Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
10
|
| pubmed:dateCreated |
1994-12-7
|
| pubmed:databankReference | |
| pubmed:abstractText |
We report the cloning and initial characterization of the mouse homologues of the bcl-2-related gene, bcl-x. We compare these to the two major isoforms of human bcl-x that were previously identified, bcl-xLong (bcl-xL) which has death repressor activity similar to bcl-2, and bcl-xShort (bcl-xS), an alternative mRNA splice product that deletes a highly conserved domain shared by bcl-2 family members and promotes cell death in transfection studies. In addition to murine (m) bcl-xL and mbcl-xS, we have cloned a novel cDNA isoform that we designate mbcl-x delta TM. This cDNA deletes, by means of alternative splicing, the carboxy terminal transmembrane domain of bcl-x and is predicted to be a soluble, rather than membrane-bound, protein. We found that mbcl-x mRNA is highly inducible in splenocytes stimulated with either anti-CD3 Abs or LPS/dextran sulfate, and that the major species of mbcl-x mRNA in a variety of cell lines and tissues was the xL isoform. Transfection of mbcl-xL or mbcl-xS into Hela cells resulted in targeting primarily to mitochondria, whereas mbcl-x delta TM localized diffusely throughout the cytosol. Overexpression of the novel delta TM isoform in an IL-3-dependent cell line delayed the onset of apoptosis induced by growth factor withdrawal. Thus, a naturally-occurring form of mbcl-x present in lymphocytes that does not localize to the mitochondrial membrane is functional in preventing apoptotic cell death. Moreover, these data suggest that bcl-x provides a life signal in activated lymphocytes.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
AIM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/BCL2L1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Bcl2l1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-bcl-2,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/bcl-X Protein
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Nov
|
| pubmed:issn |
0022-1767
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
15
|
| pubmed:volume |
153
|
| pubmed:geneSymbol |
bcl-x
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
4388-98
|
| pubmed:dateRevised |
2007-11-14
|
| pubmed:meshHeading |
pubmed-meshheading:7963517-Amino Acid Sequence,
pubmed-meshheading:7963517-Animals,
pubmed-meshheading:7963517-Apoptosis,
pubmed-meshheading:7963517-Base Sequence,
pubmed-meshheading:7963517-Blotting, Northern,
pubmed-meshheading:7963517-Cloning, Molecular,
pubmed-meshheading:7963517-HeLa Cells,
pubmed-meshheading:7963517-Humans,
pubmed-meshheading:7963517-Mice,
pubmed-meshheading:7963517-Microscopy, Confocal,
pubmed-meshheading:7963517-Mitochondria,
pubmed-meshheading:7963517-Molecular Sequence Data,
pubmed-meshheading:7963517-Polymerase Chain Reaction,
pubmed-meshheading:7963517-Protein Biosynthesis,
pubmed-meshheading:7963517-Proto-Oncogene Proteins,
pubmed-meshheading:7963517-Proto-Oncogene Proteins c-bcl-2,
pubmed-meshheading:7963517-RNA, Messenger,
pubmed-meshheading:7963517-Sequence Homology, Amino Acid,
pubmed-meshheading:7963517-Spleen,
pubmed-meshheading:7963517-Transfection,
pubmed-meshheading:7963517-bcl-X Protein
|
| pubmed:year |
1994
|
| pubmed:articleTitle |
Cloning and molecular characterization of mouse bcl-x in B and T lymphocytes.
|
| pubmed:affiliation |
Department of Medicine/Rheumatology, University of Minnesota, Minneapolis 55455.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|