Linked Life Data

15389724

Source:http://linkedlifedata.com/resource/pubmed/id/15389724

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2004-10-25
pubmed:abstractText
In the Large(myd) mouse, dystroglycan is incompletely glycosylated and thus cannot bind its extracellular ligands, causing a muscular dystrophy that is usually lethal in early adulthood. We show that the Large(myd) mutation alters the composition and organization of the sarcolemma of fast-twitch skeletal muscle fibers in young adult mice. Costameres at the sarcolemma of the tibialis anterior muscle of Large(myd) mice contain reduced levels of several membrane cytoskeletal proteins, including dystrophin and beta-spectrin. In the quadriceps, longitudinally oriented costameric structures tend to become thickened and branched. More strikingly, proteins of the dystrophin complex present between costameres in controls are absent from Large(myd) muscles. We propose that the absence of the dystrophin complex from these regions destabilizes the sarcolemma of the Large(myd) mouse and thereby contributes to the severity of its muscular dystrophy. Thus, the positioning of sarcolemmal proteins may have a profound effect on the health of skeletal muscle.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0148-639X
pubmed:author
pubmed:issnType
Print
pubmed:volume
30
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
585-95
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
The sarcolemma in the Large(myd) mouse.
pubmed:affiliation
Department of Physiology, University of Maryland School of Medicine, 660 West Redwood Street, Baltimore, Maryland 21201, USA.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't