Linked Life Data

6189526

Source:http://linkedlifedata.com/resource/pubmed/id/6189526

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1983-7-15
pubmed:abstractText
The effects of competitive inhibitors of transglutaminase on the formation of myotubes by the fusion of myoblasts in vitro has been investigated. Myotube formation was inhibited when myoblasts from 11-day-old chick embryos were cultured in vitro in the presence of 10 mM histamine or 0.2 mM dansyl cadaverine. The inhibitions observed were reversed when the treated cells were subsequently cultured in normal medium. Glycine methyl ester also inhibited myotube formation but sarcosine methyl ester, which is not a competitive inhibitor of transglutaminase, had little if any inhibitory action. The formation of myotubes was not inhibited by cultivation in normal medium adjusted to pH 8.0-8.1, indicating that the observed effects of histamine and of dansyl cadaverine were not mediated by a lysosomotropic effect. Inhibition of myotube formation in the presence of histamine was accompanied by the production of abnormal multinucleated cells, indicating that myoblast fusion occurred in the treated cultures but that the fused cells failed to elongate into normal myotubes. Transglutaminase activity has been found in cell-free lysates of embryonic chick myoblasts and it is concluded that a transglutaminase enzyme, activated by an increase in the concentration of intracellular Ca2+, plays an important role in stabilising the cytoskeletal network of developing myotubes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
2
pubmed:volume
762
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
429-36
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
Inhibition of the formation of myotubes in vitro by inhibitors of transglutaminase.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't