Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1 Pt 1
pubmed:dateCreated
1990-8-23
pubmed:abstractText
The elastic filament was studied in chemically skinned fibers from rabbit psoas muscle by electron microscopy and resting tension measurements. Extraction of skinned fibers with 40 mM sodium pyrophosphate caused a selective removal of about two-thirds of the thick filaments and formed a gap between the remaining portion of the A band and the I band. Very thin filaments were seen in the gap and were decorated by anti-titin antibody. The resting tension of these fibers was comparable to that of unextracted control fibers. When the M band was completely extracted by a solution containing 0.6 M NaCl, the resting tension completely disappeared at sarcomere lengths from 2.8 to approximately 3.4 microns. These results suggest that the elastic force of short sarcomeres is endowed in the titin filaments and that these filaments are anchored to some structures of the Z and M lines. Other filaments were found in the gap between the two I bands of NaCl-extracted sarcomeres. These filaments differed from titin filaments by a larger diameter and the anchoring points. They may represent the sarcomeric structures responsible for the resting tension of extracted fibers stretched at sarcomere lengths longer than 3.4 microns.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0002-9513
pubmed:author
pubmed:issnType
Print
pubmed:volume
259
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
C144-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Morphological and functional characterization of the endosarcomeric elastic filament.
pubmed:affiliation
Consiglio Nazionale delle Ricerche Centro di Studio per la Biologia e la Fisiopatologia Muscolare, Università di Padova, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't