Linked Life Data

8852373

Source:http://linkedlifedata.com/resource/pubmed/id/8852373

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1996-12-6
pubmed:abstractText
The expression of drebrin A was induced in mouse fibroblasts (L cells) after transformation of cells with a vector that carried cDNA for rat drebrin A (developmentally regulated brain protein A) under the control of the promoter of the gene for metallothionein-I. When drebrin was expressed in the transformed cells (MTI-5 cells), the organization of actin filaments changed such that stress fibers were converted to a mesh-like structure. After subsequent treatment with 5 micrograms/ml cytochalasin D (a reagent that depolymerizes actin filaments), MTI-5 cells maintained their shape, while cells of a drebrin-negative cell line, MTI-11, formed retraction processes. Simultaneously, actin filaments changed into patchy dot-like aggregates in the cytoplasm of both MTI-5 and MTI-11 cells. These aggregates are known as cytoplasmic pools. In MTI-5 cells, adhesion plaques that were resistant to treatment with cytochalasin D appeared upon expression of drebrin. These adhesion plaques were immunostained with vinculin-specific antibodies, while those in MTI-11 cells were hardly immunostained. The amount of vinculin in MTI-5 cells increased in parallel with increase in the level of drebrin. These results suggest that expression of drebrin A induces changes in the assembly of actin filaments and adhesion plaques, with resultant modulation of cellular adhesion to the substratum.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0165-3806
pubmed:author
pubmed:issnType
Print
pubmed:day
26
pubmed:volume
91
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
227-36
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Stabilization of adhesion plaques by the expression of drebrin A in fibroblasts.
pubmed:affiliation
Department of Physiology, Keio University, Tokyo, Japan.
pubmed:publicationType
Journal Article