Source:http://linkedlifedata.com/resource/pubmed/id/16888644
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
|
| pubmed:dateCreated |
2007-2-15
|
| pubmed:abstractText |
The HIV-1 encoded apoptogenic protein Vpr induces mitochondrial membrane permeabilization (MMP) via interactions with the voltage-dependent anion channel (VDAC) and the adenine nucleotide translocator (ANT). We have designed a peptide, TEAM-VP, composed of two functional domains, one a tumor blood vessel RGD-like 'homing' motif and the other an MMP-inducing sequence derived from Vpr. When added to isolated mitochondria, TEAM-VP interacts with ANT and VDAC, reduces oxygen consumption and overcomes Bcl-2 protection to cause inner and outer MMP. TEAM-VP specifically recognizes cell-surface expressed alpha(V)beta(3) integrins, internalizes, temporarily localizes to lysosomes and progressively co-distributes with the mitochondrial compartment with no sign of lysosomal membrane permeabilization. Finally TEAM-VP reaches mitochondria of angiogenic endothelial cells to induce mitochondrial fission, dissipation of the mitochondrial transmembrane potential (DeltaPsi(m)), cytochrome c release and apoptosis hallmarks. Hence, this chimeric peptide constitutes the first example of a virus-derived mitochondriotoxic compound as a candidate to kill selectively tumor neo-endothelia.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Mar
|
| pubmed:issn |
1350-9047
|
| pubmed:author |
pubmed-author:BavaDD,
pubmed-author:Borgne-SanchezAA,
pubmed-author:BrabantMM,
pubmed-author:BrennerCC,
pubmed-author:BrièreJ-JJJ,
pubmed-author:BriandJ-PJP,
pubmed-author:ChauvierDD,
pubmed-author:DéasOO,
pubmed-author:DeniaudAA,
pubmed-author:DupontSS,
pubmed-author:EdelmanLL,
pubmed-author:HoebekeJJ,
pubmed-author:JacototEE,
pubmed-author:LangonnéAA,
pubmed-author:LassalleMM,
pubmed-author:LecoeurHH,
pubmed-author:PéchouxCC,
pubmed-author:RebouillatDD,
pubmed-author:RouxPP,
pubmed-author:RustinPP
|
| pubmed:issnType |
Print
|
| pubmed:volume |
14
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
422-35
|
| pubmed:meshHeading |
pubmed-meshheading:16888644-Amino Acid Sequence,
pubmed-meshheading:16888644-Animals,
pubmed-meshheading:16888644-Apoptosis,
pubmed-meshheading:16888644-Cell Survival,
pubmed-meshheading:16888644-Dose-Response Relationship, Drug,
pubmed-meshheading:16888644-Endothelial Cells,
pubmed-meshheading:16888644-Gene Products, vpr,
pubmed-meshheading:16888644-Humans,
pubmed-meshheading:16888644-Integrin alphaVbeta3,
pubmed-meshheading:16888644-Lysosomes,
pubmed-meshheading:16888644-Mice,
pubmed-meshheading:16888644-Mice, Inbred BALB C,
pubmed-meshheading:16888644-Mitochondria,
pubmed-meshheading:16888644-Mitochondrial Membranes,
pubmed-meshheading:16888644-Molecular Sequence Data,
pubmed-meshheading:16888644-Peptides,
pubmed-meshheading:16888644-Permeability
|
| pubmed:year |
2007
|
| pubmed:articleTitle |
Targeted Vpr-derived peptides reach mitochondria to induce apoptosis of alphaVbeta3-expressing endothelial cells.
|
| pubmed:affiliation |
Theraptosis Research Laboratory, THERAPTOSIS S.A., 28 rue du Dr. Roux, Paris cedex 15, France.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Evaluation Studies
|