Linked Life Data

2664503

Source:http://linkedlifedata.com/resource/pubmed/id/2664503

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1989-8-25
pubmed:abstractText
Muscle biopsies from 20 cases of spinal muscular atrophy (SMA), mostly diagnosed as Werdnig-Hoffmann (W-H) disease, were examined for myosin heavy chain (HC) composition. The fetal, fast, and slow heavy chains were characterized in the isolated muscle myosin, and in myosin of single, chemically skinned fibers, by electrophoresis in SDS-6% polyacrylamide gels and by immunoblot techniques, using specific antibodies directed to each main type of myosin HC. The fiber distribution of myosin HC isozymes was further investigated on muscle cryostat sections by an indirect immunofluorescent technique. Fetal myosin HC was found to be expressed in a subpopulation of severely atrophic fibers, alone or together with the slow form of myosin HC. Triangulated fibers of intermediate size contained fetal and fast myosin or fast myosin alone. The hypertrophic fibers were characterized by the predominant expression of slow myosin HC; but in some of these fibers, also low amounts of HC fetal were found to be expressed. These findings are discussed in relation to developmental transitions of myosin heavy chains in human muscle.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0148-639X
pubmed:author
pubmed:issnType
Print
pubmed:volume
12
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
43-51
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Myosin heavy chain composition of muscle fibers in spinal muscular atrophy.
pubmed:affiliation
National Research Council Unit for Muscle Biology and Physiopathology, University of Padova, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't