Document Detail


Cellular inhibitor of apoptosis 1 (cIAP-1) degradation by caspase 8 during TNF-related apoptosis-inducing ligand (TRAIL)-induced apoptosis.
MedLine Citation:
PMID:  20951133     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
TNF-related apoptosis-inducing ligand (TRAIL) is a potential chemotherapeutic agent with high selectivity for malignant cells. Many tumors, however, are resistant to TRAIL cytotoxicity. Although cellular inhibitors of apoptosis 1 and 2 (cIAP-1 and -2) are often over-expressed in cancers, their role in mediating TRAIL resistance remains unclear. Here, we demonstrate that TRAIL-induced apoptosis of liver cancer cells is associated with degradation of cIAP-1 and X-linked IAP (XIAP), whereas cIAP-2 remains unchanged. Lower concentrations of TRAIL causing minimal or no apoptosis do not alter cIAP-1 or XIAP protein levels. Silencing of cIAP-1 expression, but not XIAP or cIAP-2, as well as co-treatment with a second mitochondrial activator of caspases (SMAC) mimetic (which results in rapid depletion of cIAP-1), sensitizes the cells to TRAIL. TRAIL-induced loss of cIAP-1 and XIAP requires caspase activity. In particular, caspase 8 knockdown stabilizes both cIAP-1 and XIAP, while caspase 9 knockdown prevents XIAP, but not cIAP-1 degradation. Cell-free experiments confirmed cIAP-1 is a substrate for caspase 8, with likely multiple cleavage sites. These results suggest that TRAIL-mediated apoptosis proceeds through caspase 8-dependent degradation of cIAP-1. Targeted depletion of cIAP-1 by SMAC mimetics in conjunction with TRAIL may be beneficial for the treatment of human hepatobiliary malignancies.
Authors:
Maria Eugenia Guicciardi; Justin L Mott; Steven F Bronk; Satoshi Kurita; Christian D Fingas; Gregory J Gores
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2010-10-14
Journal Detail:
Title:  Experimental cell research     Volume:  317     ISSN:  1090-2422     ISO Abbreviation:  Exp. Cell Res.     Publication Date:  2011 Jan 
Date Detail:
Created Date:  2010-11-24     Completed Date:  2010-12-14     Revised Date:  2012-01-04    
Medline Journal Info:
Nlm Unique ID:  0373226     Medline TA:  Exp Cell Res     Country:  United States    
Other Details:
Languages:  eng     Pagination:  107-16     Citation Subset:  IM    
Copyright Information:
Copyright © 2010 Elsevier Inc. All rights reserved.
Affiliation:
Division of Gastroenterology and Hepatology, College of Medicine, Mayo Clinic, 200 First Street SW, Rochester, MN, 55905, USA.
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MeSH Terms
Descriptor/Qualifier:
Apoptosis / drug effects*,  genetics,  physiology
Caspase 8 / antagonists & inhibitors,  genetics,  metabolism*,  physiology
Caspase 9 / antagonists & inhibitors,  genetics,  metabolism
Gene Knockdown Techniques
Humans
Inhibitor of Apoptosis Proteins / antagonists & inhibitors,  genetics,  metabolism*
Protein Processing, Post-Translational / drug effects
RNA, Small Interfering / pharmacology
Signal Transduction / drug effects,  genetics
TNF-Related Apoptosis-Inducing Ligand / pharmacology*
Tumor Cells, Cultured
X-Linked Inhibitor of Apoptosis Protein / antagonists & inhibitors,  genetics
Grant Support
ID/Acronym/Agency:
K01 DK079875-05/DK/NIDDK NIH HHS; P30 DK84567/DK/NIDDK NIH HHS; R01 DK063947-09/DK/NIDDK NIH HHS; R01DK63947/DK/NIDDK NIH HHS
Chemical
Reg. No./Substance:
0/BIRC3 protein, human; 0/Inhibitor of Apoptosis Proteins; 0/RNA, Small Interfering; 0/TNF-Related Apoptosis-Inducing Ligand; 0/TNFSF10 protein, human; 0/X-Linked Inhibitor of Apoptosis Protein; 0/XIAP protein, human; EC 3.4.22.-/CASP8 protein, human; EC 3.4.22.-/Caspase 8; EC 3.4.22.-/Caspase 9

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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