Linked Life Data

7053377

Source:http://linkedlifedata.com/resource/pubmed/id/7053377

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1982-2-25
pubmed:abstractText
Villin, a 95,000-dalton protein, is a major component of microvillus cores isolated from intestinal brush borders. In this study, we compared the Ca2+-dependent action of this protein on actin filaments with that of cytochalasin B, a fungal metabolite that binds to the "barbed" end of actin filaments and nuclei. We found that substoichiometric levels of villin inhibit actin filament elongation and self-association in a cytochalasin-like manner. In addition, the protein releases membrane-bound F-actin in the absence of high shear force, probably by severing the filaments. The filament fragments formed in the presence of villin, as well as a nucleating complex consisting of villin and actin, bind stoichiometric amounts of [3H]cytochalasin B with high affinity. The results of this study indicate that both villin and cytochalasin B bind to the same end of actin filaments, yet differ in their binding sites.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
257
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
395-9
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
Interaction of cytochalasin B with actin filaments nucleated or fragmented by villin.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't