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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1991-7-31
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pubmed:abstractText |
Differentiation of skeletal muscle involves withdrawal of myoblasts from cell replication, fusion to form multinucleated myotubes, coordinate appearance of a variety of muscle-specific proteins and the disappearance of a set of other proteins responsible for cell growth. The possible activation of the interferon (IFN) system in this process was studied. Thus, the activity of two IFN-induced enzymes known to be part of the system-(2'-5') oligoadenylate synthetase (2-5A synthetase) and double-stranded RNA-activated protein kinase as well as the expression of 2-5A synthetase coding genes were examined during myogenesis. It is demonstrated that the activity of the enzymes is transiently increased in cultured myoblasts, reaching a peak activity on the 3rd day in culture and then declining to a basal level. This peak activity precedes both cell fusion and the appearance of muscle-specific proteins--acetylcholine receptors (AChR) and creatine kinase. The same kinetics of 2-5A synthetase activity was evident in myoblasts from chick, rat or mouse origin. The enzymatic product appears to be primarily the trimer form of 2-5A, rather than a set of oligomers observed in enzymatic reactions performed on IFN-treated cells, including muscle cultures. The kinetics of 2-5A synthetase gene expression revealed that the largest amount of specific RNA transcripts appeared on the 1st day after seeding, followed by a reduction thereafter. In addition, a decrease was also observed in expression of c-myc, a cell-growth-associated protooncogene. However, an increase towards the 2nd day of both AChR and myosin light chain gene expression was evident, indicating selective regulation of gene expression during myogenesis.
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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/2',5'-Oligoadenylate Synthetase,
http://linkedlifedata.com/resource/pubmed/chemical/Interferons,
http://linkedlifedata.com/resource/pubmed/chemical/Myosins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-myc,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cholinergic
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0301-4681
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
45
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pubmed:geneSymbol |
c-myc
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
138-45
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:1711486-2',5'-Oligoadenylate Synthetase,
pubmed-meshheading:1711486-Animals,
pubmed-meshheading:1711486-Cells, Cultured,
pubmed-meshheading:1711486-Gene Expression,
pubmed-meshheading:1711486-Interferons,
pubmed-meshheading:1711486-Mice,
pubmed-meshheading:1711486-Muscles,
pubmed-meshheading:1711486-Myosins,
pubmed-meshheading:1711486-Proto-Oncogene Proteins c-myc,
pubmed-meshheading:1711486-Rats,
pubmed-meshheading:1711486-Receptors, Cholinergic,
pubmed-meshheading:1711486-Transcription, Genetic
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pubmed:year |
1990
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pubmed:articleTitle |
Activation of the interferon system during myogenesis in vitro.
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pubmed:affiliation |
Department of Life Sciences, Bar-Ilan University, Ramat-Gan, Israel.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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