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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1989-10-25
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pubmed:abstractText |
A differentiation-defective mouse myoblast subclone (DD-1), cells of which do not fuse into myotubes nor synthesize muscle-specific proteins, was employed to help define the role of eicosanoids in mouse myoblast differentiation. We observed by hplc, tlc, and radioimmunoassay that the DD-1 cells release strikingly higher levels of cyclooxygenase pathway products prostaglandin E2 and F2 alpha into the culture medium than the parental non-differentiation-defective cells (DZ). In contrast, the levels of 15-hydroxyeicosatetraenoic acid (15-HETE), a lipoxygenase product, and a putatively identified second lipoxygenase product (LLP) did not differ greatly in the two cell types. The DD-1 cells also have strikingly higher levels of cyclooxygenase activity than the parental cells as determined by intact and broken cell assays. Additional fusion-defective clones were isolated on the basis of their flattened appearance and ability to grow in "mitogen-poor" medium and these cells also released strikingly higher levels of prostaglandins E2 and F2 alpha into the growth medium. The "turn on" of the cyclooxygenase pathway in the DD-1 cells and other fusion-defective cells is consistent with the hypothesis that the products of this pathway contribute to the inability of myoblasts to fuse with one another. This hypothesis is supported by the observation that there is a dose-dependent decrease in fusion of DZ cells when PGE2 is added to commitment medium.
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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/15-hydroxy-5,8,11,13-eicosatetraenoi...,
http://linkedlifedata.com/resource/pubmed/chemical/Dinoprost,
http://linkedlifedata.com/resource/pubmed/chemical/Dinoprostone,
http://linkedlifedata.com/resource/pubmed/chemical/Hydroxyeicosatetraenoic Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoxygenase,
http://linkedlifedata.com/resource/pubmed/chemical/Prostaglandin-Endoperoxide Synthases,
http://linkedlifedata.com/resource/pubmed/chemical/Prostaglandins
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0021-9541
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
141
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
142-7
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:2506193-Animals,
pubmed-meshheading:2506193-Cell Differentiation,
pubmed-meshheading:2506193-Cell Fusion,
pubmed-meshheading:2506193-Chromatography, Thin Layer,
pubmed-meshheading:2506193-Clone Cells,
pubmed-meshheading:2506193-Dinoprost,
pubmed-meshheading:2506193-Dinoprostone,
pubmed-meshheading:2506193-Hydroxyeicosatetraenoic Acids,
pubmed-meshheading:2506193-Lipoxygenase,
pubmed-meshheading:2506193-Mice,
pubmed-meshheading:2506193-Muscles,
pubmed-meshheading:2506193-Mutation,
pubmed-meshheading:2506193-Prostaglandin-Endoperoxide Synthases,
pubmed-meshheading:2506193-Prostaglandins
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pubmed:year |
1989
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pubmed:articleTitle |
Possible role of prostaglandins in the regulation of mouse myoblasts.
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pubmed:affiliation |
Biological Sciences, University of Kentucky, Lexington 40506.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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