Linked Life Data

9486859

Source:http://linkedlifedata.com/resource/pubmed/id/9486859

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1998-3-13
pubmed:abstractText
To discriminate between the influences of a motoneuron and muscle activity on the conformation of actin filaments, the extrinsic polarized fluorescence [of rhodamine-phalloidin and N-(iodoacetylamine)-1-naphthylamine-5-sulfonic acid attached to F-actin] was measured in "ghost" fibers from intact rat soleus muscles and atrophying muscles after denervation, immobilization, or tenotomy. The results show that the conformation of F-actin changed in all the atrophying muscles, but differently. In the denervated muscle, the flexibility of the actin filaments decreased, whereas in the other experimental muscles it remained as in the intact muscle. In the denervated muscle, the mobility of the C-terminus of the actin polypeptide increased. Attachment of myosin subfragment-1 influenced the F-actin conformation differently in the denervated muscle than in the other muscles studied. These results suggest that changes in the conformation of the actin filament are induced by the lack of connection with the motoneuron rather than by muscle inactivity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0148-639X
pubmed:author
pubmed:issnType
Print
pubmed:volume
21
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
309-17
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Effects of denervation and muscle inactivity on the organization of F-actin.
pubmed:affiliation
Department of Cell Biochemistry, Nencki Institute of Experimental Biology, Warsaw, Poland.
pubmed:publicationType
Journal Article