Document Detail


Apoptosis in hematopoietic cells (FL5.12) caused by interleukin-3 withdrawal: relationship to caspase activity and the loss of glutathione.
MedLine Citation:
PMID:  10200549     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The mechanism of cell death caused by cytokine deprivation remains largely unknown. FL5.12 cells (a murine prolymphocytic cell line), following interleukin-3 (IL-3) withdrawal, undergo a decrease in intracellular glutathione (GSH) that precedes the onset of apoptosis. In the present study, the induction of apoptosis following IL-3 withdrawal or GSH depletion with DL-buthionine-[S,R,]-sulfoximine (BSO) was examined. Both conditions caused time-dependent increases in phosphatidylserine externalization, acridine orange and ethidium bromide staining, decreases in mitochondrial membrane potential, processing and activation of caspase-3 and proteolysis of the endogenous caspase substrate poly(adenosine diphosphate ribose)polymerase (PARP). Apoptosis induced by IL-3 deprivation but not BSO also caused lamin B1 cleavage, suggesting activation of caspase-6. Despite a more profound depletion of GSH after BSO than withdrawal of IL-3, the extent of apoptosis was somewhat lower. Benzyloxycarbonyl-Val-Ala-Asp(OMe)fluoromethyl ketone (z-VAD.fmk) blocked this caspase activity and prevented cell death after BSO exposure but not after IL-3 deprivation. Following IL-3 withdrawal, the caspase inhibitors z-VAD.fmk and boc-asp(OMe)fluoromethylketone (boc-asp.fmk) prevented the cleavage and activation of caspase-3, the breakdown of lamin B1 and partially mitigated PARP degradation. However, the externalization of phosphatidylserine, the fall in mitochondrial membrane potential and subsequent apoptotic cell death still occurred. These results suggest that IL-3 withdrawal may mediate cell death by a mechanism independent of both caspase activation and the accompanying loss of GSH.
Authors:
H K Bojes; X Feng; J P Kehrer; G M Cohen
Related Documents :
19561399 - Alpha-tocopheryl succinate potentiates the paclitaxel-induced apoptosis through enforce...
14676829 - Essential role of caspases in epigallocatechin-3-gallate-mediated inhibition of nuclear...
17114439 - Cyclosporin a abolishes cd28-mediated resistance to cd95-induced apoptosis via superind...
8637709 - Bcl-2 and adenovirus e1b 19 kda protein prevent e1a-induced processing of cpp32 and cle...
19619589 - Analysis of apoptosis induced by caprine herpesvirus 1 in vitro.
18678619 - Nonsteroidal anti-inflammatory drugs induced endothelial apoptosis by perturbing peroxi...
20129149 - Host immunity as a determinant of treatment outcome in plasmodium falciparum malaria.
21844239 - Neisseria gonorrhoeae-mediated inhibition of apoptotic signalling in polymorphonuclear ...
12706809 - Mitochondria in apoptosis of ischemic heart.
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Cell death and differentiation     Volume:  6     ISSN:  1350-9047     ISO Abbreviation:  Cell Death Differ.     Publication Date:  1999 Jan 
Date Detail:
Created Date:  1999-04-29     Completed Date:  1999-04-29     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  9437445     Medline TA:  Cell Death Differ     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  61-70     Citation Subset:  IM    
Affiliation:
Division of Pharmacology and Toxicology, College of Pharmacy, The University of Texas at Austin, Texas, USA.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Amino Acid Chloromethyl Ketones / pharmacology
Animals
Apoptosis*
Buthionine Sulfoximine / pharmacology
Caspase 3
Caspases / metabolism*
Cell Line
Coumarins / metabolism
Glutathione / metabolism*
Glutathione Disulfide / metabolism
Hematopoietic Stem Cells
Interleukin-3 / metabolism*
Lamin Type B*
Lamins
Membrane Potentials / drug effects
Mice
Mitochondria / drug effects
Nuclear Proteins / metabolism
Oligopeptides / metabolism
Phosphatidylserines / metabolism
Poly(ADP-ribose) Polymerases
Protease Inhibitors / pharmacology
Proteins / metabolism
Grant Support
ID/Acronym/Agency:
ES 07247/ES/NIEHS NIH HHS; ES 07784/ES/NIEHS NIH HHS; HL 51005/HL/NHLBI NIH HHS
Chemical
Reg. No./Substance:
0/Amino Acid Chloromethyl Ketones; 0/Coumarins; 0/Interleukin-3; 0/Lamin Type B; 0/Lamins; 0/Nuclear Proteins; 0/Oligopeptides; 0/Phosphatidylserines; 0/Protease Inhibitors; 0/Proteins; 0/acetyl-aspartyl-glutamyl-valyl-aspartyl-amino-4-methylcoumarin; 0/benzyloxycarbonylvalyl-alanyl-aspartyl fluoromethyl ketone; 0/butyloxycarbonyl-O-methyl-aspartyl-fluoromethyl ketone; 0/lamin B1; 27025-41-8/Glutathione Disulfide; 5072-26-4/Buthionine Sulfoximine; 70-18-8/Glutathione; EC 2.4.2.30/Parp1 protein, mouse; EC 2.4.2.30/Poly(ADP-ribose) Polymerases; EC 3.4.22.-/Casp3 protein, mouse; EC 3.4.22.-/Caspase 3; EC 3.4.22.-/Caspases

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


Previous Document:  Alterations in cell death and cell cycle progression in the UV-irradiated epidermis of bcl-2-deficie...
Next Document:  The role of macrophage cell death in tuberculosis.