Evolution of myosin filament arrangements in vertebrate skeletal muscle.
Identifieur interne : 000875 ( Ncbi/Merge ); précédent : 000874; suivant : 000876Evolution of myosin filament arrangements in vertebrate skeletal muscle.
Auteurs : P K Luther [Royaume-Uni] ; J M Squire ; P L ForeySource :
- Journal of morphology [ 0362-2525 ] ; 1996.
English descriptors
- KwdEn :
- MESH :
- chemical , ultrastructure : Myosins.
- anatomy & histology : Vertebrates.
- ultrastructure : Muscle, Skeletal.
- Animals, Biological Evolution, Microscopy, Electron.
Abstract
A survey of skeletal muscles throughout craniates shows basic kinds of myosin filament arrangement, simple-lattice and superlattice, within the A-band of each sarcomere. Distribution of simple- and superlattice arrangements across a phylogeny of craniates suggests that the superlattice arrangement is primitive and that Amia and teleosts are derived in showing simple-lattice arrangements. Two taxa examined (Scyliorhinus and Acipenser) show both lattice types within the same organism implying that there is not a simple evolutionary transformation of one to the other fiber arrangement. We discuss the possible functional significance of the different lattice types. We believe that the crossbridges may have greater competition for actin binding sites in simple-lattice muscles compared to the superlattice types.
DOI: 10.1002/(SICI)1097-4687(199609)229:3<325::AID-JMOR7>3.0.CO;2-X
PubMed: 8765810
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Distribution of simple- and superlattice arrangements across a phylogeny of craniates suggests that the superlattice arrangement is primitive and that Amia and teleosts are derived in showing simple-lattice arrangements. Two taxa examined (Scyliorhinus and Acipenser) show both lattice types within the same organism implying that there is not a simple evolutionary transformation of one to the other fiber arrangement. We discuss the possible functional significance of the different lattice types. We believe that the crossbridges may have greater competition for actin binding sites in simple-lattice muscles compared to the superlattice types.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">8765810</PMID><DateCreated><Year>1996</Year><Month>09</Month><Day>13</Day></DateCreated><DateCompleted><Year>1996</Year><Month>09</Month><Day>13</Day></DateCompleted><DateRevised><Year>2010</Year><Month>11</Month><Day>18</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0362-2525</ISSN><JournalIssue CitedMedium="Print"><Volume>229</Volume><Issue>3</Issue><PubDate><Year>1996</Year><Month>Sep</Month></PubDate></JournalIssue><Title>Journal of morphology</Title><ISOAbbreviation>J. Morphol.</ISOAbbreviation></Journal><ArticleTitle>Evolution of myosin filament arrangements in vertebrate skeletal muscle.</ArticleTitle><Pagination><MedlinePgn>325-35</MedlinePgn></Pagination><Abstract><AbstractText>A survey of skeletal muscles throughout craniates shows basic kinds of myosin filament arrangement, simple-lattice and superlattice, within the A-band of each sarcomere. Distribution of simple- and superlattice arrangements across a phylogeny of craniates suggests that the superlattice arrangement is primitive and that Amia and teleosts are derived in showing simple-lattice arrangements. Two taxa examined (Scyliorhinus and Acipenser) show both lattice types within the same organism implying that there is not a simple evolutionary transformation of one to the other fiber arrangement. We discuss the possible functional significance of the different lattice types. 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