Linked Life Data

7592801

Source:http://linkedlifedata.com/resource/pubmed/id/7592801

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
44
pubmed:dateCreated
1995-12-21
pubmed:abstractText
Bcl-2 and Bax are homologous proteins which can heterodimerize with each other. These proteins have opposing effects on cell survival when overexpressed in cells, with Bcl-2 blocking and Bax promoting apoptosis. Here we demonstrate that gene transfer-mediated elevations in Bcl-2 protein levels result in a marked increase in the steady-state levels of endogenous p21Bax protein as determined by immunoblotting in the Jurkat T-cell and 697 pre-B-cell leukemia cell lines, but not in several other cell lines including CEM T-cell leukemia, 32D.3 myeloid progenitor, PC12 pheochromocytoma, and NIH-3T3 fibroblasts. Steady-state levels of p21Bax protein were also elevated in the lymph nodes of Bcl-2 transgenic mice in which a BCL-2 transgene is expressed at high levels in B-cells. Northern blot analysis of BCL-2-transfected and control-transfected Jurkat and 697 leukemia cells revealed no Bcl-2-induced alterations in the steady-state levels of BAX mRNAs. In contrast, L-[35S]methionine pulse-chase analysis indicated a marked increase in the half-life (t1/2) of the p21Bax protein in BCL-2-transfected 697 cells compared to control-transfected cells (t1/2 > 24 h versus approximately 4 h), whereas the rate of Bax degradation was unaltered in Bcl-2-transfected CEM cells. The results demonstrate that levels of the proapoptotic p21Bax protein can be post-translationally regulated by Bcl-2, probably in a tissue-specific fashion, and suggest the existence of a feedback mechanism that may help to maintain the ratio of Bcl-2 to Bax protein in physiologically appropriate ranges.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
3
pubmed:volume
270
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
26049-52
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:7592801-3T3 Cells, pubmed-meshheading:7592801-Adrenal Gland Neoplasms, pubmed-meshheading:7592801-Animals, pubmed-meshheading:7592801-Base Sequence, pubmed-meshheading:7592801-Cell Line, pubmed-meshheading:7592801-DNA Primers, pubmed-meshheading:7592801-Feedback, pubmed-meshheading:7592801-Gene Expression, pubmed-meshheading:7592801-Hippocampus, pubmed-meshheading:7592801-Humans, pubmed-meshheading:7592801-Immunoblotting, pubmed-meshheading:7592801-Leukemia, T-Cell, pubmed-meshheading:7592801-Methionine, pubmed-meshheading:7592801-Mice, pubmed-meshheading:7592801-Molecular Sequence Data, pubmed-meshheading:7592801-PC12 Cells, pubmed-meshheading:7592801-Pheochromocytoma, pubmed-meshheading:7592801-Polymerase Chain Reaction, pubmed-meshheading:7592801-Protein-Tyrosine Kinases, pubmed-meshheading:7592801-Proto-Oncogene Proteins, pubmed-meshheading:7592801-Proto-Oncogene Proteins c-bcl-2, pubmed-meshheading:7592801-RNA, Messenger, pubmed-meshheading:7592801-Rats, pubmed-meshheading:7592801-Recombinant Proteins, pubmed-meshheading:7592801-Transfection, pubmed-meshheading:7592801-Tumor Cells, Cultured, pubmed-meshheading:7592801-bcl-2-Associated X Protein
pubmed:year
1995
pubmed:articleTitle
Overexpression of the Bcl-2 protein increases the half-life of p21Bax.
pubmed:affiliation
La Jolla Cancer Research Foundation, California 92037, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't