Linked Life Data

10219627

Source:http://linkedlifedata.com/resource/pubmed/id/10219627

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1999-7-21
pubmed:abstractText
Myofibrillar ATPase (mATPase), succinate dehydrogenase (SDH) and alpha-glycerophosphate dehydrogenase (GPD) activities and cross-sectional area (CSA) were measured in fibres of rat medial gastrocnemius muscle using quantitative histochemistry. The same fibres were typed immunohistochemically using monoclonal antibodies specific to selected myosin heavy chain (MHC) isoforms. The values of mATPase, SDH, GPD and CSA formed a continuum, but significant differences in mean values were observed among fibre types of presumed homogeneous MHC content. Type I fibres had the lowest mATPase activity, followed in rank order by type IIA < type IID/X < type IIB. Type IIA fibres had the highest SDH activity, followed in rank order by type IID/X > type I > type IIB. The mean GPD activity was consistently ranked according to fibre type such that type IIB > type IID/X > type IIA > type I. Type IIA fibres were the smallest, type IIB fibres were the largest and types I and IID/X were of intermediate size. Significant interrelationships between mATPase, SDH, GPD and CSA values were found on a fibre-to-fibre basis. Consequently, discrimination of fibres according to their MHC content was possible on the basis of their mATPase, SDH, GPD and CSA profiles. These intrafibre interrelationships suggest that the MHC isoform is associated with phenotypic differences in contractile, metabolic and size properties of muscle fibre types.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0948-6143
pubmed:author
pubmed:issnType
Print
pubmed:volume
111
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
277-87
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Interrelationships of myofibrillar ATPase activity and metabolic properties of myosin heavy chain-based fibre types in rat skeletal muscle.
pubmed:affiliation
Department of Comparative and Pathological Anatomy, Faculty of Veterinary Science, University of Cordoba, Spain.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't