Source:http://linkedlifedata.com/resource/pubmed/id/18403482
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
7
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pubmed:dateCreated |
2008-6-30
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pubmed:abstractText |
Amphibian metamorphosis induced by T(3) involves programmed cell death and the differentiation of various types of cells in degenerated and reconstructed tissues. However, the signaling pathway that directs the T(3)-dependent cell-fate determinations remains unclear. TNF-alpha is a pleiotropic cytokine that affects diverse cellular responses. Engagement of TNF-alpha with its receptor (TNFR1) causes intracellular apoptotic and/or survival signaling. To investigate TNF signaling functions during anuran metamorphosis, we first identified Xenopus laevis orthologs of TNF (xTNF)-alpha and its receptor. We found that xTNF-alpha activated nuclear factor-kappaB in X. laevis A6 cells through the Fas-associated death domain and receptor-interacting protein 1. Interestingly, xTNF-alpha mRNA in blood cells showed prominent expression at prometamorphosis during metamorphosis. Next, to elucidate the apoptotic and/or survival signaling induced by xTNF-alpha in an in vitro model of metamorphosis, we established a vascular endothelial cell line, XLgoo, from X. laevis tadpole tail. XLgoo cells formed actin stress fibers and elongated in response to xTNF-alpha. T(3) induced apoptosis in these cells, but the addition of xTNF-alpha blocked the T(3)-induced apoptosis. In addition, treatment of the cells with T(3) for 2 d induced the expression of thyroid hormone receptor-beta and caspase-3, and this thyroid hormone receptor-beta induction was drastically repressed by xTNF-alpha. Furthermore, in organ culture of the tail, xTNF-alpha significantly attenuated the tail degeneration induced by T(3). These findings suggested that xTNF-alpha could protect vascular endothelial cells from apoptotic cell death induced by T(3) during metamorphosis and thereby participate in the regulation of cell fate.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Fas-Associated Death Domain Protein,
http://linkedlifedata.com/resource/pubmed/chemical/NF-kappa B,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Tumor Necrosis Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Thyroid Hormones,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Necrosis Factor-alpha
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0013-7227
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
149
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3379-89
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pubmed:meshHeading |
pubmed-meshheading:18403482-Amino Acid Sequence,
pubmed-meshheading:18403482-Animals,
pubmed-meshheading:18403482-Apoptosis,
pubmed-meshheading:18403482-Cell Line,
pubmed-meshheading:18403482-Cells, Cultured,
pubmed-meshheading:18403482-Endothelial Cells,
pubmed-meshheading:18403482-Fas-Associated Death Domain Protein,
pubmed-meshheading:18403482-Humans,
pubmed-meshheading:18403482-Larva,
pubmed-meshheading:18403482-Molecular Sequence Data,
pubmed-meshheading:18403482-NF-kappa B,
pubmed-meshheading:18403482-Protein Binding,
pubmed-meshheading:18403482-Receptors, Tumor Necrosis Factor,
pubmed-meshheading:18403482-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:18403482-Sequence Homology, Amino Acid,
pubmed-meshheading:18403482-Tail,
pubmed-meshheading:18403482-Thyroid Hormones,
pubmed-meshheading:18403482-Tumor Necrosis Factor-alpha,
pubmed-meshheading:18403482-Xenopus laevis
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pubmed:year |
2008
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pubmed:articleTitle |
Tumor necrosis factor-alpha attenuates thyroid hormone-induced apoptosis in vascular endothelial cell line XLgoo established from Xenopus tadpole tails.
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pubmed:affiliation |
Department of Biosciences, School of Science, Kitasato University, 1-15-1 Kitasato, Sagamihara, Japan.
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pubmed:publicationType |
Journal Article
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