Document Detail


Deficiency of Bid protein reduces sepsis-induced apoptosis and inflammation, while improving septic survival.
MedLine Citation:
PMID:  20023601     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Increased apoptotic cell death is believed to play a pathological role in patients with sepsis and experimental animals. Apoptosis can be induced by either a cell death receptor (extrinsic) or a mitochondrial (intrinsic) pathway. Bid, a proapoptotic member of the Bcl-2 family, is thought to mediate the cross talk between the extrinsic and intrinsic pathways of apoptosis; however, little is known about the action of Bid in the development of apoptosis and organ-specific tissue damage/cell death as seen in polymicrobial sepsis. Our results show that after the onset of sepsis, tBid (the active form of Bid) is significantly increased in mitochondrial fractions of the thymus, spleen, Peyer patches, and liver, and that Fas or FasL deficiency blocks Bid activation in various tissues after septic challenge. Increased Bid activation is correlated with increased active caspase-3, caspase-9, and apoptosis during sepsis. Bid-deficient mice exhibit significantly reduced apoptosis in the thymus, spleen, and Peyer patches compared with background mice after sepsis. Furthermore, Bid-deficient mice had significantly reduced systemic and local inflammatory cytokine levels and improved survival after sepsis. These data support not only the contribution of Bid to sepsis-induced apoptosis and the onset of septic morbidity/mortality, but also the existence of a bridge between extrinsic apoptotic signals, e.g., FasL:Fas, TNF:TNFR, and so on, and the intrinsic mitochondrial pathway via Bid-tBid activation during sepsis.
Authors:
Chun-Shiang Chung; Fabienne Venet; Yaping Chen; Leslie N Jones; Douglas C Wilson; Carol A Ayala; Alfred Ayala
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural    
Journal Detail:
Title:  Shock (Augusta, Ga.)     Volume:  34     ISSN:  1540-0514     ISO Abbreviation:  Shock     Publication Date:  2010 Aug 
Date Detail:
Created Date:  2010-07-22     Completed Date:  2010-11-10     Revised Date:  2011-08-03    
Medline Journal Info:
Nlm Unique ID:  9421564     Medline TA:  Shock     Country:  United States    
Other Details:
Languages:  eng     Pagination:  150-61     Citation Subset:  IM    
Affiliation:
Division of Surgical Research, Department of Surgery, Rhode Island Hospital, Providence, RI 02903, USA.
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MeSH Terms
Descriptor/Qualifier:
Alanine Transaminase / blood
Animals
Apoptosis / physiology*
BH3 Interacting Domain Death Agonist Protein / deficiency*,  physiology
Caspase 9 / metabolism
Cytokines / metabolism
Cytosol / metabolism
Fas Ligand Protein / physiology
Inflammation / immunology
Liver / immunology
Male
Mice
Mitochondria / metabolism
Protein Transport
Receptors, Tumor Necrosis Factor / physiology
Sepsis / immunology*,  mortality,  pathology
Signal Transduction / physiology
Spleen / immunology
Grant Support
ID/Acronym/Agency:
GM53209-10/GM/NIGMS NIH HHS; R01 GM053209-14/GM/NIGMS NIH HHS; R01 GM053209-16/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/BH3 Interacting Domain Death Agonist Protein; 0/Cytokines; 0/Fas Ligand Protein; 0/Receptors, Tumor Necrosis Factor; EC 2.6.1.2/Alanine Transaminase; EC 3.4.22.-/Caspase 9
Comments/Corrections

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