Source:http://linkedlifedata.com/resource/pubmed/id/10395645
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1999-7-29
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pubmed:abstractText |
NF-kappa B is involved in the transcriptional control of various genes that act as extrinsic and intrinsic survival factors for T cells. Our findings show that suppression of NF-kappa B activity with cell-permeable SN50 peptide, which masks the nuclear localization sequence of NF-kappa B1 dimers and prevents their nuclear localization, induces apoptosis in resting normal human PBL. Inhibition of NF-kappa B resulted in the externalization of phosphatidylserine, induction of DNA breaks, and morphological changes consistent with apoptosis. DNA fragmentation was efficiently blocked by the caspase inhibitor Z-VAD-fmk and partially blocked by Ac-DEVD-fmk, suggesting that SN50-mediated apoptosis is caspase-dependent. Interestingly, apoptosis induced by NF-kappa B suppression, in contrast to that induced by TPEN (N,N,N',N'-tetrakis [2-pyridylmethyl]ethylenediamine) or soluble Fas ligand (CD95), was observed in the absence of active death effector proteases caspase-1-like (IL-1 converting enzyme), caspase-3-like (CPP32/Yama/apopain), and caspase-6-like and without cleavage of caspase-3 substrates poly(ADP-ribose) polymerase and DNA fragmentation factor-45. These findings suggest either low level of activation is required or that different caspases are involved. Preactivation of T cells resulting in NF-kappa B nuclear translocation protected cells from SN50-induced apoptosis. Our findings demonstrate an essential role of NF-kappa B in survival of naive PBL.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/CASP3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/CASP6 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Caspase 1,
http://linkedlifedata.com/resource/pubmed/chemical/Caspase 3,
http://linkedlifedata.com/resource/pubmed/chemical/Caspase 6,
http://linkedlifedata.com/resource/pubmed/chemical/Caspases,
http://linkedlifedata.com/resource/pubmed/chemical/Immunosuppressive Agents,
http://linkedlifedata.com/resource/pubmed/chemical/NF-kappa B,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylserines,
http://linkedlifedata.com/resource/pubmed/chemical/SN50 peptide
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0022-1767
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
163
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
590-8
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:10395645-Apoptosis,
pubmed-meshheading:10395645-Caspase 1,
pubmed-meshheading:10395645-Caspase 3,
pubmed-meshheading:10395645-Caspase 6,
pubmed-meshheading:10395645-Caspases,
pubmed-meshheading:10395645-Cell Survival,
pubmed-meshheading:10395645-Enzyme Activation,
pubmed-meshheading:10395645-Humans,
pubmed-meshheading:10395645-Immunosuppressive Agents,
pubmed-meshheading:10395645-Interphase,
pubmed-meshheading:10395645-Lymphocyte Activation,
pubmed-meshheading:10395645-NF-kappa B,
pubmed-meshheading:10395645-Peptides,
pubmed-meshheading:10395645-Phosphatidylserines,
pubmed-meshheading:10395645-Protein Binding,
pubmed-meshheading:10395645-T-Lymphocytes
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pubmed:year |
1999
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pubmed:articleTitle |
Inhibition of NF-kappa B activity in human T lymphocytes induces caspase-dependent apoptosis without detectable activation of caspase-1 and -3.
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pubmed:affiliation |
Department of Immunology, Cleveland Clinic Foundation, OH 44195, USA. kolenkv@ces.mtp.ccf.org
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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