Source:http://linkedlifedata.com/resource/pubmed/id/10446348
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
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| pubmed:dateCreated |
1999-10-7
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| pubmed:abstractText |
Caspases and Bcl-xL, the mammalian homologues of the Caenorhabditis elegans (C. elegans) ced-3 and ced-9 genes, respectively, regulate apoptosis of various cells. Caspase-3 is processed into an active form (p20 or p17 and p12) during apoptosis. We investigated the relation between caspase-3 and Bcl-xL during development by examining activation of caspase-3 and apoptotic cells in Bcl-x-deficient (bcl-x(-/-)) mice at embryonic (E) day 11.5. We used a double-staining technique with a cleavage site-directed antibody against caspase-3 (anti-p20/17) and terminal-deoxytransferase-mediated deoxyuridine triphosphate nick-end labeling (TUNEL). Bcl-xL-deficiency increased both numbers of p20/17-positive and -negative apoptotic cells in dorsal root ganglia (DRG); the numbers of p20/17-positive apoptotic cells in the caudal parts of the ventral hindbrain and ventral spinal cord; and the numbers of p20/17-negative apoptotic cells in the dorsal midbrain, dorsal hindbrain, and dorsal spinal cord. Thus, Bcl-xL blocks the caspase-3-dependent apoptotic pathway in the restricted regions of the nervous system during development. Furthermore, these observations suggest that Bcl-xL protects against activation of the caspase-3-independent apoptotic pathway. Other caspases or apoptotic mechanisms may also be activated in the nervous systems of bcl-x(-/-) mice.
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| 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, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Casp3 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Caspase 3,
http://linkedlifedata.com/resource/pubmed/chemical/Caspases,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-bcl-2,
http://linkedlifedata.com/resource/pubmed/chemical/bcl-X Protein
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| pubmed:status |
MEDLINE
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| pubmed:month |
Aug
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| pubmed:issn |
0165-3806
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| pubmed:author | |
| pubmed:copyrightInfo |
Copyright 1999 Elsevier Science B.V.
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| pubmed:issnType |
Print
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| pubmed:day |
5
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| pubmed:volume |
116
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
69-78
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:10446348-Animals,
pubmed-meshheading:10446348-Apoptosis,
pubmed-meshheading:10446348-Caspase 3,
pubmed-meshheading:10446348-Caspases,
pubmed-meshheading:10446348-Cell Aging,
pubmed-meshheading:10446348-Embryonic and Fetal Development,
pubmed-meshheading:10446348-Enzyme Activation,
pubmed-meshheading:10446348-Female,
pubmed-meshheading:10446348-Ganglia, Spinal,
pubmed-meshheading:10446348-Gene Expression Regulation, Developmental,
pubmed-meshheading:10446348-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:10446348-In Situ Nick-End Labeling,
pubmed-meshheading:10446348-Male,
pubmed-meshheading:10446348-Mice,
pubmed-meshheading:10446348-Mice, Mutant Strains,
pubmed-meshheading:10446348-Neurons,
pubmed-meshheading:10446348-Proto-Oncogene Proteins c-bcl-2,
pubmed-meshheading:10446348-Rhombencephalon,
pubmed-meshheading:10446348-Spinal Cord,
pubmed-meshheading:10446348-bcl-X Protein
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| pubmed:year |
1999
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| pubmed:articleTitle |
Bcl-xL is a negative regulator of caspase-3 activation in immature neurons during development.
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| pubmed:affiliation |
Division of Development and Differentiation, National Institute of Neuroscience, NCNP, Kodaira, Tokyo 187-8502, Japan.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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