Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1995-1-20
pubmed:abstractText
Skeletal muscles of different mammalian species contain four major myosin heavy-chain (MHC) isoforms: the "slow" or beta-MHC and the three "fast" IIa-, IIx-, and IIb-MHCs; and three major myosin light-chain (MLC) isoforms, the "slow" MLC1s and the two "fast" MLC1f and MLC3f. The differential distribution of the MHCs defines four major fiber types containing a single MHC isoform and a number of intermediate hybrid fiber populations containing both beta/slow- and IIa-MHC, IIa- and IIx-MHC, or IIx- and IIb-MHC. The IIa-, IIx-, and IIb-MHCs were first detected in neonatal muscles, and their expression in developing and adult muscle is regulated by neural, hormonal, and mechanical factors. The transcriptional mechanisms responsible for the fiber type-specific regulation of MHC and MLC gene expression are not known and are presently being explored by in vivo transfection experiments. The functional role of MHC isoforms has been in part clarified by correlated biochemical-physiological studies on single skinned fibers: these studies, in agreement with results from in vitro motility assays, indicate that both MHC and MLC isoforms determine the maximum velocity of shortening of skeletal muscle fibers.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
8750-7587
pubmed:author
pubmed:issnType
Print
pubmed:volume
77
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
493-501
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Myosin isoforms in mammalian skeletal muscle.
pubmed:affiliation
Department of Biomedical Sciences, University of Padova, Italy.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't