Source:http://linkedlifedata.com/resource/pubmed/id/15870695
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
30
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pubmed:dateCreated |
2005-7-14
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pubmed:abstractText |
Bcl-xL plays a critical role in maintaining cell survival. However, the relationship between the potential interaction of Bcl-xL with other cytosolic proteins and the regulation of cell survival remains incompletely defined. We have identified translationally controlled tumor protein (TCTP), a multifunctional protein, as a novel antiapoptotic Bcl-xL-interacting protein. TCTP interacted in vivo and in vitro with Bcl-xL, and their sites have been mapped to an N-terminal region of TCTP and the Bcl-2 homology domain 3 of Bcl-xL. Consistent with a role in maintaining T-cell survival during activation, TCTP was significantly upregulated in murine T cells activated by T-cell antigen receptor (TCR) ligation and CD28 costimulation, which was correlated with the upregulation of Bcl-xL in activated T cells. Moreover, downregulation of TCTP expression by antisense technology in T cells results in the increase of T-cell apoptosis. Furthermore, the N-terminal region of TCTP was required for its ability to inhibit apoptosis. In conclusion, this study has demonstrated that an N-terminal region of a cytosolic protein, TCTP, is required for its binding to Bcl-xL and for its antiapoptotic activity.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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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/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-bcl-2,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Markers, Biological,
http://linkedlifedata.com/resource/pubmed/chemical/bcl-X Protein,
http://linkedlifedata.com/resource/pubmed/chemical/translationally controlled tumor...
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0950-9232
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
14
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pubmed:volume |
24
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4778-88
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:15870695-Amino Acid Sequence,
pubmed-meshheading:15870695-Animals,
pubmed-meshheading:15870695-Apoptosis,
pubmed-meshheading:15870695-Binding Sites,
pubmed-meshheading:15870695-Humans,
pubmed-meshheading:15870695-Lymphocyte Activation,
pubmed-meshheading:15870695-Mice,
pubmed-meshheading:15870695-Protein Binding,
pubmed-meshheading:15870695-Protein Biosynthesis,
pubmed-meshheading:15870695-Protein Structure, Tertiary,
pubmed-meshheading:15870695-Proteins,
pubmed-meshheading:15870695-Proto-Oncogene Proteins c-bcl-2,
pubmed-meshheading:15870695-Sequence Alignment,
pubmed-meshheading:15870695-T-Lymphocytes,
pubmed-meshheading:15870695-Tumor Markers, Biological,
pubmed-meshheading:15870695-Up-Regulation,
pubmed-meshheading:15870695-bcl-X Protein
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pubmed:year |
2005
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pubmed:articleTitle |
An N-terminal region of translationally controlled tumor protein is required for its antiapoptotic activity.
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pubmed:affiliation |
Department of Medicine, Laboratory of Immunopathology, Biology of Inflammation Center, Baylor College of Medicine, Houston, TX 77030, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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