Linked Life Data

16824191

Source:http://linkedlifedata.com/resource/pubmed/id/16824191

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
2006-7-7
pubmed:abstractText
Two major apoptotic signaling pathways have been defined in mammals, the extrinsic pathway, initiated by ligation of death receptors, and the intrinsic pathway, triggered by cytochrome c release from mitochondria. Here, we identified and characterized the Xenopus homologs of caspase-10 (xCaspase-10beta), a novel initiator caspase, and Bid (xBid), a BH3-only molecule of the Bcl-2 family involved in both the extrinsic and intrinsic pathways. Exogenous expression of these molecules induced apoptosis of mammalian cells. By biochemical and cytological analyses, we clarified that xCaspase-10beta and xBid exhibit structural and functional similarities to their mammalian orthologues. We also detected xCaspase-10beta and xBid transcripts during embryogenesis by whole-mount in situ hybridization and RT-PCR analysis. Microinjection of mRNA encoding a protease-defect xCaspase-10beta mutant into embryos resulted in irregular development. Enforced expression of active xBid induced cell death in developing embryos. Using transgenic frogs established to allow monitoring of caspase activation in vivo, we confirmed that this form of cell death is caspase-dependent apoptosis. Thus, we demonstrated that the machinery governing the extrinsic and intrinsic apoptotic pathways are already established in Xenopus embryos. Additionally, we propose that the functions of the initiator caspase and BH3-only molecule are evolutionarily conserved in vertebrates, functioning during embryonic development.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
1356-9597
pubmed:author
pubmed:issnType
Print
pubmed:volume
11
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
701-17
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:16824191-Amino Acid Sequence, pubmed-meshheading:16824191-Animals, pubmed-meshheading:16824191-Apoptosis Regulatory Proteins, pubmed-meshheading:16824191-BH3 Interacting Domain Death Agonist Protein, pubmed-meshheading:16824191-Caspase 10, pubmed-meshheading:16824191-Caspases, pubmed-meshheading:16824191-Chickens, pubmed-meshheading:16824191-Evolution, Molecular, pubmed-meshheading:16824191-Green Fluorescent Proteins, pubmed-meshheading:16824191-HeLa Cells, pubmed-meshheading:16824191-Humans, pubmed-meshheading:16824191-Mice, pubmed-meshheading:16824191-Mitochondria, pubmed-meshheading:16824191-Molecular Sequence Data, pubmed-meshheading:16824191-Peptide Hydrolases, pubmed-meshheading:16824191-RNA, Messenger, pubmed-meshheading:16824191-Sequence Alignment, pubmed-meshheading:16824191-Transfection, pubmed-meshheading:16824191-Xenopus
pubmed:year
2006
pubmed:articleTitle
The initiator caspase, caspase-10beta, and the BH-3-only molecule, Bid, demonstrate evolutionary conservation in Xenopus of their pro-apoptotic activities in the extrinsic and intrinsic pathways.
pubmed:affiliation
Department of Animal Development and Physiology, Graduate School of Biostudies, Kyoto University, Kyoto 606-8501, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't