Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
1997-5-22
pubmed:abstractText
Programmed cell death or apoptosis provides an irreversible mechanism for the elimination of excess or damaged cells. Several recent studies have implicated the activation of the interleukin 1beta-converting enzyme/Ced-3 (ICE/Ced-3) family of proteases as the "point of no return" in apoptotic cell death, while others have suggested that loss of mitochondrial membrane potential (delta psi(m)) is the ultimate determinant of cell death. The temporal relationship of these two events during apoptosis and the role of Bcl-2 proteins in inhibiting these steps has not been defined. To examine these issues, control and Bcl-x(L)-transfected Jurkat T cells were treated with Fas antibodies in the presence and absence of the ICE protease inhibitor zVAD-FMK. ICE/Ced-3 protease activity was monitored by following the cleavage of poly(ADP-ribose) polymerase (PARP) and delta psi(m) was followed by rhodamine 123 fluorescence. Although Bcl-x(L) expression did not block Fas-induced protease activation, it substantially inhibited the subsequent loss of delta psi(m) and cell death in Fas-treated cells. In contrast, zVAD-FMK blocked PARP cleavage as well as loss of delta psi(m) and cell death. Together these data demonstrate that Bcl-x(L) can maintain cell viability by preventing the loss of mitochondrial membrane potential that occurs as a consequence of ICE/Ced-3 protease activation.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/9108051-7533326, http://linkedlifedata.com/resource/pubmed/commentcorrection/9108051-7536900, http://linkedlifedata.com/resource/pubmed/commentcorrection/9108051-7536901, http://linkedlifedata.com/resource/pubmed/commentcorrection/9108051-7629499, http://linkedlifedata.com/resource/pubmed/commentcorrection/9108051-7640294, http://linkedlifedata.com/resource/pubmed/commentcorrection/9108051-7655019, http://linkedlifedata.com/resource/pubmed/commentcorrection/9108051-7689176, http://linkedlifedata.com/resource/pubmed/commentcorrection/9108051-7698643, http://linkedlifedata.com/resource/pubmed/commentcorrection/9108051-7722446, http://linkedlifedata.com/resource/pubmed/commentcorrection/9108051-7759479, http://linkedlifedata.com/resource/pubmed/commentcorrection/9108051-7878463, http://linkedlifedata.com/resource/pubmed/commentcorrection/9108051-7954787, http://linkedlifedata.com/resource/pubmed/commentcorrection/9108051-8244956, http://linkedlifedata.com/resource/pubmed/commentcorrection/9108051-8402648, http://linkedlifedata.com/resource/pubmed/commentcorrection/9108051-8521815, http://linkedlifedata.com/resource/pubmed/commentcorrection/9108051-8564847, http://linkedlifedata.com/resource/pubmed/commentcorrection/9108051-8614469, http://linkedlifedata.com/resource/pubmed/commentcorrection/9108051-8642244, http://linkedlifedata.com/resource/pubmed/commentcorrection/9108051-8642303, http://linkedlifedata.com/resource/pubmed/commentcorrection/9108051-8642305, http://linkedlifedata.com/resource/pubmed/commentcorrection/9108051-8666886, http://linkedlifedata.com/resource/pubmed/commentcorrection/9108051-8681372, http://linkedlifedata.com/resource/pubmed/commentcorrection/9108051-8681376, http://linkedlifedata.com/resource/pubmed/commentcorrection/9108051-8681377, http://linkedlifedata.com/resource/pubmed/commentcorrection/9108051-8689682, http://linkedlifedata.com/resource/pubmed/commentcorrection/9108051-8692274, http://linkedlifedata.com/resource/pubmed/commentcorrection/9108051-8695785, http://linkedlifedata.com/resource/pubmed/commentcorrection/9108051-8752896, http://linkedlifedata.com/resource/pubmed/commentcorrection/9108051-8805273
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
94
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3759-64
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Bcl-x(L) can inhibit apoptosis in cells that have undergone Fas-induced protease activation.
pubmed:affiliation
Gwen Knapp Center for Lupus and Immunology Research, Department of Medicine, University of Chicago, IL 60637, USA.
pubmed:publicationType
Journal Article