Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
1984-6-14
pubmed:abstractText
We previously reported that the cell fusion that occurs during muscle development, when mononucleated myoblasts fuse to form multinucleated myotubes, requires endogenous metalloendoprotease activity at the time of fusion. We report here that myoblasts contain both soluble and membrane-associated metalloendoproteases, and that these proteases have different inhibitor specificities. Several inhibitors, previously shown to block myoblast fusion, inhibit only soluble and not membrane-associated metalloendoprotease activity in myoblasts. Another metalloendoprotease inhibitor, phosphoramidon, which had no effect on fusion, inhibits only the membrane-associated metalloendoprotease. These observations implicate a soluble metalloendoprotease in myoblast fusion. Two soluble metalloendoproteases can be demonstrated by column chromatofocusing, with pI values at pH 5.9 and 4.8. The soluble metalloendoprotease eluted at pH 5.9 is not inhibited by an inhibitor which blocks fusion, while the soluble metalloendoprotease eluted at pH 4.8 is inhibited. Of the three metalloendoprotease activities identified in myoblasts, the metalloendoprotease required in myoblast fusion appears to be the soluble metalloendoprotease with a pI of 4.8.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
259
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5396-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Specific blockers of myoblast fusion inhibit a soluble and not the membrane-associated metalloendoprotease in myoblasts.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't