Linked Life Data

11557573

Source:http://linkedlifedata.com/resource/pubmed/id/11557573

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2001-9-14
pubmed:abstractText
Titin, the third myofilament type of cardiac muscle, contains a molecular spring segment that gives rise to passive forces in stretched myocardium and to restoring forces in shortened myocardium. We studied cardiac titin isoforms (N2B and N2BA) that contain length variants of the molecular spring segment. We investigated how coexpression of isoforms takes place at the level of the half-sarcomere, and whether coexpression affects the extensibility of the isoforms. Immunoelectron microscopy was used to study local coexpression of isoforms in a range of species. It was found that the cardiac sarcomere of large mammals coexpresses N2B and N2BA titin isoforms at the level of the half-sarcomere, and that when coexpressed, the isoforms act independently of one another. Coexpressing isoforms at varying ratios results in modulation of the passive mechanical behavior of the sarcomere without impacting other functions of titin and allows for adjustment of the diastolic properties of the myocardium.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0363-6135
pubmed:author
pubmed:issnType
Print
pubmed:volume
281
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
H1793-9
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Cardiac titin isoforms are coexpressed in the half-sarcomere and extend independently.
pubmed:affiliation
Veterinary and Comparative Anatomy, Pharmacology and Physiology, Washington State University, Pullman, Washington 99164-6520, USA.
pubmed:publicationType
Journal Article, In Vitro, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't