Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1991-1-22
pubmed:abstractText
Brevin is a protein which regulates the actin gel-sol transformation: it severs F-actin filaments into shorter ones. This action is Ca-dependent and is prevented by tropomyosin. We tested the effect of brevin on isometric contractions of skinned smooth muscle (taenia coli) and noted a dramatic loss of tension that possibly reflects some F-actin fragmentation. This effect is tentatively attributed to a partial loss of tropomyosin in the skinning procedure. We also studied the effect of brevin on unloaded shortenings of skinned preparations: thin bundles and enzymatically dissociated cells. We observed a marked increase of the velocity of shortening in the presence of brevin. This effect cannot be attributed to an increased ATPase activity as the latter is slightly reduced in the presence of brevin. We interpret this result as reflecting a decrease in internal resistance to movement, possibly by solation of an actin-filamin domain.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0142-4319
pubmed:author
pubmed:issnType
Print
pubmed:volume
11
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
293-301
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
The action of brevin, an F-actin severing protein, on the mechanical properties and ATPase activity of skinned smooth muscle.
pubmed:affiliation
Département de Physiologie, Université Catholique de Louvain, Bruxelles, Belgium.
pubmed:publicationType
Journal Article