Morrison ◽  
Matthew Noble ◽  
...  
Keyword(s):  
Cell Death ◽  
X Chromosome ◽  
Kupffer Cell ◽  
Inhibitor Of Apoptosis ◽  
Inhibitor Of Apoptosis Protein ◽  
Apoptosis Protein

scholarly journals Diablo Promotes Apoptosis by Removing Miha/Xiap from Processed Caspase 9

2001 ◽  
Vol 152 (3) ◽  
pp. 483-490 ◽  
Author(s):  
Paul G. Ekert ◽  
John Silke ◽  
Christine J. Hawkins ◽  
Anne M. Verhagen ◽  
David L. Vaux
Keyword(s):  
Cell Death ◽  
Cytochrome C ◽  
Caspase 3 ◽  
Direct Interaction ◽  
Inhibitor Of Apoptosis ◽  
Caspase 9 ◽  
Inhibitor Of Apoptosis Protein ◽  
Grim Reaper ◽  
Apoptosis Protein ◽  
Mammalian Protein

MIHA is an inhibitor of apoptosis protein (IAP) that can inhibit cell death by direct interaction with caspases, the effector proteases of apoptosis. DIABLO is a mammalian protein that can bind to IAPs and antagonize their antiapoptotic effect, a function analogous to that of the proapoptotic Drosophila molecules, Grim, Reaper, and HID. Here, we show that after UV radiation, MIHA prevented apoptosis by inhibiting caspase 9 and caspase 3 activation. Unlike Bcl-2, MIHA functioned after release of cytochrome c and DIABLO from the mitochondria and was able to bind to both processed caspase 9 and processed caspase 3 to prevent feedback activation of their zymogen forms. Once released into the cytosol, DIABLO bound to MIHA and disrupted its association with processed caspase 9, thereby allowing caspase 9 to activate caspase 3, resulting in apoptosis.

Ketoconazole-induced JNK phosphorylation and subsequent cell death via apoptosis in human osteosarcoma cells

2009 ◽  
Vol 23 (7) ◽  
pp. 1268-1276 ◽  
Author(s):  
Ko-Long Lin ◽  
Chorng-Chih Huang ◽  
Jin-Shiung Cheng ◽  
Jeng-Yu Tsai ◽  
Yih-Chau Lu ◽  
...  
Keyword(s):  
Cell Death ◽  
Osteosarcoma Cells ◽  
Human Osteosarcoma ◽  
Human Osteosarcoma Cells

scholarly journals Decoding the anticancer activity of VO-clioquinol compound: the mechanism of action and cell death pathways in human osteosarcoma cells

Metallomics ◽  
2017 ◽  
Vol 9 (7) ◽  
pp. 891-901 ◽  
Author(s):  
Ignacio E. León ◽  
Paula Díez ◽  
Enrique J. Baran ◽  
Susana B. Etcheverry ◽  
Manuel Fuentes
Keyword(s):  
Cell Death ◽  
Anticancer Drugs ◽  
Mechanism Of Action ◽  
Platinum Metal ◽  
Osteosarcoma Cells ◽  
Vanadium Compounds ◽  
New Class ◽  
Human Osteosarcoma ◽  
Cell Death Pathways ◽  
Human Osteosarcoma Cells

Vanadium compounds were studied in recent years by considering them as a representative of a new class of non-platinum metal anticancer drugs.

scholarly journals The plant alkaloid voacamine induces apoptosis-independent autophagic cell death on both sensitive and multidrug resistant human osteosarcoma cells

Autophagy ◽  
2008 ◽  
Vol 4 (8) ◽  
pp. 1020-1033 ◽  
Author(s):  
Stefania Meschini ◽  
Maria Condello ◽  
Annarica Calcabrini ◽  
Manuela Marra ◽  
Giuseppe Formisano ◽  
...  
Keyword(s):  
Cell Death ◽  
Multidrug Resistant ◽  
Autophagic Cell Death ◽  
Osteosarcoma Cells ◽  
Human Osteosarcoma ◽  
Human Osteosarcoma Cells

Hyperthermia enhances the effect of β-lapachone to cause γH2AX formations and cell death in human osteosarcoma cells

2010 ◽  
Vol 27 (1) ◽  
pp. 53-62 ◽  
Author(s):  
Takeshi Hori ◽  
Takashi Kondo ◽  
Hyemi Lee ◽  
Chang W. Song ◽  
Heon Joo Park
Keyword(s):  
Cell Death ◽  
Osteosarcoma Cells ◽  
Human Osteosarcoma ◽  
Human Osteosarcoma Cells
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